Burazer, Lidija

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Authority KeyName Variants
orcid::0000-0001-8955-4496
  • Burazer, Lidija (56)
Projects
Molecular properties and modifications of some respiratory and nutritional allergens Ispitivanje strukture i funkcije biološki važnih makromolekula u fiziološkim i patološkim stanjima
Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research Allergens, antibodies, enzymes and small physiologically important molecules: design, structure, function and relevance
Belgian Special Research Fund BOF StG [01N01718] FoodEnTwin-Twinning of research activities for the frontier research in the fields of food, nutrition and environmental omics
Clinical-epidemiological research of diseases of public health importance in Serbia King Gustaf V's 80-year Foundation
Swedish Asthma and Allergy Association's Research Foundation Swedish Cancer and Allergy Foundation
Swedish Heart-Lung FoundationSwedish Heart-Lung Foundation Swedish Research CouncilSwedish Research Council
COSTEuropean Cooperation in Science and Technology (COST) [928] Hesselman Foundation
Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200168 (University of Belgrade, Faculty of Chemistry) Karolinska InstitutetKarolinska Institutet
Konsul Th C Bergh Foundation Konsul Th C Berg's Foundation
Lars Hierta Memorial Foundation Magnus Bergvall Foundation
Serbian Academy of Sciences and Arts GA [F-26] Stockholm County Council (ALF project)Stockholm County Council
Stockholm County Council (ALF Project)Stockholm County Council

Author's Bibliography

Impact of Tree Pollen Distribution on Allergic Diseases in Serbia: Evidence of Implementation of Allergen Immunotherapy to Betula verrucosa

Minić, Rajna; Josipović, Mirjana; Tomić-Spirić, Vesna; Gavrović-Jankulović, Marija; Perić-Popadić, Aleksandra; Prokopijević, Ivana; Ljubičić, Ana; Stamenković, Danijela; Burazer, Lidija

(MDPI, Basel, 2020)

TY  - JOUR
AU  - Minić, Rajna
AU  - Josipović, Mirjana
AU  - Tomić-Spirić, Vesna
AU  - Gavrović-Jankulović, Marija
AU  - Perić-Popadić, Aleksandra
AU  - Prokopijević, Ivana
AU  - Ljubičić, Ana
AU  - Stamenković, Danijela
AU  - Burazer, Lidija
PY  - 2020
UR  - http://intor.torlakinstitut.com/handle/123456789/565
AB  - Background and objectives: The relationship between air pollen quantity and the sensitization of allergic patients is crucial for both the diagnosis and treatment of allergic diseases. Weather conditions influence the distribution of allergenic pollen and increases in pollen concentration may negatively affect the health of allergic patients. The aim of this study was to analyze the implementation of allergen immunotherapy with regard to air pollen concentration. Material and Methods: Here we examined the relationship between Betula air pollen concentration and the usage of Betula verrucosa allergen immunotherapy in Serbia. Examination covered the period from 2015 to 2018. Measurement of airborne pollen concentration was performed with Lanzoni volumetric pollen traps. The evidence of the usage of sublingual allergen immunotherapy (SLIT) was gathered from patients with documented sensitization to specific pollen. Results: During this period tree pollens were represented with 58% +/- 21% of all measured air pollen species, while Betula pollen represented 15% +/- 8% of all tree pollens. Betula pollination peaked in April. Allergen immunotherapy to Betula verrucosa in Serbia is entirely conducted as sublingual immunotherapy and represents 47.1% +/- 1.4% of issued tree pollen SLIT. The use of pollen SLIT increased by 68% from 2015 to 2018, with an even greater increase in usage recorded for Betula SLIT-80%. Conclusions: This analysis shows a clear causative relationship between pollination and the type/prevalence of applied allergen immunotherapy. Information about the flowering seasons of allergenic plants is very important for people who suffer from allergy, for clinical allergologists, as well as for governing authorities. The presented data is of practical importance to the proper timing of immunotherapy initiation and of importance for urban landscaping. The obtained data can be the starting point for the instatement of a thorough epidemiological study and the inclusion of Serbia on the pollen map of Europe.
PB  - MDPI, Basel
T2  - Medicina-Lithuania
T1  - Impact of Tree Pollen Distribution on Allergic Diseases in Serbia: Evidence of Implementation of Allergen Immunotherapy to Betula verrucosa
IS  - 2
VL  - 56
DO  - 10.3390/medicina56020059
UR  - conv_471
ER  - 
@article{
author = "Minić, Rajna and Josipović, Mirjana and Tomić-Spirić, Vesna and Gavrović-Jankulović, Marija and Perić-Popadić, Aleksandra and Prokopijević, Ivana and Ljubičić, Ana and Stamenković, Danijela and Burazer, Lidija",
year = "2020",
abstract = "Background and objectives: The relationship between air pollen quantity and the sensitization of allergic patients is crucial for both the diagnosis and treatment of allergic diseases. Weather conditions influence the distribution of allergenic pollen and increases in pollen concentration may negatively affect the health of allergic patients. The aim of this study was to analyze the implementation of allergen immunotherapy with regard to air pollen concentration. Material and Methods: Here we examined the relationship between Betula air pollen concentration and the usage of Betula verrucosa allergen immunotherapy in Serbia. Examination covered the period from 2015 to 2018. Measurement of airborne pollen concentration was performed with Lanzoni volumetric pollen traps. The evidence of the usage of sublingual allergen immunotherapy (SLIT) was gathered from patients with documented sensitization to specific pollen. Results: During this period tree pollens were represented with 58% +/- 21% of all measured air pollen species, while Betula pollen represented 15% +/- 8% of all tree pollens. Betula pollination peaked in April. Allergen immunotherapy to Betula verrucosa in Serbia is entirely conducted as sublingual immunotherapy and represents 47.1% +/- 1.4% of issued tree pollen SLIT. The use of pollen SLIT increased by 68% from 2015 to 2018, with an even greater increase in usage recorded for Betula SLIT-80%. Conclusions: This analysis shows a clear causative relationship between pollination and the type/prevalence of applied allergen immunotherapy. Information about the flowering seasons of allergenic plants is very important for people who suffer from allergy, for clinical allergologists, as well as for governing authorities. The presented data is of practical importance to the proper timing of immunotherapy initiation and of importance for urban landscaping. The obtained data can be the starting point for the instatement of a thorough epidemiological study and the inclusion of Serbia on the pollen map of Europe.",
publisher = "MDPI, Basel",
journal = "Medicina-Lithuania",
title = "Impact of Tree Pollen Distribution on Allergic Diseases in Serbia: Evidence of Implementation of Allergen Immunotherapy to Betula verrucosa",
number = "2",
volume = "56",
doi = "10.3390/medicina56020059",
url = "conv_471"
}
Minić, R., Josipović, M., Tomić-Spirić, V., Gavrović-Jankulović, M., Perić-Popadić, A., Prokopijević, I., Ljubičić, A., Stamenković, D.,& Burazer, L.. (2020). Impact of Tree Pollen Distribution on Allergic Diseases in Serbia: Evidence of Implementation of Allergen Immunotherapy to Betula verrucosa. in Medicina-Lithuania
MDPI, Basel., 56(2).
https://doi.org/10.3390/medicina56020059
conv_471
Minić R, Josipović M, Tomić-Spirić V, Gavrović-Jankulović M, Perić-Popadić A, Prokopijević I, Ljubičić A, Stamenković D, Burazer L. Impact of Tree Pollen Distribution on Allergic Diseases in Serbia: Evidence of Implementation of Allergen Immunotherapy to Betula verrucosa. in Medicina-Lithuania. 2020;56(2).
doi:10.3390/medicina56020059
conv_471 .
Minić, Rajna, Josipović, Mirjana, Tomić-Spirić, Vesna, Gavrović-Jankulović, Marija, Perić-Popadić, Aleksandra, Prokopijević, Ivana, Ljubičić, Ana, Stamenković, Danijela, Burazer, Lidija, "Impact of Tree Pollen Distribution on Allergic Diseases in Serbia: Evidence of Implementation of Allergen Immunotherapy to Betula verrucosa" in Medicina-Lithuania, 56, no. 2 (2020),
https://doi.org/10.3390/medicina56020059 .,
conv_471 .
1
1
1
1

Digestomics of Cow's Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation

Radosavljević, Jelena; Apostolović, Danijela; Mihailović, Jelena; Atanasković-Marković, Marina; Burazer, Lidija; van Hage, Marianne; Ćirković-Veličković, Tanja

(MDPI, Basel, 2020)

TY  - JOUR
AU  - Radosavljević, Jelena
AU  - Apostolović, Danijela
AU  - Mihailović, Jelena
AU  - Atanasković-Marković, Marina
AU  - Burazer, Lidija
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2020
UR  - http://intor.torlakinstitut.com/handle/123456789/547
AB  - The aim of this study was to identify short digestion-resistant peptides (SDRPs) released by pepsin digestion of the whole cow's milk and examine their IgE reactivity and allergenicity. Raw milk was subjected to simulated gastric digestion. SDRPs were fractionated from the digests and identified by MS. Milk SDRPs were evaluated for aggregability, propensity to compete for IgE binding with individual milk allergens, and ability to bind IgG4 from allergic and milk-tolerant individuals. The majority of milk SDRPs originated from caseins (97% of peptides) and overlapped with the known IgE epitopes of cow's milk allergens. SDRPs competed with milk proteins for binding to human IgE and readily formed aggregates. The average peptide length was 10.6 +/- 3.5 amino acids. The ability to provoke allergenic in vivo responses was confirmed by skin-prick testing (SPT) in five milk-allergic subjects. This was attributed to the peptide ability to aggregate into non-covalent complexes. SDRPs are able to induce response in SPT, but only in 50% of the sera SDRPs were able to inhibit IgG4 binding to caseins. Hence, SDRPs corresponding to the mainly continuous epitopes of milk proteins induce allergenic in vivo responses in milk-allergic subjects due to aggregation.
PB  - MDPI, Basel
T2  - Foods
T1  - Digestomics of Cow's Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation
IS  - 11
VL  - 9
DO  - 10.3390/foods9111576
UR  - conv_485
ER  - 
@article{
author = "Radosavljević, Jelena and Apostolović, Danijela and Mihailović, Jelena and Atanasković-Marković, Marina and Burazer, Lidija and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2020",
abstract = "The aim of this study was to identify short digestion-resistant peptides (SDRPs) released by pepsin digestion of the whole cow's milk and examine their IgE reactivity and allergenicity. Raw milk was subjected to simulated gastric digestion. SDRPs were fractionated from the digests and identified by MS. Milk SDRPs were evaluated for aggregability, propensity to compete for IgE binding with individual milk allergens, and ability to bind IgG4 from allergic and milk-tolerant individuals. The majority of milk SDRPs originated from caseins (97% of peptides) and overlapped with the known IgE epitopes of cow's milk allergens. SDRPs competed with milk proteins for binding to human IgE and readily formed aggregates. The average peptide length was 10.6 +/- 3.5 amino acids. The ability to provoke allergenic in vivo responses was confirmed by skin-prick testing (SPT) in five milk-allergic subjects. This was attributed to the peptide ability to aggregate into non-covalent complexes. SDRPs are able to induce response in SPT, but only in 50% of the sera SDRPs were able to inhibit IgG4 binding to caseins. Hence, SDRPs corresponding to the mainly continuous epitopes of milk proteins induce allergenic in vivo responses in milk-allergic subjects due to aggregation.",
publisher = "MDPI, Basel",
journal = "Foods",
title = "Digestomics of Cow's Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation",
number = "11",
volume = "9",
doi = "10.3390/foods9111576",
url = "conv_485"
}
Radosavljević, J., Apostolović, D., Mihailović, J., Atanasković-Marković, M., Burazer, L., van Hage, M.,& Ćirković-Veličković, T.. (2020). Digestomics of Cow's Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation. in Foods
MDPI, Basel., 9(11).
https://doi.org/10.3390/foods9111576
conv_485
Radosavljević J, Apostolović D, Mihailović J, Atanasković-Marković M, Burazer L, van Hage M, Ćirković-Veličković T. Digestomics of Cow's Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation. in Foods. 2020;9(11).
doi:10.3390/foods9111576
conv_485 .
Radosavljević, Jelena, Apostolović, Danijela, Mihailović, Jelena, Atanasković-Marković, Marina, Burazer, Lidija, van Hage, Marianne, Ćirković-Veličković, Tanja, "Digestomics of Cow's Milk: Short Digestion-Resistant Peptides of Casein Form Functional Complexes by Aggregation" in Foods, 9, no. 11 (2020),
https://doi.org/10.3390/foods9111576 .,
conv_485 .
7
4

Tropomyosin sensitization as a link between shellfish anaphylaxis and asthma reactivation

Blagojević, Gordan; Burazer, Lidija; Prokopijević, Ivana

(Wiley, Hoboken, 2020)

TY  - CONF
AU  - Blagojević, Gordan
AU  - Burazer, Lidija
AU  - Prokopijević, Ivana
PY  - 2020
UR  - http://intor.torlakinstitut.com/handle/123456789/544
PB  - Wiley, Hoboken
C3  - Allergy
T1  - Tropomyosin sensitization as a link between shellfish anaphylaxis and asthma reactivation
EP  - 544
SP  - 543
VL  - 75
UR  - conv_481
ER  - 
@conference{
author = "Blagojević, Gordan and Burazer, Lidija and Prokopijević, Ivana",
year = "2020",
publisher = "Wiley, Hoboken",
journal = "Allergy",
title = "Tropomyosin sensitization as a link between shellfish anaphylaxis and asthma reactivation",
pages = "544-543",
volume = "75",
url = "conv_481"
}
Blagojević, G., Burazer, L.,& Prokopijević, I.. (2020). Tropomyosin sensitization as a link between shellfish anaphylaxis and asthma reactivation. in Allergy
Wiley, Hoboken., 75, 543-544.
conv_481
Blagojević G, Burazer L, Prokopijević I. Tropomyosin sensitization as a link between shellfish anaphylaxis and asthma reactivation. in Allergy. 2020;75:543-544.
conv_481 .
Blagojević, Gordan, Burazer, Lidija, Prokopijević, Ivana, "Tropomyosin sensitization as a link between shellfish anaphylaxis and asthma reactivation" in Allergy, 75 (2020):543-544,
conv_481 .

In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress

Smiljanić, Katarina; Prodić, Ivana; Apostolović, Danijela; Cvetković, Anka; Veljović, Đorđe; Mutić, Jelena; van Hage, Marianne; Burazer, Lidija; Ćirković-Veličković, Tanja

(Pergamon-Elsevier Science Ltd, Oxford, 2019)

TY  - JOUR
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Cvetković, Anka
AU  - Veljović, Đorđe
AU  - Mutić, Jelena
AU  - van Hage, Marianne
AU  - Burazer, Lidija
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://intor.torlakinstitut.com/handle/123456789/536
AB  - An association between pollution (e.g., from traffic emissions) and the increased prevalence of respiratory allergies has been observed. Field-realistic exposure studies provide the most relevant assessment of the effects of the intensity and diversity of urban and industrial contamination on pollen structure and allergenicity. The significance of in-depth post-translational modification (PTM) studies of pollen proteomes, when compared with studies on other aspects of pollution and altered pollen allergenicity, has not yet been determined; hence, little progress has been made within this field. We undertook a comprehensive comparative analysis of multiple polluted and environmentally preserved Phleum pratense (Timothy grass) pollen samples using scanning electron microscopy, in-depth PTM profiling, determination of organic and inorganic pollutants, analysis of the release of sub-pollen particles and phenols/proteins, and analysis of proteome expression using high resolution tandem mass spectrometry. In addition, we used quantitative enzyme-linked immunosorbent assays (ELISA) and immunoglobulin E (IgE) immunoblotting. An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, including a significantly higher content of mercury, cadmium, and manganese, with irregular long spines on pollen grain surface structures. Antioxidative defense-related enzymes were significantly upregulated and seven oxidative PTMs were significantly increased (methionine, histidine, lysine, and proline oxidation; tyrosine glycosylation, lysine 4-hydroxy-2-nonenal adduct, and lysine carbamylation) in pollen exposed to the chemical plant and road traffic pollution sources. Oxidative modifications affected several Timothy pollen allergens; Phl p 6, in particular, exhibited several different oxidative modifications. The expression of Phl p 6, 12, and 13 allergens were downregulated in polluted pollen, and IgE binding to pollen extract was substantially lower in the 18 patients studied, as measured by quantitative ELISA. Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach pointed to modification of Timothy pollen allergens and suggested that heavy metals are primarily responsible for oxidative stress effects observed in pollen proteins.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Environment International
T1  - In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress
EP  - 658
SP  - 644
VL  - 126
DO  - 10.1016/j.envint.2019.03.001
UR  - conv_451
ER  - 
@article{
author = "Smiljanić, Katarina and Prodić, Ivana and Apostolović, Danijela and Cvetković, Anka and Veljović, Đorđe and Mutić, Jelena and van Hage, Marianne and Burazer, Lidija and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "An association between pollution (e.g., from traffic emissions) and the increased prevalence of respiratory allergies has been observed. Field-realistic exposure studies provide the most relevant assessment of the effects of the intensity and diversity of urban and industrial contamination on pollen structure and allergenicity. The significance of in-depth post-translational modification (PTM) studies of pollen proteomes, when compared with studies on other aspects of pollution and altered pollen allergenicity, has not yet been determined; hence, little progress has been made within this field. We undertook a comprehensive comparative analysis of multiple polluted and environmentally preserved Phleum pratense (Timothy grass) pollen samples using scanning electron microscopy, in-depth PTM profiling, determination of organic and inorganic pollutants, analysis of the release of sub-pollen particles and phenols/proteins, and analysis of proteome expression using high resolution tandem mass spectrometry. In addition, we used quantitative enzyme-linked immunosorbent assays (ELISA) and immunoglobulin E (IgE) immunoblotting. An increased phenolic content and release of sub-pollen particles was found in pollen samples from the polluted area, including a significantly higher content of mercury, cadmium, and manganese, with irregular long spines on pollen grain surface structures. Antioxidative defense-related enzymes were significantly upregulated and seven oxidative PTMs were significantly increased (methionine, histidine, lysine, and proline oxidation; tyrosine glycosylation, lysine 4-hydroxy-2-nonenal adduct, and lysine carbamylation) in pollen exposed to the chemical plant and road traffic pollution sources. Oxidative modifications affected several Timothy pollen allergens; Phl p 6, in particular, exhibited several different oxidative modifications. The expression of Phl p 6, 12, and 13 allergens were downregulated in polluted pollen, and IgE binding to pollen extract was substantially lower in the 18 patients studied, as measured by quantitative ELISA. Quantitative, unrestricted, and detailed PTM searches using an enrichment-free approach pointed to modification of Timothy pollen allergens and suggested that heavy metals are primarily responsible for oxidative stress effects observed in pollen proteins.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Environment International",
title = "In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress",
pages = "658-644",
volume = "126",
doi = "10.1016/j.envint.2019.03.001",
url = "conv_451"
}
Smiljanić, K., Prodić, I., Apostolović, D., Cvetković, A., Veljović, Đ., Mutić, J., van Hage, M., Burazer, L.,& Ćirković-Veličković, T.. (2019). In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress. in Environment International
Pergamon-Elsevier Science Ltd, Oxford., 126, 644-658.
https://doi.org/10.1016/j.envint.2019.03.001
conv_451
Smiljanić K, Prodić I, Apostolović D, Cvetković A, Veljović Đ, Mutić J, van Hage M, Burazer L, Ćirković-Veličković T. In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress. in Environment International. 2019;126:644-658.
doi:10.1016/j.envint.2019.03.001
conv_451 .
Smiljanić, Katarina, Prodić, Ivana, Apostolović, Danijela, Cvetković, Anka, Veljović, Đorđe, Mutić, Jelena, van Hage, Marianne, Burazer, Lidija, Ćirković-Veličković, Tanja, "In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental oxidative stress" in Environment International, 126 (2019):644-658,
https://doi.org/10.1016/j.envint.2019.03.001 .,
conv_451 .
2
6
5
7

In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental pollution and oxidative stress

Smiljanić, Katarina; Prodić, Ivana; Apostolović, Danijela; Cvetković, Anka; Veljović, Đorđe; Mutić, Jelena; van Hage, Marianne; Burazer, Lidija; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2019)

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Cvetković, Anka
AU  - Veljović, Đorđe
AU  - Mutić, Jelena
AU  - van Hage, Marianne
AU  - Burazer, Lidija
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://intor.torlakinstitut.com/handle/123456789/532
PB  - Wiley, Hoboken
C3  - Allergy
T1  - In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental pollution and oxidative stress
EP  - 878
SP  - 878
VL  - 74
UR  - conv_457
ER  - 
@conference{
author = "Smiljanić, Katarina and Prodić, Ivana and Apostolović, Danijela and Cvetković, Anka and Veljović, Đorđe and Mutić, Jelena and van Hage, Marianne and Burazer, Lidija and Ćirković-Veličković, Tanja",
year = "2019",
publisher = "Wiley, Hoboken",
journal = "Allergy",
title = "In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental pollution and oxidative stress",
pages = "878-878",
volume = "74",
url = "conv_457"
}
Smiljanić, K., Prodić, I., Apostolović, D., Cvetković, A., Veljović, Đ., Mutić, J., van Hage, M., Burazer, L.,& Ćirković-Veličković, T.. (2019). In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental pollution and oxidative stress. in Allergy
Wiley, Hoboken., 74, 878-878.
conv_457
Smiljanić K, Prodić I, Apostolović D, Cvetković A, Veljović Đ, Mutić J, van Hage M, Burazer L, Ćirković-Veličković T. In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental pollution and oxidative stress. in Allergy. 2019;74:878-878.
conv_457 .
Smiljanić, Katarina, Prodić, Ivana, Apostolović, Danijela, Cvetković, Anka, Veljović, Đorđe, Mutić, Jelena, van Hage, Marianne, Burazer, Lidija, Ćirković-Veličković, Tanja, "In-depth quantitative profiling of post-translational modifications of Timothy grass pollen allergome in relation to environmental pollution and oxidative stress" in Allergy, 74 (2019):878-878,
conv_457 .

Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides

Prodić, Ivana; Stanić-Vučinić, Dragana; Apostolović, Danijela; Mihailović, Jelena; Radibratović, M.; Radosavljević, Jelena; Burazer, Lidija; Milcić, M.; Smiljanić, Katarina; van Hage, Marianne; Ćirković-Veličković, Tanja

(Blackwell Publishing Ltd, 2018)

TY  - JOUR
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Apostolović, Danijela
AU  - Mihailović, Jelena
AU  - Radibratović, M.
AU  - Radosavljević, Jelena
AU  - Burazer, Lidija
AU  - Milcić, M.
AU  - Smiljanić, Katarina
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://intor.torlakinstitut.com/handle/123456789/608
AB  - Background: Most food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10 kDa) released by gastric digestion under standardized and physiologically relevant in vitro conditions has not been investigated. Objective: The aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. Methods: Two-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. Results: Ara h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical Relevance: Peanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.
PB  - Blackwell Publishing Ltd
T2  - Clinical and Experimental Allergy
T1  - Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides
EP  - 740
IS  - 6
SP  - 731
VL  - 48
DO  - 10.1111/cea.13113
ER  - 
@article{
author = "Prodić, Ivana and Stanić-Vučinić, Dragana and Apostolović, Danijela and Mihailović, Jelena and Radibratović, M. and Radosavljević, Jelena and Burazer, Lidija and Milcić, M. and Smiljanić, Katarina and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "Background: Most food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10 kDa) released by gastric digestion under standardized and physiologically relevant in vitro conditions has not been investigated. Objective: The aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. Methods: Two-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. Results: Ara h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical Relevance: Peanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.",
publisher = "Blackwell Publishing Ltd",
journal = "Clinical and Experimental Allergy",
title = "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides",
pages = "740-731",
number = "6",
volume = "48",
doi = "10.1111/cea.13113"
}
Prodić, I., Stanić-Vučinić, D., Apostolović, D., Mihailović, J., Radibratović, M., Radosavljević, J., Burazer, L., Milcić, M., Smiljanić, K., van Hage, M.,& Ćirković-Veličković, T.. (2018). Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy
Blackwell Publishing Ltd., 48(6), 731-740.
https://doi.org/10.1111/cea.13113
Prodić I, Stanić-Vučinić D, Apostolović D, Mihailović J, Radibratović M, Radosavljević J, Burazer L, Milcić M, Smiljanić K, van Hage M, Ćirković-Veličković T. Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy. 2018;48(6):731-740.
doi:10.1111/cea.13113 .
Prodić, Ivana, Stanić-Vučinić, Dragana, Apostolović, Danijela, Mihailović, Jelena, Radibratović, M., Radosavljević, Jelena, Burazer, Lidija, Milcić, M., Smiljanić, Katarina, van Hage, Marianne, Ćirković-Veličković, Tanja, "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides" in Clinical and Experimental Allergy, 48, no. 6 (2018):731-740,
https://doi.org/10.1111/cea.13113 . .
3
31
24
29

Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides

Prodić, Ivana; Stanić-Vučinić, Dragana; Apostolović, Danijela; Mihailović, Jelena; Radibratović, M.; Radosavljević, Jelena; Burazer, Lidija; Milcić, M.; Smiljanić, Katarina; van Hage, Marianne; Ćirković-Veličković, Tanja

(Blackwell Publishing Ltd, 2018)

TY  - JOUR
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Apostolović, Danijela
AU  - Mihailović, Jelena
AU  - Radibratović, M.
AU  - Radosavljević, Jelena
AU  - Burazer, Lidija
AU  - Milcić, M.
AU  - Smiljanić, Katarina
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://intor.torlakinstitut.com/handle/123456789/514
AB  - Background: Most food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10 kDa) released by gastric digestion under standardized and physiologically relevant in vitro conditions has not been investigated. Objective: The aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. Methods: Two-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. Results: Ara h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical Relevance: Peanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.
PB  - Blackwell Publishing Ltd
T2  - Clinical and Experimental Allergy
T1  - Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides
EP  - 740
IS  - 6
SP  - 731
VL  - 48
DO  - 10.1111/cea.13113
UR  - conv_518
ER  - 
@article{
author = "Prodić, Ivana and Stanić-Vučinić, Dragana and Apostolović, Danijela and Mihailović, Jelena and Radibratović, M. and Radosavljević, Jelena and Burazer, Lidija and Milcić, M. and Smiljanić, Katarina and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "Background: Most food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10 kDa) released by gastric digestion under standardized and physiologically relevant in vitro conditions has not been investigated. Objective: The aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. Methods: Two-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. Results: Ara h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical Relevance: Peanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.",
publisher = "Blackwell Publishing Ltd",
journal = "Clinical and Experimental Allergy",
title = "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides",
pages = "740-731",
number = "6",
volume = "48",
doi = "10.1111/cea.13113",
url = "conv_518"
}
Prodić, I., Stanić-Vučinić, D., Apostolović, D., Mihailović, J., Radibratović, M., Radosavljević, J., Burazer, L., Milcić, M., Smiljanić, K., van Hage, M.,& Ćirković-Veličković, T.. (2018). Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy
Blackwell Publishing Ltd., 48(6), 731-740.
https://doi.org/10.1111/cea.13113
conv_518
Prodić I, Stanić-Vučinić D, Apostolović D, Mihailović J, Radibratović M, Radosavljević J, Burazer L, Milcić M, Smiljanić K, van Hage M, Ćirković-Veličković T. Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy. 2018;48(6):731-740.
doi:10.1111/cea.13113
conv_518 .
Prodić, Ivana, Stanić-Vučinić, Dragana, Apostolović, Danijela, Mihailović, Jelena, Radibratović, M., Radosavljević, Jelena, Burazer, Lidija, Milcić, M., Smiljanić, Katarina, van Hage, Marianne, Ćirković-Veličković, Tanja, "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides" in Clinical and Experimental Allergy, 48, no. 6 (2018):731-740,
https://doi.org/10.1111/cea.13113 .,
conv_518 .
3
31
24
29

Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes

Radosavljević, Jelena; Apostolović, Danijela; Mihailović, Jelena; Atanasković-Marković, Marina; Burazer, Lidija; van Hage, Marianne; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2018)

TY  - CONF
AU  - Radosavljević, Jelena
AU  - Apostolović, Danijela
AU  - Mihailović, Jelena
AU  - Atanasković-Marković, Marina
AU  - Burazer, Lidija
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://intor.torlakinstitut.com/handle/123456789/504
PB  - Wiley, Hoboken
C3  - FEBS Open Bio
T1  - Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes
EP  - 257
SP  - 257
VL  - 8
UR  - conv_436
ER  - 
@conference{
author = "Radosavljević, Jelena and Apostolović, Danijela and Mihailović, Jelena and Atanasković-Marković, Marina and Burazer, Lidija and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2018",
publisher = "Wiley, Hoboken",
journal = "FEBS Open Bio",
title = "Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes",
pages = "257-257",
volume = "8",
url = "conv_436"
}
Radosavljević, J., Apostolović, D., Mihailović, J., Atanasković-Marković, M., Burazer, L., van Hage, M.,& Ćirković-Veličković, T.. (2018). Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes. in FEBS Open Bio
Wiley, Hoboken., 8, 257-257.
conv_436
Radosavljević J, Apostolović D, Mihailović J, Atanasković-Marković M, Burazer L, van Hage M, Ćirković-Veličković T. Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes. in FEBS Open Bio. 2018;8:257-257.
conv_436 .
Radosavljević, Jelena, Apostolović, Danijela, Mihailović, Jelena, Atanasković-Marković, Marina, Burazer, Lidija, van Hage, Marianne, Ćirković-Veličković, Tanja, "Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes" in FEBS Open Bio, 8 (2018):257-257,
conv_436 .

Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study

Smiljanić, Katarina; Apostolović, Danijela; Trifunović, S.; Ognjenović, Jana; Perusko, M.; Mihajlović, Luka; Burazer, Lidija; van Hage, Marianne; Ćirković-Veličković, Tanja

(Blackwell Publishing Ltd, 2017)

TY  - JOUR
AU  - Smiljanić, Katarina
AU  - Apostolović, Danijela
AU  - Trifunović, S.
AU  - Ognjenović, Jana
AU  - Perusko, M.
AU  - Mihajlović, Luka
AU  - Burazer, Lidija
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2017
UR  - http://intor.torlakinstitut.com/handle/123456789/610
AB  - Background: Short ragweed (Ambrosia artemisiifolia) allergies affect more than 36 million people annually. Ragweed pollen grains release subpollen particles (SPP) of respirable size upon hydration or a change in air electrical conditions. The aim of this study was to characterize the proteomes and allergomes of short ragweed SPP and total pollen protein extract (TOT), and compare their effects with those of standard aqueous pollen protein extract (APE) using sera from short ragweed pollen-sensitized patients. Methods: Quantitative 2D gel-based and shotgun proteomics, 1D and 2D immunoblotting, and quantitative ELISA were applied. Novel SPP extraction and preparation protocols enabled appropriate sample preparation and further downstream analysis by quantitative proteomics. Results: The SPP fraction contained the highest proportion (94%) of the allergome, with the largest quantities of the minor Amb a 4 and major Amb a 1 allergens, and as unique, NADH dehydrogenases. APE was the richest in Amb a 6, Amb a 5 and Amb a 3, and TOT fraction was the richest in the Amb a 8 allergens (89% and 83% of allergome, respectively). Allergenic potency correlated well among the three fractions tested, with 1D immunoblots demonstrating a slight predominance of IgE reactivity to SPP compared to TOT and APE. However, the strongest IgE binding in ELISA was noted against APE. New allergenic candidates, phosphoglycerate mutase and phosphoglucomutase, were identified in all the three pollen fractions. Enolase, UTP-glucose-1-phosphate uridylyltransferase and polygalacturonase were observed in SPP and TOT fractions as novel allergens of the short ragweed pollen, as previously described. Conclusion and Clinical Relevance: We demonstrated that the complete major (Amb a 1 and 11) and almost all minor (Amb a 3, 4, 5, 6, 8 and 9) short ragweed pollen allergen repertoire as well as NADH oxidases are present in SPP, highlighting an important role for SPP in allergic sensitization to short ragweed.
PB  - Blackwell Publishing Ltd
T2  - Clinical and Experimental Allergy
T1  - Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study
EP  - 828
IS  - 6
SP  - 815
VL  - 47
DO  - 10.1111/cea.12874
ER  - 
@article{
author = "Smiljanić, Katarina and Apostolović, Danijela and Trifunović, S. and Ognjenović, Jana and Perusko, M. and Mihajlović, Luka and Burazer, Lidija and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2017",
abstract = "Background: Short ragweed (Ambrosia artemisiifolia) allergies affect more than 36 million people annually. Ragweed pollen grains release subpollen particles (SPP) of respirable size upon hydration or a change in air electrical conditions. The aim of this study was to characterize the proteomes and allergomes of short ragweed SPP and total pollen protein extract (TOT), and compare their effects with those of standard aqueous pollen protein extract (APE) using sera from short ragweed pollen-sensitized patients. Methods: Quantitative 2D gel-based and shotgun proteomics, 1D and 2D immunoblotting, and quantitative ELISA were applied. Novel SPP extraction and preparation protocols enabled appropriate sample preparation and further downstream analysis by quantitative proteomics. Results: The SPP fraction contained the highest proportion (94%) of the allergome, with the largest quantities of the minor Amb a 4 and major Amb a 1 allergens, and as unique, NADH dehydrogenases. APE was the richest in Amb a 6, Amb a 5 and Amb a 3, and TOT fraction was the richest in the Amb a 8 allergens (89% and 83% of allergome, respectively). Allergenic potency correlated well among the three fractions tested, with 1D immunoblots demonstrating a slight predominance of IgE reactivity to SPP compared to TOT and APE. However, the strongest IgE binding in ELISA was noted against APE. New allergenic candidates, phosphoglycerate mutase and phosphoglucomutase, were identified in all the three pollen fractions. Enolase, UTP-glucose-1-phosphate uridylyltransferase and polygalacturonase were observed in SPP and TOT fractions as novel allergens of the short ragweed pollen, as previously described. Conclusion and Clinical Relevance: We demonstrated that the complete major (Amb a 1 and 11) and almost all minor (Amb a 3, 4, 5, 6, 8 and 9) short ragweed pollen allergen repertoire as well as NADH oxidases are present in SPP, highlighting an important role for SPP in allergic sensitization to short ragweed.",
publisher = "Blackwell Publishing Ltd",
journal = "Clinical and Experimental Allergy",
title = "Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study",
pages = "828-815",
number = "6",
volume = "47",
doi = "10.1111/cea.12874"
}
Smiljanić, K., Apostolović, D., Trifunović, S., Ognjenović, J., Perusko, M., Mihajlović, L., Burazer, L., van Hage, M.,& Ćirković-Veličković, T.. (2017). Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study. in Clinical and Experimental Allergy
Blackwell Publishing Ltd., 47(6), 815-828.
https://doi.org/10.1111/cea.12874
Smiljanić K, Apostolović D, Trifunović S, Ognjenović J, Perusko M, Mihajlović L, Burazer L, van Hage M, Ćirković-Veličković T. Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study. in Clinical and Experimental Allergy. 2017;47(6):815-828.
doi:10.1111/cea.12874 .
Smiljanić, Katarina, Apostolović, Danijela, Trifunović, S., Ognjenović, Jana, Perusko, M., Mihajlović, Luka, Burazer, Lidija, van Hage, Marianne, Ćirković-Veličković, Tanja, "Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study" in Clinical and Experimental Allergy, 47, no. 6 (2017):815-828,
https://doi.org/10.1111/cea.12874 . .
2
19
15
18

Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study

Smiljanić, Katarina; Apostolović, Danijela; Trifunović, S.; Ognjenović, Jana; Perusko, M.; Mihajlović, Luka; Burazer, Lidija; van Hage, Marianne; Ćirković-Veličković, Tanja

(Blackwell Publishing Ltd, 2017)

TY  - JOUR
AU  - Smiljanić, Katarina
AU  - Apostolović, Danijela
AU  - Trifunović, S.
AU  - Ognjenović, Jana
AU  - Perusko, M.
AU  - Mihajlović, Luka
AU  - Burazer, Lidija
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2017
UR  - http://intor.torlakinstitut.com/handle/123456789/479
AB  - Background: Short ragweed (Ambrosia artemisiifolia) allergies affect more than 36 million people annually. Ragweed pollen grains release subpollen particles (SPP) of respirable size upon hydration or a change in air electrical conditions. The aim of this study was to characterize the proteomes and allergomes of short ragweed SPP and total pollen protein extract (TOT), and compare their effects with those of standard aqueous pollen protein extract (APE) using sera from short ragweed pollen-sensitized patients. Methods: Quantitative 2D gel-based and shotgun proteomics, 1D and 2D immunoblotting, and quantitative ELISA were applied. Novel SPP extraction and preparation protocols enabled appropriate sample preparation and further downstream analysis by quantitative proteomics. Results: The SPP fraction contained the highest proportion (94%) of the allergome, with the largest quantities of the minor Amb a 4 and major Amb a 1 allergens, and as unique, NADH dehydrogenases. APE was the richest in Amb a 6, Amb a 5 and Amb a 3, and TOT fraction was the richest in the Amb a 8 allergens (89% and 83% of allergome, respectively). Allergenic potency correlated well among the three fractions tested, with 1D immunoblots demonstrating a slight predominance of IgE reactivity to SPP compared to TOT and APE. However, the strongest IgE binding in ELISA was noted against APE. New allergenic candidates, phosphoglycerate mutase and phosphoglucomutase, were identified in all the three pollen fractions. Enolase, UTP-glucose-1-phosphate uridylyltransferase and polygalacturonase were observed in SPP and TOT fractions as novel allergens of the short ragweed pollen, as previously described. Conclusion and Clinical Relevance: We demonstrated that the complete major (Amb a 1 and 11) and almost all minor (Amb a 3, 4, 5, 6, 8 and 9) short ragweed pollen allergen repertoire as well as NADH oxidases are present in SPP, highlighting an important role for SPP in allergic sensitization to short ragweed.
PB  - Blackwell Publishing Ltd
T2  - Clinical and Experimental Allergy
T1  - Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study
EP  - 828
IS  - 6
SP  - 815
VL  - 47
DO  - 10.1111/cea.12874
UR  - conv_533
ER  - 
@article{
author = "Smiljanić, Katarina and Apostolović, Danijela and Trifunović, S. and Ognjenović, Jana and Perusko, M. and Mihajlović, Luka and Burazer, Lidija and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2017",
abstract = "Background: Short ragweed (Ambrosia artemisiifolia) allergies affect more than 36 million people annually. Ragweed pollen grains release subpollen particles (SPP) of respirable size upon hydration or a change in air electrical conditions. The aim of this study was to characterize the proteomes and allergomes of short ragweed SPP and total pollen protein extract (TOT), and compare their effects with those of standard aqueous pollen protein extract (APE) using sera from short ragweed pollen-sensitized patients. Methods: Quantitative 2D gel-based and shotgun proteomics, 1D and 2D immunoblotting, and quantitative ELISA were applied. Novel SPP extraction and preparation protocols enabled appropriate sample preparation and further downstream analysis by quantitative proteomics. Results: The SPP fraction contained the highest proportion (94%) of the allergome, with the largest quantities of the minor Amb a 4 and major Amb a 1 allergens, and as unique, NADH dehydrogenases. APE was the richest in Amb a 6, Amb a 5 and Amb a 3, and TOT fraction was the richest in the Amb a 8 allergens (89% and 83% of allergome, respectively). Allergenic potency correlated well among the three fractions tested, with 1D immunoblots demonstrating a slight predominance of IgE reactivity to SPP compared to TOT and APE. However, the strongest IgE binding in ELISA was noted against APE. New allergenic candidates, phosphoglycerate mutase and phosphoglucomutase, were identified in all the three pollen fractions. Enolase, UTP-glucose-1-phosphate uridylyltransferase and polygalacturonase were observed in SPP and TOT fractions as novel allergens of the short ragweed pollen, as previously described. Conclusion and Clinical Relevance: We demonstrated that the complete major (Amb a 1 and 11) and almost all minor (Amb a 3, 4, 5, 6, 8 and 9) short ragweed pollen allergen repertoire as well as NADH oxidases are present in SPP, highlighting an important role for SPP in allergic sensitization to short ragweed.",
publisher = "Blackwell Publishing Ltd",
journal = "Clinical and Experimental Allergy",
title = "Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study",
pages = "828-815",
number = "6",
volume = "47",
doi = "10.1111/cea.12874",
url = "conv_533"
}
Smiljanić, K., Apostolović, D., Trifunović, S., Ognjenović, J., Perusko, M., Mihajlović, L., Burazer, L., van Hage, M.,& Ćirković-Veličković, T.. (2017). Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study. in Clinical and Experimental Allergy
Blackwell Publishing Ltd., 47(6), 815-828.
https://doi.org/10.1111/cea.12874
conv_533
Smiljanić K, Apostolović D, Trifunović S, Ognjenović J, Perusko M, Mihajlović L, Burazer L, van Hage M, Ćirković-Veličković T. Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study. in Clinical and Experimental Allergy. 2017;47(6):815-828.
doi:10.1111/cea.12874
conv_533 .
Smiljanić, Katarina, Apostolović, Danijela, Trifunović, S., Ognjenović, Jana, Perusko, M., Mihajlović, Luka, Burazer, Lidija, van Hage, Marianne, Ćirković-Veličković, Tanja, "Subpollen particles are rich carriers of major short ragweed allergens and NADH dehydrogenases: quantitative proteomic and allergomic study" in Clinical and Experimental Allergy, 47, no. 6 (2017):815-828,
https://doi.org/10.1111/cea.12874 .,
conv_533 .
2
19
15
18

Hypoallergenic acid-sensitive modification preserves major mugwort allergen fold and delivers full repertoire of MHC class II-binding peptides during endolysosomal degradation

Stanić-Vučinić, Dragana; Stojadinović, Marija; Mirkov, Ivana; Apostolović, Danijela; Burazer, Lidija; Atanasković-Marković, Marina; Kataranovski, Milena; Ćirković-Veličković, Tanja

(Royal Soc Chemistry, Cambridge, 2016)

TY  - JOUR
AU  - Stanić-Vučinić, Dragana
AU  - Stojadinović, Marija
AU  - Mirkov, Ivana
AU  - Apostolović, Danijela
AU  - Burazer, Lidija
AU  - Atanasković-Marković, Marina
AU  - Kataranovski, Milena
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - http://intor.torlakinstitut.com/handle/123456789/456
AB  - Modified allergens are a safer and more efficient alternative to natural allergens for specific immunotherapy. As the modification of an allergen can diminish its immunogenicity due to the alteration of T-cell epitopes, in this paper we study the effects of a reversible chemical modification of Art v 1, the main allergen of mugwort pollen, on its allergenicity and immunogenicity. Modification of Art v 1 by cis-aconitylation into a polyanionic derivative (CAA) did not result in any significant structural alteration. However, IgE-binding epitopes on CAA were blocked, resulting in a reduced IgE-binding and basophil activation. Both proteins induced proliferation of CD3(+)CD4(+) T-cells in mugwort-allergic patients, but only unmodified allergens increased IL-4, IL-5 and IL-10 production. Rabbit and mouse anti-CAA antibodies exhibited cross-reactivity with native allergens and blocked human IgE-binding to Art v 1. Degradation of CAA by lysosomal fraction enzymes resulted in a similar set of peptides, harboring MHC class II-binding peptides, as unmodified proteins. Thus, cis-aconitylation modified Art v 1 had a significantly reduced allergenicity, whereas its immunogenicity was completely preserved. Acid-environment-responsive modification, which releases a full repertoire of native allergen epitopes within a particular site, can be considered a smart drug delivery system, which is able to deliver a therapeutically-effective dose in a controlled manner, and minimizes adverse side effects.
PB  - Royal Soc Chemistry, Cambridge
T2  - RSC Advances
T1  - Hypoallergenic acid-sensitive modification preserves major mugwort allergen fold and delivers full repertoire of MHC class II-binding peptides during endolysosomal degradation
EP  - 88228
IS  - 91
SP  - 88216
VL  - 6
DO  - 10.1039/c6ra17261j
UR  - conv_394
ER  - 
@article{
author = "Stanić-Vučinić, Dragana and Stojadinović, Marija and Mirkov, Ivana and Apostolović, Danijela and Burazer, Lidija and Atanasković-Marković, Marina and Kataranovski, Milena and Ćirković-Veličković, Tanja",
year = "2016",
abstract = "Modified allergens are a safer and more efficient alternative to natural allergens for specific immunotherapy. As the modification of an allergen can diminish its immunogenicity due to the alteration of T-cell epitopes, in this paper we study the effects of a reversible chemical modification of Art v 1, the main allergen of mugwort pollen, on its allergenicity and immunogenicity. Modification of Art v 1 by cis-aconitylation into a polyanionic derivative (CAA) did not result in any significant structural alteration. However, IgE-binding epitopes on CAA were blocked, resulting in a reduced IgE-binding and basophil activation. Both proteins induced proliferation of CD3(+)CD4(+) T-cells in mugwort-allergic patients, but only unmodified allergens increased IL-4, IL-5 and IL-10 production. Rabbit and mouse anti-CAA antibodies exhibited cross-reactivity with native allergens and blocked human IgE-binding to Art v 1. Degradation of CAA by lysosomal fraction enzymes resulted in a similar set of peptides, harboring MHC class II-binding peptides, as unmodified proteins. Thus, cis-aconitylation modified Art v 1 had a significantly reduced allergenicity, whereas its immunogenicity was completely preserved. Acid-environment-responsive modification, which releases a full repertoire of native allergen epitopes within a particular site, can be considered a smart drug delivery system, which is able to deliver a therapeutically-effective dose in a controlled manner, and minimizes adverse side effects.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "RSC Advances",
title = "Hypoallergenic acid-sensitive modification preserves major mugwort allergen fold and delivers full repertoire of MHC class II-binding peptides during endolysosomal degradation",
pages = "88228-88216",
number = "91",
volume = "6",
doi = "10.1039/c6ra17261j",
url = "conv_394"
}
Stanić-Vučinić, D., Stojadinović, M., Mirkov, I., Apostolović, D., Burazer, L., Atanasković-Marković, M., Kataranovski, M.,& Ćirković-Veličković, T.. (2016). Hypoallergenic acid-sensitive modification preserves major mugwort allergen fold and delivers full repertoire of MHC class II-binding peptides during endolysosomal degradation. in RSC Advances
Royal Soc Chemistry, Cambridge., 6(91), 88216-88228.
https://doi.org/10.1039/c6ra17261j
conv_394
Stanić-Vučinić D, Stojadinović M, Mirkov I, Apostolović D, Burazer L, Atanasković-Marković M, Kataranovski M, Ćirković-Veličković T. Hypoallergenic acid-sensitive modification preserves major mugwort allergen fold and delivers full repertoire of MHC class II-binding peptides during endolysosomal degradation. in RSC Advances. 2016;6(91):88216-88228.
doi:10.1039/c6ra17261j
conv_394 .
Stanić-Vučinić, Dragana, Stojadinović, Marija, Mirkov, Ivana, Apostolović, Danijela, Burazer, Lidija, Atanasković-Marković, Marina, Kataranovski, Milena, Ćirković-Veličković, Tanja, "Hypoallergenic acid-sensitive modification preserves major mugwort allergen fold and delivers full repertoire of MHC class II-binding peptides during endolysosomal degradation" in RSC Advances, 6, no. 91 (2016):88216-88228,
https://doi.org/10.1039/c6ra17261j .,
conv_394 .
1
1
1

Efficacy of Sublingual Immunotherapy with Dermatophagoides Pteronyssinus: A Real-life Study

Tomić-Spirić, Vesna; Dizdarević, Denisa; Janković, Slavenka; Burazer, Lidija; Barac, Aleksandra; Bolpacić, Jasna; Đurić, Vojislav; Perić-Popadić, Aleksandra; Aleksić, Aleksandra; Bogić, Mirjana

(Tehran Univ Medical Sciences, Tehran, 2016)

TY  - JOUR
AU  - Tomić-Spirić, Vesna
AU  - Dizdarević, Denisa
AU  - Janković, Slavenka
AU  - Burazer, Lidija
AU  - Barac, Aleksandra
AU  - Bolpacić, Jasna
AU  - Đurić, Vojislav
AU  - Perić-Popadić, Aleksandra
AU  - Aleksić, Aleksandra
AU  - Bogić, Mirjana
PY  - 2016
UR  - http://intor.torlakinstitut.com/handle/123456789/474
AB  - Sublingual allergen immunotherapy (SLIT) is considered to be safer and more convenient than subcutaneus immunotherapy. SLIT trials with house dust mites involving patients with allergic rhinitis (AR) and asthma reported discordant results. The aim of the study was to investigate the clinical efficacy and safety of SLIT with Dermatophagoides pteronyssinus (D.pt) extract produced in Serbia and patient's satisfaction through open-label trial. Adult patients with allergic rhinitis were randomized into two groups: one received drugs and SLIT, while other received only drugs. Symptom score (SS), medication score (MS) and cumulative score (CS), skin prick tests (SPT) and serum level of D. pt specific IgE were assessed. One year after, the patients were re-evaluated. In total, 61 patients were enrolled in the study, but 52 of them were analyzed at the end of the year. CS (29.3%, p lt  0.001) and MS (54.3%, p lt  0.05) reduced significantly in the SLIT group. There was a significant improvement of MS and CS in the SLIT compared to control group (p lt  0.001 and p lt  0.05 respectively). There was no significant improvement of SS as well as specific slgE. Patients in the SLIT group were more satisfied with treatment (p lt  0.001). The incidence of mild adverse reaction was 38.4%. Specific lgG was not done. One year SLIT with D. pt extract was clinically efficient treatment in AR patients.
PB  - Tehran Univ Medical Sciences, Tehran
T2  - Iranian Journal of Allergy, Asthma and Immunology
T1  - Efficacy of Sublingual Immunotherapy with Dermatophagoides Pteronyssinus: A Real-life Study
EP  - 121
IS  - 2
SP  - 112
VL  - 15
UR  - conv_388
ER  - 
@article{
author = "Tomić-Spirić, Vesna and Dizdarević, Denisa and Janković, Slavenka and Burazer, Lidija and Barac, Aleksandra and Bolpacić, Jasna and Đurić, Vojislav and Perić-Popadić, Aleksandra and Aleksić, Aleksandra and Bogić, Mirjana",
year = "2016",
abstract = "Sublingual allergen immunotherapy (SLIT) is considered to be safer and more convenient than subcutaneus immunotherapy. SLIT trials with house dust mites involving patients with allergic rhinitis (AR) and asthma reported discordant results. The aim of the study was to investigate the clinical efficacy and safety of SLIT with Dermatophagoides pteronyssinus (D.pt) extract produced in Serbia and patient's satisfaction through open-label trial. Adult patients with allergic rhinitis were randomized into two groups: one received drugs and SLIT, while other received only drugs. Symptom score (SS), medication score (MS) and cumulative score (CS), skin prick tests (SPT) and serum level of D. pt specific IgE were assessed. One year after, the patients were re-evaluated. In total, 61 patients were enrolled in the study, but 52 of them were analyzed at the end of the year. CS (29.3%, p lt  0.001) and MS (54.3%, p lt  0.05) reduced significantly in the SLIT group. There was a significant improvement of MS and CS in the SLIT compared to control group (p lt  0.001 and p lt  0.05 respectively). There was no significant improvement of SS as well as specific slgE. Patients in the SLIT group were more satisfied with treatment (p lt  0.001). The incidence of mild adverse reaction was 38.4%. Specific lgG was not done. One year SLIT with D. pt extract was clinically efficient treatment in AR patients.",
publisher = "Tehran Univ Medical Sciences, Tehran",
journal = "Iranian Journal of Allergy, Asthma and Immunology",
title = "Efficacy of Sublingual Immunotherapy with Dermatophagoides Pteronyssinus: A Real-life Study",
pages = "121-112",
number = "2",
volume = "15",
url = "conv_388"
}
Tomić-Spirić, V., Dizdarević, D., Janković, S., Burazer, L., Barac, A., Bolpacić, J., Đurić, V., Perić-Popadić, A., Aleksić, A.,& Bogić, M.. (2016). Efficacy of Sublingual Immunotherapy with Dermatophagoides Pteronyssinus: A Real-life Study. in Iranian Journal of Allergy, Asthma and Immunology
Tehran Univ Medical Sciences, Tehran., 15(2), 112-121.
conv_388
Tomić-Spirić V, Dizdarević D, Janković S, Burazer L, Barac A, Bolpacić J, Đurić V, Perić-Popadić A, Aleksić A, Bogić M. Efficacy of Sublingual Immunotherapy with Dermatophagoides Pteronyssinus: A Real-life Study. in Iranian Journal of Allergy, Asthma and Immunology. 2016;15(2):112-121.
conv_388 .
Tomić-Spirić, Vesna, Dizdarević, Denisa, Janković, Slavenka, Burazer, Lidija, Barac, Aleksandra, Bolpacić, Jasna, Đurić, Vojislav, Perić-Popadić, Aleksandra, Aleksić, Aleksandra, Bogić, Mirjana, "Efficacy of Sublingual Immunotherapy with Dermatophagoides Pteronyssinus: A Real-life Study" in Iranian Journal of Allergy, Asthma and Immunology, 15, no. 2 (2016):112-121,
conv_388 .
3
4

Composition of polyphenol and polyamide compounds in common ragweed (Ambrosia artemisiifolia L.) pollen and sub-pollen particles

Mihajlović, Luka; Radosavljević, Jelena; Burazer, Lidija; Smiljanić, Katarina; Ćirković-Veličković, Tanja

(Pergamon-Elsevier Science Ltd, Oxford, 2015)

TY  - JOUR
AU  - Mihajlović, Luka
AU  - Radosavljević, Jelena
AU  - Burazer, Lidija
AU  - Smiljanić, Katarina
AU  - Ćirković-Veličković, Tanja
PY  - 2015
UR  - http://intor.torlakinstitut.com/handle/123456789/451
AB  - Phenolic composition of Ambrosia artemisiifolia L. pollen and sub-pollen particles (SPP) aqueous extracts was determined, using a novel extraction procedure. Total phenolic and flavonoid content was determined, as well as the antioxidative properties of the extract. Main components of water-soluble pollen phenolics are monoglycosides and malonyl-mono- and diglycosides of isorhamnetin, quercetin and kaempferol, while spermidine derivatives were identified as the dominant polyamides. SPP are similar in composition to pollen phenolics (predominant isorhamnetin and quercetin monoglycosides), but lacking small phenolic molecules ( lt 450 Da). Ethanol-based extraction protocol revealed one-third lower amount of total phenolics in SPP than in pollen. For the first time in any pollen species, SPP and pollen phenolic compositions were compared in detail, with an UHPLC/ESI-LTQ-Orbitrap-MS-MS approach, revealing the presence of spermidine derivatives in both SPP and pollen, not previously reported in Ambrosia species. (C) 2014 Elsevier Ltd. All rights reserved.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Phytochemistry
T1  - Composition of polyphenol and polyamide compounds in common ragweed (Ambrosia artemisiifolia L.) pollen and sub-pollen particles
EP  - 132
SP  - 125
VL  - 109
DO  - 10.1016/j.phytochem.2014.10.022
UR  - conv_350
ER  - 
@article{
author = "Mihajlović, Luka and Radosavljević, Jelena and Burazer, Lidija and Smiljanić, Katarina and Ćirković-Veličković, Tanja",
year = "2015",
abstract = "Phenolic composition of Ambrosia artemisiifolia L. pollen and sub-pollen particles (SPP) aqueous extracts was determined, using a novel extraction procedure. Total phenolic and flavonoid content was determined, as well as the antioxidative properties of the extract. Main components of water-soluble pollen phenolics are monoglycosides and malonyl-mono- and diglycosides of isorhamnetin, quercetin and kaempferol, while spermidine derivatives were identified as the dominant polyamides. SPP are similar in composition to pollen phenolics (predominant isorhamnetin and quercetin monoglycosides), but lacking small phenolic molecules ( lt 450 Da). Ethanol-based extraction protocol revealed one-third lower amount of total phenolics in SPP than in pollen. For the first time in any pollen species, SPP and pollen phenolic compositions were compared in detail, with an UHPLC/ESI-LTQ-Orbitrap-MS-MS approach, revealing the presence of spermidine derivatives in both SPP and pollen, not previously reported in Ambrosia species. (C) 2014 Elsevier Ltd. All rights reserved.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Phytochemistry",
title = "Composition of polyphenol and polyamide compounds in common ragweed (Ambrosia artemisiifolia L.) pollen and sub-pollen particles",
pages = "132-125",
volume = "109",
doi = "10.1016/j.phytochem.2014.10.022",
url = "conv_350"
}
Mihajlović, L., Radosavljević, J., Burazer, L., Smiljanić, K.,& Ćirković-Veličković, T.. (2015). Composition of polyphenol and polyamide compounds in common ragweed (Ambrosia artemisiifolia L.) pollen and sub-pollen particles. in Phytochemistry
Pergamon-Elsevier Science Ltd, Oxford., 109, 125-132.
https://doi.org/10.1016/j.phytochem.2014.10.022
conv_350
Mihajlović L, Radosavljević J, Burazer L, Smiljanić K, Ćirković-Veličković T. Composition of polyphenol and polyamide compounds in common ragweed (Ambrosia artemisiifolia L.) pollen and sub-pollen particles. in Phytochemistry. 2015;109:125-132.
doi:10.1016/j.phytochem.2014.10.022
conv_350 .
Mihajlović, Luka, Radosavljević, Jelena, Burazer, Lidija, Smiljanić, Katarina, Ćirković-Veličković, Tanja, "Composition of polyphenol and polyamide compounds in common ragweed (Ambrosia artemisiifolia L.) pollen and sub-pollen particles" in Phytochemistry, 109 (2015):125-132,
https://doi.org/10.1016/j.phytochem.2014.10.022 .,
conv_350 .
26
20
25

The importance of cross-reactivity in grass pollen allergy

Aleksić, Ivana; Vučković, Olga; Smiljanić, Katarina; Gavrović-Jankulović, Marija; Krsmanović, Vera; Burazer, Lidija

(Srpsko biološko društvo, Beograd, i dr., 2014)

TY  - JOUR
AU  - Aleksić, Ivana
AU  - Vučković, Olga
AU  - Smiljanić, Katarina
AU  - Gavrović-Jankulović, Marija
AU  - Krsmanović, Vera
AU  - Burazer, Lidija
PY  - 2014
UR  - http://intor.torlakinstitut.com/handle/123456789/407
AB  - According to the data obtained from in vivo and in vitro testing in Serbia, a significant number of patients have allergic symptoms caused by grass pollen. We examined the protein composition of grass pollens (Dactylis glomerata, Lolium perenne and Phleum pratense) and cross-reactivity in patients allergic to grass pollen from our region. The grass pollen allergen extract was characterized by SDS-PAGE, while cross-reactivity of single grass pollens was revealed by immunoblot analysis. A high degree of cross-reactivity was demonstrated for all three single pollens in the sera of allergic patients compared to the grass pollen extract mixture. Confirmation of the existence of cross-reactivity between different antigenic sources facilitates the use of monovalent vaccines, which are easier to standardize and at the same time prevent further sensitization of patients and reduces adverse reactions.
PB  - Srpsko biološko društvo, Beograd, i dr.
T2  - Archives of Biological Sciences
T1  - The importance of cross-reactivity in grass pollen allergy
EP  - 1155
IS  - 3
SP  - 1149
VL  - 66
DO  - 10.2298/ABS1403149A
UR  - conv_348
ER  - 
@article{
author = "Aleksić, Ivana and Vučković, Olga and Smiljanić, Katarina and Gavrović-Jankulović, Marija and Krsmanović, Vera and Burazer, Lidija",
year = "2014",
abstract = "According to the data obtained from in vivo and in vitro testing in Serbia, a significant number of patients have allergic symptoms caused by grass pollen. We examined the protein composition of grass pollens (Dactylis glomerata, Lolium perenne and Phleum pratense) and cross-reactivity in patients allergic to grass pollen from our region. The grass pollen allergen extract was characterized by SDS-PAGE, while cross-reactivity of single grass pollens was revealed by immunoblot analysis. A high degree of cross-reactivity was demonstrated for all three single pollens in the sera of allergic patients compared to the grass pollen extract mixture. Confirmation of the existence of cross-reactivity between different antigenic sources facilitates the use of monovalent vaccines, which are easier to standardize and at the same time prevent further sensitization of patients and reduces adverse reactions.",
publisher = "Srpsko biološko društvo, Beograd, i dr.",
journal = "Archives of Biological Sciences",
title = "The importance of cross-reactivity in grass pollen allergy",
pages = "1155-1149",
number = "3",
volume = "66",
doi = "10.2298/ABS1403149A",
url = "conv_348"
}
Aleksić, I., Vučković, O., Smiljanić, K., Gavrović-Jankulović, M., Krsmanović, V.,& Burazer, L.. (2014). The importance of cross-reactivity in grass pollen allergy. in Archives of Biological Sciences
Srpsko biološko društvo, Beograd, i dr.., 66(3), 1149-1155.
https://doi.org/10.2298/ABS1403149A
conv_348
Aleksić I, Vučković O, Smiljanić K, Gavrović-Jankulović M, Krsmanović V, Burazer L. The importance of cross-reactivity in grass pollen allergy. in Archives of Biological Sciences. 2014;66(3):1149-1155.
doi:10.2298/ABS1403149A
conv_348 .
Aleksić, Ivana, Vučković, Olga, Smiljanić, Katarina, Gavrović-Jankulović, Marija, Krsmanović, Vera, Burazer, Lidija, "The importance of cross-reactivity in grass pollen allergy" in Archives of Biological Sciences, 66, no. 3 (2014):1149-1155,
https://doi.org/10.2298/ABS1403149A .,
conv_348 .
1
1
1

Biochemical and immunological characterization of a recombinantlyproduced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa)

Popović, Milica; Anđelković, Uroš; Burazer, Lidija; Lindner, Buko; Petersen, Arnd; Gavrović-Jankulović, Marija

(Elsevier Ltd, 2013)

TY  - JOUR
AU  - Popović, Milica
AU  - Anđelković, Uroš
AU  - Burazer, Lidija
AU  - Lindner, Buko
AU  - Petersen, Arnd
AU  - Gavrović-Jankulović, Marija
PY  - 2013
UR  - http://intor.torlakinstitut.com/handle/123456789/388
AB  - Plant proteinase inhibitors are considered important defense molecules against insect and pathogen attack. The cysteine proteinase inhibitor (CPI) from green kiwifruit (Actinidia deliciosa) belongs to the cystatin family and shows potent antifungal activity (in vitro and in vivo). However, the low abundance of this molecule in fruit (6 μg/g of fresh fruit) seems to limit further investigations on the interaction between phytocystatin and photopathogenic fungi. In this paper the cDNA of the kiwi CPI was expressed in Escherichia coli. Fifteen N-terminal amino acids were identified by Edman degradation, and 77% of the rCPI primary structure was confirmed by mass fingerprint. The structural homology of recombinant CPI (rCPI) to its natural counterpart has been clearly demonstrated in immunological assays (immunoblot and ELISA inhibition). Biological activity of rCPI was demonstrated in inhibition assay with cysteine proteinase papain (EC50 2.78 nM). In addition, rCPI reveals antifungal properties toward pathogenic fungi (Alternaria radicina and Botrytis cinerea), which designates it as an interesting model protein for the exploration of plant phytocystatins - pathogen interactions. Understanding the molecular mechanisms of natural plant resistance could lead to the development of ecologically safe fungicides for controlling postharvest diseases and maintaining food quality.
PB  - Elsevier Ltd
T2  - Phytochemistry
T1  - Biochemical and immunological characterization of a recombinantlyproduced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa)
EP  - 59
SP  - 53
VL  - 94
DO  - 10.1016/j.phytochem.2013.06.006
UR  - conv_519
ER  - 
@article{
author = "Popović, Milica and Anđelković, Uroš and Burazer, Lidija and Lindner, Buko and Petersen, Arnd and Gavrović-Jankulović, Marija",
year = "2013",
abstract = "Plant proteinase inhibitors are considered important defense molecules against insect and pathogen attack. The cysteine proteinase inhibitor (CPI) from green kiwifruit (Actinidia deliciosa) belongs to the cystatin family and shows potent antifungal activity (in vitro and in vivo). However, the low abundance of this molecule in fruit (6 μg/g of fresh fruit) seems to limit further investigations on the interaction between phytocystatin and photopathogenic fungi. In this paper the cDNA of the kiwi CPI was expressed in Escherichia coli. Fifteen N-terminal amino acids were identified by Edman degradation, and 77% of the rCPI primary structure was confirmed by mass fingerprint. The structural homology of recombinant CPI (rCPI) to its natural counterpart has been clearly demonstrated in immunological assays (immunoblot and ELISA inhibition). Biological activity of rCPI was demonstrated in inhibition assay with cysteine proteinase papain (EC50 2.78 nM). In addition, rCPI reveals antifungal properties toward pathogenic fungi (Alternaria radicina and Botrytis cinerea), which designates it as an interesting model protein for the exploration of plant phytocystatins - pathogen interactions. Understanding the molecular mechanisms of natural plant resistance could lead to the development of ecologically safe fungicides for controlling postharvest diseases and maintaining food quality.",
publisher = "Elsevier Ltd",
journal = "Phytochemistry",
title = "Biochemical and immunological characterization of a recombinantlyproduced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa)",
pages = "59-53",
volume = "94",
doi = "10.1016/j.phytochem.2013.06.006",
url = "conv_519"
}
Popović, M., Anđelković, U., Burazer, L., Lindner, B., Petersen, A.,& Gavrović-Jankulović, M.. (2013). Biochemical and immunological characterization of a recombinantlyproduced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa). in Phytochemistry
Elsevier Ltd., 94, 53-59.
https://doi.org/10.1016/j.phytochem.2013.06.006
conv_519
Popović M, Anđelković U, Burazer L, Lindner B, Petersen A, Gavrović-Jankulović M. Biochemical and immunological characterization of a recombinantlyproduced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa). in Phytochemistry. 2013;94:53-59.
doi:10.1016/j.phytochem.2013.06.006
conv_519 .
Popović, Milica, Anđelković, Uroš, Burazer, Lidija, Lindner, Buko, Petersen, Arnd, Gavrović-Jankulović, Marija, "Biochemical and immunological characterization of a recombinantlyproduced antifungal cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa)" in Phytochemistry, 94 (2013):53-59,
https://doi.org/10.1016/j.phytochem.2013.06.006 .,
conv_519 .
1
16
16
17

Kiwifruit (Actinidia deliciosa) extract shows potential as a low-cost andefficient milk-clotting agent

Grozdanović, Milica; Burazer, Lidija; Gavrović-Jankulović, Marija

(2013)

TY  - JOUR
AU  - Grozdanović, Milica
AU  - Burazer, Lidija
AU  - Gavrović-Jankulović, Marija
PY  - 2013
UR  - http://intor.torlakinstitut.com/handle/123456789/373
AB  - Actinidin, a cysteine protease accounting for more than 50% of the soluble proteins in kiwifruit pulp, has shown promise as a milk-clotting agent. In this study, the potential use of kiwifruit pulp extract as a clotting agent was investigated. It was shown that three kiwifruit extracts made from the pulp of a single fruit have significantly different levels of active actinidin, depending on the extraction buffer employed. Kiwifruit extract prepared at pH 5.0 had the best milk-clotting properties, with a nearly 30% better ratio of clotting activity to proteolytic activity than purified actinidin. This extract produced a casein coagulum clearly separated from the whey proteins, and was shown to be stable at room temperature for up to two months. This extract has the potential to be employed as an efficient and low-cost milk-clotting agent in the production of dairy products.
T2  - International Dairy Journal
T1  - Kiwifruit (Actinidia deliciosa) extract shows potential as a low-cost andefficient milk-clotting agent
EP  - 52
IS  - 1
SP  - 46
VL  - 32
DO  - 10.1016/j.idairyj.2013.03.001
UR  - conv_527
ER  - 
@article{
author = "Grozdanović, Milica and Burazer, Lidija and Gavrović-Jankulović, Marija",
year = "2013",
abstract = "Actinidin, a cysteine protease accounting for more than 50% of the soluble proteins in kiwifruit pulp, has shown promise as a milk-clotting agent. In this study, the potential use of kiwifruit pulp extract as a clotting agent was investigated. It was shown that three kiwifruit extracts made from the pulp of a single fruit have significantly different levels of active actinidin, depending on the extraction buffer employed. Kiwifruit extract prepared at pH 5.0 had the best milk-clotting properties, with a nearly 30% better ratio of clotting activity to proteolytic activity than purified actinidin. This extract produced a casein coagulum clearly separated from the whey proteins, and was shown to be stable at room temperature for up to two months. This extract has the potential to be employed as an efficient and low-cost milk-clotting agent in the production of dairy products.",
journal = "International Dairy Journal",
title = "Kiwifruit (Actinidia deliciosa) extract shows potential as a low-cost andefficient milk-clotting agent",
pages = "52-46",
number = "1",
volume = "32",
doi = "10.1016/j.idairyj.2013.03.001",
url = "conv_527"
}
Grozdanović, M., Burazer, L.,& Gavrović-Jankulović, M.. (2013). Kiwifruit (Actinidia deliciosa) extract shows potential as a low-cost andefficient milk-clotting agent. in International Dairy Journal, 32(1), 46-52.
https://doi.org/10.1016/j.idairyj.2013.03.001
conv_527
Grozdanović M, Burazer L, Gavrović-Jankulović M. Kiwifruit (Actinidia deliciosa) extract shows potential as a low-cost andefficient milk-clotting agent. in International Dairy Journal. 2013;32(1):46-52.
doi:10.1016/j.idairyj.2013.03.001
conv_527 .
Grozdanović, Milica, Burazer, Lidija, Gavrović-Jankulović, Marija, "Kiwifruit (Actinidia deliciosa) extract shows potential as a low-cost andefficient milk-clotting agent" in International Dairy Journal, 32, no. 1 (2013):46-52,
https://doi.org/10.1016/j.idairyj.2013.03.001 .,
conv_527 .
2
25
19
25

Immunoproteomic characterization of Ambrosia artemisiifolia pollen allergens in canine atopic dermatitis

Ognjenović, Jana; Milčić-Matić, Natalija; Smiljanić, Katarina; Vučković, Olga; Burazer, Lidija; Popović, Nikola; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier Science Bv, Amsterdam, 2013)

TY  - JOUR
AU  - Ognjenović, Jana
AU  - Milčić-Matić, Natalija
AU  - Smiljanić, Katarina
AU  - Vučković, Olga
AU  - Burazer, Lidija
AU  - Popović, Nikola
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2013
UR  - http://intor.torlakinstitut.com/handle/123456789/375
AB  - Canine atopic dermatitis (CAD) is an immune system disorder that affects 10-15% of the canine population. Short ragweed (Ambrosia artemisiifolia) pollen represents one of the major seasonal sources of allergenic pollen proteins in Europe, particularly in the Pannonian valley of the Balkan region. In Serbia, about 66% of atopic dogs showed a positive intradermal skin test with its pollen extract, which is second to house dust mites. Therefore, characterization of Ambrosia artemisiifolia pollen components, in terms of defining major and minor allergens that induce clinically manifested allergic reaction in dogs, is important for valid diagnosis and efficient therapy. This study has, for the first time, characterized and identified major Ambrosia artemisiifolia allergens in CAD, using an immunoproteomic approach. To assess the prevalence of specific IgE in electrophoretically separated ragweed pollen proteins, individual reactivity of sera from dogs with CAD was analyzed and compared to the reactivity of sera from healthy dogs in the non-reducing conditions, which were found optimal for specific canine IgE detection. A specific IgE band (38 kDa) was recognized as the most dominant allergen in CAD, occurring in 81% of positive dog's sera. 2-D immunoblotting followed by a mass spectrometry peptide fingerprint analyses with pooled canine and human atopic sera, revealed that 38 kDa major Ambrosia atremisiifolia allergens in CAD were all five isoallergens of the Amb a 1 group (antigen E), including the previously named Amb a 2 (antigen K). In contrast to canine sera, human atopic sera also recognized lower mass allergens such as the 13 fragment of Amb a 1 and profilins (Amb a 8 variants). The most prominent ragweed proteins in CAD, represent, as in humans, variants of all five isoallergens of the Amb a 1 group (pectate lyase): Amb a 1.0101 and its natural variant E1XUL2, Amb a 1.0202, 1.0304, 1.0402 and the natural variant of Amb a 1.0501, E1XUM0, as well as the a fragment of pollen allergen Amb a 1.0201. (C) 2013 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
T2  - Veterinary Immunology and Immunopathology
T1  - Immunoproteomic characterization of Ambrosia artemisiifolia pollen allergens in canine atopic dermatitis
EP  - 47
IS  - 1-2
SP  - 38
VL  - 155
DO  - 10.1016/j.vetimm.2013.06.005
UR  - conv_315
ER  - 
@article{
author = "Ognjenović, Jana and Milčić-Matić, Natalija and Smiljanić, Katarina and Vučković, Olga and Burazer, Lidija and Popović, Nikola and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2013",
abstract = "Canine atopic dermatitis (CAD) is an immune system disorder that affects 10-15% of the canine population. Short ragweed (Ambrosia artemisiifolia) pollen represents one of the major seasonal sources of allergenic pollen proteins in Europe, particularly in the Pannonian valley of the Balkan region. In Serbia, about 66% of atopic dogs showed a positive intradermal skin test with its pollen extract, which is second to house dust mites. Therefore, characterization of Ambrosia artemisiifolia pollen components, in terms of defining major and minor allergens that induce clinically manifested allergic reaction in dogs, is important for valid diagnosis and efficient therapy. This study has, for the first time, characterized and identified major Ambrosia artemisiifolia allergens in CAD, using an immunoproteomic approach. To assess the prevalence of specific IgE in electrophoretically separated ragweed pollen proteins, individual reactivity of sera from dogs with CAD was analyzed and compared to the reactivity of sera from healthy dogs in the non-reducing conditions, which were found optimal for specific canine IgE detection. A specific IgE band (38 kDa) was recognized as the most dominant allergen in CAD, occurring in 81% of positive dog's sera. 2-D immunoblotting followed by a mass spectrometry peptide fingerprint analyses with pooled canine and human atopic sera, revealed that 38 kDa major Ambrosia atremisiifolia allergens in CAD were all five isoallergens of the Amb a 1 group (antigen E), including the previously named Amb a 2 (antigen K). In contrast to canine sera, human atopic sera also recognized lower mass allergens such as the 13 fragment of Amb a 1 and profilins (Amb a 8 variants). The most prominent ragweed proteins in CAD, represent, as in humans, variants of all five isoallergens of the Amb a 1 group (pectate lyase): Amb a 1.0101 and its natural variant E1XUL2, Amb a 1.0202, 1.0304, 1.0402 and the natural variant of Amb a 1.0501, E1XUM0, as well as the a fragment of pollen allergen Amb a 1.0201. (C) 2013 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Veterinary Immunology and Immunopathology",
title = "Immunoproteomic characterization of Ambrosia artemisiifolia pollen allergens in canine atopic dermatitis",
pages = "47-38",
number = "1-2",
volume = "155",
doi = "10.1016/j.vetimm.2013.06.005",
url = "conv_315"
}
Ognjenović, J., Milčić-Matić, N., Smiljanić, K., Vučković, O., Burazer, L., Popović, N., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2013). Immunoproteomic characterization of Ambrosia artemisiifolia pollen allergens in canine atopic dermatitis. in Veterinary Immunology and Immunopathology
Elsevier Science Bv, Amsterdam., 155(1-2), 38-47.
https://doi.org/10.1016/j.vetimm.2013.06.005
conv_315
Ognjenović J, Milčić-Matić N, Smiljanić K, Vučković O, Burazer L, Popović N, Stanić-Vučinić D, Ćirković-Veličković T. Immunoproteomic characterization of Ambrosia artemisiifolia pollen allergens in canine atopic dermatitis. in Veterinary Immunology and Immunopathology. 2013;155(1-2):38-47.
doi:10.1016/j.vetimm.2013.06.005
conv_315 .
Ognjenović, Jana, Milčić-Matić, Natalija, Smiljanić, Katarina, Vučković, Olga, Burazer, Lidija, Popović, Nikola, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Immunoproteomic characterization of Ambrosia artemisiifolia pollen allergens in canine atopic dermatitis" in Veterinary Immunology and Immunopathology, 155, no. 1-2 (2013):38-47,
https://doi.org/10.1016/j.vetimm.2013.06.005 .,
conv_315 .
13
9
10

Evaluation of criteria for diagnosis of atopic dermatitis and detection of allergen specific IgE antibodies in dogs allergic to Ambrosia artemisiifolia pollen

Milčić-Matić, Natalija; Ognjenović, Jana; Burazer, Lidija; Blagojević, Gordan; Popović, Nikola; Lazarević, M.; Stanić-Vučinić, Dragana

(Univerzitet u Beogradu - Fakultet veterinarske medicine, Beograd, 2013)

TY  - JOUR
AU  - Milčić-Matić, Natalija
AU  - Ognjenović, Jana
AU  - Burazer, Lidija
AU  - Blagojević, Gordan
AU  - Popović, Nikola
AU  - Lazarević, M.
AU  - Stanić-Vučinić, Dragana
PY  - 2013
UR  - http://intor.torlakinstitut.com/handle/123456789/370
AB  - Common ragweed (Ambrosia atremisiifolia) is one of the most frequent causes of pollen-induced allergic reactions both in humans and dogs. It has not been defined yet, what is the major allergen(s) to which most dogs allergic to ragweed show a positive result on intradermal skin test (IDST). In the present study sensitization to Ambrosia artemisiifolia pollen allergens in dogs with atopic dermatitis was examined with both in vivo and in vitro tests, including IDST and serum allergen specific IgE test. Detection of specific-IgE antibodies against ragweed allergens by immunoblotting in the sera of allergic dogs was optimized, as well. Dogs that were positive, as judged by IDST reactions to ragweed pollen allergens, also had alergen specific IgE antibodies in their sera. Results indicate that major allergens of A. artemisifolia pollen in dogs are Amb a 1 and Amb a 2. Further characterization of ragweed allergens is needed before they could potentially be used in intradermal testing or allergen immunotherapy in affected dogs. Also, we evaluated new Favrots diagnostic criteria for canine atopic dermatitis in dogs allergic to Ambrosia atremisiifolia pollen. It might be concluded that proposed criteria are of great assistance for seting up suspected diagnosis of canine atopic dermatitis, after ruling out other pruritic dermatoses.
AB  - Kratka ambrozija (Ambrosia artemisiifolia) je jedan od najčešćih uzročnika alergijskih reakcija izazvanih polenom kod ljudi i pasa. Još uvek nije definisano koji je glavni alergen (i), na koji, većina pasa alergičnih na polen ambrozije, ispoljava pozitivnu reakciju na intradermalnom testu. U ovoj studiji je ispitana senzibilizacija na polen ove biljke kod pasa sa simptomima atopijskog dermatitisa in vivo i in vitro testovima, uključujući intradermalni test i dokazivanje prisustva alergen specifičnih IgE antitela u serumu. Optimizovani su uslovi za detekciju IgE specifičnih antitela iz seruma pasa alergičnih na polen ambrozije imunoblot tehnikom. Psi koji su imali pozitivnu reakciju na polen ove biljke na intradermalnom testu, takođe su imali specifična IgE antitela u serumu. Dobijeni rezultati ukazuju da su glavni alergeni Ambrosia artemisiifolia kod pasa Amb a 1 i Amb a 2. Neophodna je dalja karakterizacija alergena ambrozije kako bi se oni mogli primeniti pri rutinskom intradermalnom testiranju ili u alergen specifičnoj imunoterapiji obolelih pasa. Takođe je razmatrana i validnost Favrotovih dijagnostičkih kriterijuma kod pasa alergičnih na polen ambrozije. Može se zaključiti da su predloženi kriterijumi od velike pomoći u postavljanju suspektne dijagnoze atopijskog dermatitisa pasa, nakon isključenja drugih pruritičnih dermatoza.
PB  - Univerzitet u Beogradu - Fakultet veterinarske medicine, Beograd
T2  - Acta veterinaria - Beograd
T1  - Evaluation of criteria for diagnosis of atopic dermatitis and detection of allergen specific IgE antibodies in dogs allergic to Ambrosia artemisiifolia pollen
T1  - Evaluacija kriterijuma za dijagnozu atopijskog dermatitisa i detekcija alergen specifičnih IgE antitela kod pasa alergičnih na polen biljke Ambrosia artemisiifolia
EP  - 451
IS  - 4
SP  - 437
VL  - 63
DO  - 10.2298/AVB1304437M
UR  - conv_61
ER  - 
@article{
author = "Milčić-Matić, Natalija and Ognjenović, Jana and Burazer, Lidija and Blagojević, Gordan and Popović, Nikola and Lazarević, M. and Stanić-Vučinić, Dragana",
year = "2013",
abstract = "Common ragweed (Ambrosia atremisiifolia) is one of the most frequent causes of pollen-induced allergic reactions both in humans and dogs. It has not been defined yet, what is the major allergen(s) to which most dogs allergic to ragweed show a positive result on intradermal skin test (IDST). In the present study sensitization to Ambrosia artemisiifolia pollen allergens in dogs with atopic dermatitis was examined with both in vivo and in vitro tests, including IDST and serum allergen specific IgE test. Detection of specific-IgE antibodies against ragweed allergens by immunoblotting in the sera of allergic dogs was optimized, as well. Dogs that were positive, as judged by IDST reactions to ragweed pollen allergens, also had alergen specific IgE antibodies in their sera. Results indicate that major allergens of A. artemisifolia pollen in dogs are Amb a 1 and Amb a 2. Further characterization of ragweed allergens is needed before they could potentially be used in intradermal testing or allergen immunotherapy in affected dogs. Also, we evaluated new Favrots diagnostic criteria for canine atopic dermatitis in dogs allergic to Ambrosia atremisiifolia pollen. It might be concluded that proposed criteria are of great assistance for seting up suspected diagnosis of canine atopic dermatitis, after ruling out other pruritic dermatoses., Kratka ambrozija (Ambrosia artemisiifolia) je jedan od najčešćih uzročnika alergijskih reakcija izazvanih polenom kod ljudi i pasa. Još uvek nije definisano koji je glavni alergen (i), na koji, većina pasa alergičnih na polen ambrozije, ispoljava pozitivnu reakciju na intradermalnom testu. U ovoj studiji je ispitana senzibilizacija na polen ove biljke kod pasa sa simptomima atopijskog dermatitisa in vivo i in vitro testovima, uključujući intradermalni test i dokazivanje prisustva alergen specifičnih IgE antitela u serumu. Optimizovani su uslovi za detekciju IgE specifičnih antitela iz seruma pasa alergičnih na polen ambrozije imunoblot tehnikom. Psi koji su imali pozitivnu reakciju na polen ove biljke na intradermalnom testu, takođe su imali specifična IgE antitela u serumu. Dobijeni rezultati ukazuju da su glavni alergeni Ambrosia artemisiifolia kod pasa Amb a 1 i Amb a 2. Neophodna je dalja karakterizacija alergena ambrozije kako bi se oni mogli primeniti pri rutinskom intradermalnom testiranju ili u alergen specifičnoj imunoterapiji obolelih pasa. Takođe je razmatrana i validnost Favrotovih dijagnostičkih kriterijuma kod pasa alergičnih na polen ambrozije. Može se zaključiti da su predloženi kriterijumi od velike pomoći u postavljanju suspektne dijagnoze atopijskog dermatitisa pasa, nakon isključenja drugih pruritičnih dermatoza.",
publisher = "Univerzitet u Beogradu - Fakultet veterinarske medicine, Beograd",
journal = "Acta veterinaria - Beograd",
title = "Evaluation of criteria for diagnosis of atopic dermatitis and detection of allergen specific IgE antibodies in dogs allergic to Ambrosia artemisiifolia pollen, Evaluacija kriterijuma za dijagnozu atopijskog dermatitisa i detekcija alergen specifičnih IgE antitela kod pasa alergičnih na polen biljke Ambrosia artemisiifolia",
pages = "451-437",
number = "4",
volume = "63",
doi = "10.2298/AVB1304437M",
url = "conv_61"
}
Milčić-Matić, N., Ognjenović, J., Burazer, L., Blagojević, G., Popović, N., Lazarević, M.,& Stanić-Vučinić, D.. (2013). Evaluation of criteria for diagnosis of atopic dermatitis and detection of allergen specific IgE antibodies in dogs allergic to Ambrosia artemisiifolia pollen. in Acta veterinaria - Beograd
Univerzitet u Beogradu - Fakultet veterinarske medicine, Beograd., 63(4), 437-451.
https://doi.org/10.2298/AVB1304437M
conv_61
Milčić-Matić N, Ognjenović J, Burazer L, Blagojević G, Popović N, Lazarević M, Stanić-Vučinić D. Evaluation of criteria for diagnosis of atopic dermatitis and detection of allergen specific IgE antibodies in dogs allergic to Ambrosia artemisiifolia pollen. in Acta veterinaria - Beograd. 2013;63(4):437-451.
doi:10.2298/AVB1304437M
conv_61 .
Milčić-Matić, Natalija, Ognjenović, Jana, Burazer, Lidija, Blagojević, Gordan, Popović, Nikola, Lazarević, M., Stanić-Vučinić, Dragana, "Evaluation of criteria for diagnosis of atopic dermatitis and detection of allergen specific IgE antibodies in dogs allergic to Ambrosia artemisiifolia pollen" in Acta veterinaria - Beograd, 63, no. 4 (2013):437-451,
https://doi.org/10.2298/AVB1304437M .,
conv_61 .
1
1

Importance of sIgE measurement in evaluation of Dermatophagoides pteronyssinus major allergens in pediatric population

Burazer, Lidija; Aleksić, I.; Vučković, Olga; Gavrović, Marija

(Wiley-Blackwell, Hoboken, 2013)

TY  - CONF
AU  - Burazer, Lidija
AU  - Aleksić, I.
AU  - Vučković, Olga
AU  - Gavrović, Marija
PY  - 2013
UR  - http://intor.torlakinstitut.com/handle/123456789/380
PB  - Wiley-Blackwell, Hoboken
C3  - Allergy
T1  - Importance of sIgE measurement in evaluation of Dermatophagoides pteronyssinus major allergens in pediatric population
EP  - 689
SP  - 689
VL  - 68
UR  - conv_319
ER  - 
@conference{
author = "Burazer, Lidija and Aleksić, I. and Vučković, Olga and Gavrović, Marija",
year = "2013",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "Importance of sIgE measurement in evaluation of Dermatophagoides pteronyssinus major allergens in pediatric population",
pages = "689-689",
volume = "68",
url = "conv_319"
}
Burazer, L., Aleksić, I., Vučković, O.,& Gavrović, M.. (2013). Importance of sIgE measurement in evaluation of Dermatophagoides pteronyssinus major allergens in pediatric population. in Allergy
Wiley-Blackwell, Hoboken., 68, 689-689.
conv_319
Burazer L, Aleksić I, Vučković O, Gavrović M. Importance of sIgE measurement in evaluation of Dermatophagoides pteronyssinus major allergens in pediatric population. in Allergy. 2013;68:689-689.
conv_319 .
Burazer, Lidija, Aleksić, I., Vučković, Olga, Gavrović, Marija, "Importance of sIgE measurement in evaluation of Dermatophagoides pteronyssinus major allergens in pediatric population" in Allergy, 68 (2013):689-689,
conv_319 .
1

Optimization of the heterologous expression of banana glucanase in Escherichia coli (vol 77, pg 43, 2012)

Abughren, Mohamed; Popović, Milica; Dimitrijević, Rajna; Burazer, Lidija; Grozdanović, Milica; Atanasković-Marković, Marina; Gavrović-Jankulović, Marija

(Srpsko hemijsko društvo, Beograd, 2012)

TY  - JOUR
AU  - Abughren, Mohamed
AU  - Popović, Milica
AU  - Dimitrijević, Rajna
AU  - Burazer, Lidija
AU  - Grozdanović, Milica
AU  - Atanasković-Marković, Marina
AU  - Gavrović-Jankulović, Marija
PY  - 2012
UR  - http://intor.torlakinstitut.com/handle/123456789/364
PB  - Srpsko hemijsko društvo, Beograd
T2  - Journal of the Serbian Chemical Society
T1  - Optimization of the heterologous expression of banana glucanase in Escherichia coli (vol 77, pg 43, 2012)
EP  - 258
IS  - 2
SP  - 257
VL  - 77
UR  - conv_284
ER  - 
@article{
author = "Abughren, Mohamed and Popović, Milica and Dimitrijević, Rajna and Burazer, Lidija and Grozdanović, Milica and Atanasković-Marković, Marina and Gavrović-Jankulović, Marija",
year = "2012",
publisher = "Srpsko hemijsko društvo, Beograd",
journal = "Journal of the Serbian Chemical Society",
title = "Optimization of the heterologous expression of banana glucanase in Escherichia coli (vol 77, pg 43, 2012)",
pages = "258-257",
number = "2",
volume = "77",
url = "conv_284"
}
Abughren, M., Popović, M., Dimitrijević, R., Burazer, L., Grozdanović, M., Atanasković-Marković, M.,& Gavrović-Jankulović, M.. (2012). Optimization of the heterologous expression of banana glucanase in Escherichia coli (vol 77, pg 43, 2012). in Journal of the Serbian Chemical Society
Srpsko hemijsko društvo, Beograd., 77(2), 257-258.
conv_284
Abughren M, Popović M, Dimitrijević R, Burazer L, Grozdanović M, Atanasković-Marković M, Gavrović-Jankulović M. Optimization of the heterologous expression of banana glucanase in Escherichia coli (vol 77, pg 43, 2012). in Journal of the Serbian Chemical Society. 2012;77(2):257-258.
conv_284 .
Abughren, Mohamed, Popović, Milica, Dimitrijević, Rajna, Burazer, Lidija, Grozdanović, Milica, Atanasković-Marković, Marina, Gavrović-Jankulović, Marija, "Optimization of the heterologous expression of banana glucanase in Escherichia coli (vol 77, pg 43, 2012)" in Journal of the Serbian Chemical Society, 77, no. 2 (2012):257-258,
conv_284 .

Optimization of the heterologous expression of banana glucanase in Escherichia coli

Abughren, Mohamed; Popović, Milica; Dimitrijević, Rajna; Burazer, Lidija; Grozdanović, Milica; Atanasković-Marković, Marina; Gavrović-Jankulović, Marija

(Srpsko hemijsko društvo, Beograd, 2012)

TY  - JOUR
AU  - Abughren, Mohamed
AU  - Popović, Milica
AU  - Dimitrijević, Rajna
AU  - Burazer, Lidija
AU  - Grozdanović, Milica
AU  - Atanasković-Marković, Marina
AU  - Gavrović-Jankulović, Marija
PY  - 2012
UR  - http://intor.torlakinstitut.com/handle/123456789/350
AB  - For the heterologous production of a banana glucanase in Escherichia coli, its gene (GenBank GQ268963) was cloned into a pG EX-4T expression vector as a fusion protein with glutathione-S-transferase (GST). BL21 cells transformed with the GST-Mus a 5 con struct were employed for production of the protein induced by 1 mM isopropyl-β-D-thiogalactopyranoside (IPTG). The conditions for protein expression were optimized by varying the temperature (25, 30 and 37°C) and duration of protein expression (3, 6 and 12 h). The level of protein production was analyzed by densitometry of the sodium dodecyl sulfate-polyacrylamide gel (SDS-PAG) after electrophoretic resolution of the respective cell lysates. The optimal protein expression for downstream processing was obtained after 12 h of cell growth at 25°C upon addition of IPTG. Recombinant GST-Mus a 5 purified by glutathione affinity chromatography revealed a molecular mass of a bout 60 kDa. The IgE and IgG reactivity of the rGST-Mus a 5 was confirmed by dot blot an analysis with sera of individual patients from subjects with banana allergy and polyclonal rabbit antibodies against banana extract, respectively. The purified recombinant glucanase is a potential candidate for banana allergy diagnosis.
AB  - Za potrebe proizvodnje u Escherichia coli gen glukanaze iz banane (GenBank GQ268963) je ukloniran u ekspresioni vektor pGEX-4T sa glutation-S-transferazom (GST). Proizvodnja ovog proteina u ćelijama je indukovana 1 mM izopropil-β-D-tiogalaktopiranozidom (IPTG). Uslovi za ekspresiju proteina su optimizovani variranjem temperature (25, 30 i 37°C) i dužine trajanja proteinske sinteze (3, 6 i 12 h). Nivo proizvodnje proteina je analiziran denzitometrijom SDS-PA gela nakon elektroforetskog razdvajanja ćelijskih lizata. Optimalna proizvodnja proteina za njegovo dalje procesovanje je dobijena gajenjem ćelija nakon dodatka IPTG na 25°C tokom 12 h. Rekombinantni GST-Mus a 5 prečišćen afinitetnom hromatografijom sa glutationom pokazuje molekulsku masu od 60 kDa. IgE i IgG reaktivnost izolovane glukanaze potvrđena je u 'dot blot' sa pojedinačnim serumima osoba alergičnih na bananu, i sa poliklonskim zečijim antitelima na ekstrakt banane, redom. Prečišćena rekombinantna glukanaza je potencijalan kandidat za dijagnozu alergije na bananu.
PB  - Srpsko hemijsko društvo, Beograd
T2  - Journal of the Serbian Chemical Society
T1  - Optimization of the heterologous expression of banana glucanase in Escherichia coli
T1  - Optimizacija heterologe proizvodnje glukanaze iz banane u E. coli
EP  - 52
IS  - 1
SP  - 43
VL  - 77
DO  - 10.2298/JSC110309158A
UR  - conv_24
ER  - 
@article{
author = "Abughren, Mohamed and Popović, Milica and Dimitrijević, Rajna and Burazer, Lidija and Grozdanović, Milica and Atanasković-Marković, Marina and Gavrović-Jankulović, Marija",
year = "2012",
abstract = "For the heterologous production of a banana glucanase in Escherichia coli, its gene (GenBank GQ268963) was cloned into a pG EX-4T expression vector as a fusion protein with glutathione-S-transferase (GST). BL21 cells transformed with the GST-Mus a 5 con struct were employed for production of the protein induced by 1 mM isopropyl-β-D-thiogalactopyranoside (IPTG). The conditions for protein expression were optimized by varying the temperature (25, 30 and 37°C) and duration of protein expression (3, 6 and 12 h). The level of protein production was analyzed by densitometry of the sodium dodecyl sulfate-polyacrylamide gel (SDS-PAG) after electrophoretic resolution of the respective cell lysates. The optimal protein expression for downstream processing was obtained after 12 h of cell growth at 25°C upon addition of IPTG. Recombinant GST-Mus a 5 purified by glutathione affinity chromatography revealed a molecular mass of a bout 60 kDa. The IgE and IgG reactivity of the rGST-Mus a 5 was confirmed by dot blot an analysis with sera of individual patients from subjects with banana allergy and polyclonal rabbit antibodies against banana extract, respectively. The purified recombinant glucanase is a potential candidate for banana allergy diagnosis., Za potrebe proizvodnje u Escherichia coli gen glukanaze iz banane (GenBank GQ268963) je ukloniran u ekspresioni vektor pGEX-4T sa glutation-S-transferazom (GST). Proizvodnja ovog proteina u ćelijama je indukovana 1 mM izopropil-β-D-tiogalaktopiranozidom (IPTG). Uslovi za ekspresiju proteina su optimizovani variranjem temperature (25, 30 i 37°C) i dužine trajanja proteinske sinteze (3, 6 i 12 h). Nivo proizvodnje proteina je analiziran denzitometrijom SDS-PA gela nakon elektroforetskog razdvajanja ćelijskih lizata. Optimalna proizvodnja proteina za njegovo dalje procesovanje je dobijena gajenjem ćelija nakon dodatka IPTG na 25°C tokom 12 h. Rekombinantni GST-Mus a 5 prečišćen afinitetnom hromatografijom sa glutationom pokazuje molekulsku masu od 60 kDa. IgE i IgG reaktivnost izolovane glukanaze potvrđena je u 'dot blot' sa pojedinačnim serumima osoba alergičnih na bananu, i sa poliklonskim zečijim antitelima na ekstrakt banane, redom. Prečišćena rekombinantna glukanaza je potencijalan kandidat za dijagnozu alergije na bananu.",
publisher = "Srpsko hemijsko društvo, Beograd",
journal = "Journal of the Serbian Chemical Society",
title = "Optimization of the heterologous expression of banana glucanase in Escherichia coli, Optimizacija heterologe proizvodnje glukanaze iz banane u E. coli",
pages = "52-43",
number = "1",
volume = "77",
doi = "10.2298/JSC110309158A",
url = "conv_24"
}
Abughren, M., Popović, M., Dimitrijević, R., Burazer, L., Grozdanović, M., Atanasković-Marković, M.,& Gavrović-Jankulović, M.. (2012). Optimization of the heterologous expression of banana glucanase in Escherichia coli. in Journal of the Serbian Chemical Society
Srpsko hemijsko društvo, Beograd., 77(1), 43-52.
https://doi.org/10.2298/JSC110309158A
conv_24
Abughren M, Popović M, Dimitrijević R, Burazer L, Grozdanović M, Atanasković-Marković M, Gavrović-Jankulović M. Optimization of the heterologous expression of banana glucanase in Escherichia coli. in Journal of the Serbian Chemical Society. 2012;77(1):43-52.
doi:10.2298/JSC110309158A
conv_24 .
Abughren, Mohamed, Popović, Milica, Dimitrijević, Rajna, Burazer, Lidija, Grozdanović, Milica, Atanasković-Marković, Marina, Gavrović-Jankulović, Marija, "Optimization of the heterologous expression of banana glucanase in Escherichia coli" in Journal of the Serbian Chemical Society, 77, no. 1 (2012):43-52,
https://doi.org/10.2298/JSC110309158A .,
conv_24 .
1
2
2

One-step method for isolation and purification of native beta-lactoglobulin from bovine whey

Stojadinović, Marija; Burazer, Lidija; Ercili-Cura, Dilek; Sancho, Ana; Buchert, Johanna; Ćirković-Veličković, Tanja; Stanić-Vučinić, Dragana

(Wiley-Blackwell, Malden, 2012)

TY  - JOUR
AU  - Stojadinović, Marija
AU  - Burazer, Lidija
AU  - Ercili-Cura, Dilek
AU  - Sancho, Ana
AU  - Buchert, Johanna
AU  - Ćirković-Veličković, Tanja
AU  - Stanić-Vučinić, Dragana
PY  - 2012
UR  - http://intor.torlakinstitut.com/handle/123456789/361
AB  - BACKGROUND: The major whey protein beta-lactoglobulin (BLG) has been widely studied for its functional properties. The aim of this study was to develop an efficient, inexpensive and rapid one-step method for the isolation and purification of BLG while preserving its native structure. RESULTS: BLGwas purified fromdefattedwheyobtainedfromrawcow's milkbyanionexchangechromatography. Protein purity and identitywere determined using reverse phase high-performance liquid chromatography andmass spectrometry. Total BLG yield was 80% with protein purity from 97 to 99%. BLG isoforms A and B were separated into fractions of 91 and 99% purity respectively. The structure and native conformation of the isolated BLGwere compared with those of standard commercial BLG by circular dichroism spectrometry, susceptibility to various crosslinking enzymes and enzyme-linked immunosorbent assay inhibition. CONCLUSION: Theproposedmethodis veryuseful for the rapid preparationofBLGsuitable for studying antigenicandmolecular characteristics of this protein, aswell as the effect of food processing on these properties. The procedure requires only 1 day for the purification of about 300 mgof BLG from a single run using a small column (2.5 cmx20 cm) of diethylaminoethyl Sephadex and has potential for scaling up. (C) 2011 Society of Chemical Industry
PB  - Wiley-Blackwell, Malden
T2  - Journal of the Science of Food and Agriculture
T1  - One-step method for isolation and purification of native beta-lactoglobulin from bovine whey
EP  - 1440
IS  - 7
SP  - 1432
VL  - 92
DO  - 10.1002/jsfa.4722
UR  - conv_287
ER  - 
@article{
author = "Stojadinović, Marija and Burazer, Lidija and Ercili-Cura, Dilek and Sancho, Ana and Buchert, Johanna and Ćirković-Veličković, Tanja and Stanić-Vučinić, Dragana",
year = "2012",
abstract = "BACKGROUND: The major whey protein beta-lactoglobulin (BLG) has been widely studied for its functional properties. The aim of this study was to develop an efficient, inexpensive and rapid one-step method for the isolation and purification of BLG while preserving its native structure. RESULTS: BLGwas purified fromdefattedwheyobtainedfromrawcow's milkbyanionexchangechromatography. Protein purity and identitywere determined using reverse phase high-performance liquid chromatography andmass spectrometry. Total BLG yield was 80% with protein purity from 97 to 99%. BLG isoforms A and B were separated into fractions of 91 and 99% purity respectively. The structure and native conformation of the isolated BLGwere compared with those of standard commercial BLG by circular dichroism spectrometry, susceptibility to various crosslinking enzymes and enzyme-linked immunosorbent assay inhibition. CONCLUSION: Theproposedmethodis veryuseful for the rapid preparationofBLGsuitable for studying antigenicandmolecular characteristics of this protein, aswell as the effect of food processing on these properties. The procedure requires only 1 day for the purification of about 300 mgof BLG from a single run using a small column (2.5 cmx20 cm) of diethylaminoethyl Sephadex and has potential for scaling up. (C) 2011 Society of Chemical Industry",
publisher = "Wiley-Blackwell, Malden",
journal = "Journal of the Science of Food and Agriculture",
title = "One-step method for isolation and purification of native beta-lactoglobulin from bovine whey",
pages = "1440-1432",
number = "7",
volume = "92",
doi = "10.1002/jsfa.4722",
url = "conv_287"
}
Stojadinović, M., Burazer, L., Ercili-Cura, D., Sancho, A., Buchert, J., Ćirković-Veličković, T.,& Stanić-Vučinić, D.. (2012). One-step method for isolation and purification of native beta-lactoglobulin from bovine whey. in Journal of the Science of Food and Agriculture
Wiley-Blackwell, Malden., 92(7), 1432-1440.
https://doi.org/10.1002/jsfa.4722
conv_287
Stojadinović M, Burazer L, Ercili-Cura D, Sancho A, Buchert J, Ćirković-Veličković T, Stanić-Vučinić D. One-step method for isolation and purification of native beta-lactoglobulin from bovine whey. in Journal of the Science of Food and Agriculture. 2012;92(7):1432-1440.
doi:10.1002/jsfa.4722
conv_287 .
Stojadinović, Marija, Burazer, Lidija, Ercili-Cura, Dilek, Sancho, Ana, Buchert, Johanna, Ćirković-Veličković, Tanja, Stanić-Vučinić, Dragana, "One-step method for isolation and purification of native beta-lactoglobulin from bovine whey" in Journal of the Science of Food and Agriculture, 92, no. 7 (2012):1432-1440,
https://doi.org/10.1002/jsfa.4722 .,
conv_287 .
23
21
21

Evaluation of IgE reactivity of active and thermally inactivated actinidin, a biomarker of kiwifruit allergy

Grozdanović, Milica; Popović, Milica; Polović, Natalija; Burazer, Lidija; Vučković, Olga; Atanasković-Marković, Marina; Lindner, Buko; Petersen, Arnd; Gavrović-Jankulović, Marija

(Pergamon-Elsevier Science Ltd, Oxford, 2012)

TY  - JOUR
AU  - Grozdanović, Milica
AU  - Popović, Milica
AU  - Polović, Natalija
AU  - Burazer, Lidija
AU  - Vučković, Olga
AU  - Atanasković-Marković, Marina
AU  - Lindner, Buko
AU  - Petersen, Arnd
AU  - Gavrović-Jankulović, Marija
PY  - 2012
UR  - http://intor.torlakinstitut.com/handle/123456789/358
AB  - Actinidin, an abundant cysteine protease from kiwifruit, is a specific biomarker of isolated allergy to kiwifruit. This study evaluates the IgE-binding properties of biologically active and thermally inactivated actinidin. Employing two different activity assays (caseinolytic assay and zymogram with gelatin) we showed that actinidin obtained from kiwifruit extract under native conditions represents a mixture of inactive and active enzyme. The structural integrity of actinidin was confirmed by SDS-PAGE. Edman degradation, mass fingerprint and Western blot with polyclonal antibodies. Although it was capable of inducing positive skin prick test reactions, we failed to detect IgE reactivity of active actinidin in Western blot with patient sera. Thermally inactivated actinidin exhibited IgE reactivity both in vivo and in vitro, indicating that heat processed kiwifruit products may induce clinical reactivity. These findings imply that apart from the allergenic epitopes on its surface, actinidin also contains hidden epitopes inside the protein which become accessible to IgE upon thermal treatment. (C) 2011 Elsevier Ltd. All rights reserved.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Food and Chemical Toxicology
T1  - Evaluation of IgE reactivity of active and thermally inactivated actinidin, a biomarker of kiwifruit allergy
EP  - 1018
IS  - 3-4
SP  - 1013
VL  - 50
DO  - 10.1016/j.fct.2011.12.030
UR  - conv_290
ER  - 
@article{
author = "Grozdanović, Milica and Popović, Milica and Polović, Natalija and Burazer, Lidija and Vučković, Olga and Atanasković-Marković, Marina and Lindner, Buko and Petersen, Arnd and Gavrović-Jankulović, Marija",
year = "2012",
abstract = "Actinidin, an abundant cysteine protease from kiwifruit, is a specific biomarker of isolated allergy to kiwifruit. This study evaluates the IgE-binding properties of biologically active and thermally inactivated actinidin. Employing two different activity assays (caseinolytic assay and zymogram with gelatin) we showed that actinidin obtained from kiwifruit extract under native conditions represents a mixture of inactive and active enzyme. The structural integrity of actinidin was confirmed by SDS-PAGE. Edman degradation, mass fingerprint and Western blot with polyclonal antibodies. Although it was capable of inducing positive skin prick test reactions, we failed to detect IgE reactivity of active actinidin in Western blot with patient sera. Thermally inactivated actinidin exhibited IgE reactivity both in vivo and in vitro, indicating that heat processed kiwifruit products may induce clinical reactivity. These findings imply that apart from the allergenic epitopes on its surface, actinidin also contains hidden epitopes inside the protein which become accessible to IgE upon thermal treatment. (C) 2011 Elsevier Ltd. All rights reserved.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Food and Chemical Toxicology",
title = "Evaluation of IgE reactivity of active and thermally inactivated actinidin, a biomarker of kiwifruit allergy",
pages = "1018-1013",
number = "3-4",
volume = "50",
doi = "10.1016/j.fct.2011.12.030",
url = "conv_290"
}
Grozdanović, M., Popović, M., Polović, N., Burazer, L., Vučković, O., Atanasković-Marković, M., Lindner, B., Petersen, A.,& Gavrović-Jankulović, M.. (2012). Evaluation of IgE reactivity of active and thermally inactivated actinidin, a biomarker of kiwifruit allergy. in Food and Chemical Toxicology
Pergamon-Elsevier Science Ltd, Oxford., 50(3-4), 1013-1018.
https://doi.org/10.1016/j.fct.2011.12.030
conv_290
Grozdanović M, Popović M, Polović N, Burazer L, Vučković O, Atanasković-Marković M, Lindner B, Petersen A, Gavrović-Jankulović M. Evaluation of IgE reactivity of active and thermally inactivated actinidin, a biomarker of kiwifruit allergy. in Food and Chemical Toxicology. 2012;50(3-4):1013-1018.
doi:10.1016/j.fct.2011.12.030
conv_290 .
Grozdanović, Milica, Popović, Milica, Polović, Natalija, Burazer, Lidija, Vučković, Olga, Atanasković-Marković, Marina, Lindner, Buko, Petersen, Arnd, Gavrović-Jankulović, Marija, "Evaluation of IgE reactivity of active and thermally inactivated actinidin, a biomarker of kiwifruit allergy" in Food and Chemical Toxicology, 50, no. 3-4 (2012):1013-1018,
https://doi.org/10.1016/j.fct.2011.12.030 .,
conv_290 .
22
19
24

Erratum: Complementary-DNA (cDNA): (Journal of the Serbian Chemical Society (2012) 77:1 (257-258))

Abughren, Mohamed; Popović, Milica; Dimitrijević, Rajna; Burazer, Lidija; Grozdanović, Milica; Atanasković-Marković, Marina; Gavrović-Jankulović, Marija

(Srpsko hemijsko društvo, Beograd, 2012)

TY  - JOUR
AU  - Abughren, Mohamed
AU  - Popović, Milica
AU  - Dimitrijević, Rajna
AU  - Burazer, Lidija
AU  - Grozdanović, Milica
AU  - Atanasković-Marković, Marina
AU  - Gavrović-Jankulović, Marija
PY  - 2012
UR  - http://intor.torlakinstitut.com/handle/123456789/365
PB  - Srpsko hemijsko društvo, Beograd
T2  - Journal of the Serbian Chemical Society
T1  - Erratum: Complementary-DNA (cDNA): (Journal of the Serbian Chemical Society (2012) 77:1 (257-258))
EP  - 258
IS  - 2
SP  - 257
VL  - 77
UR  - conv_590
ER  - 
@article{
author = "Abughren, Mohamed and Popović, Milica and Dimitrijević, Rajna and Burazer, Lidija and Grozdanović, Milica and Atanasković-Marković, Marina and Gavrović-Jankulović, Marija",
year = "2012",
publisher = "Srpsko hemijsko društvo, Beograd",
journal = "Journal of the Serbian Chemical Society",
title = "Erratum: Complementary-DNA (cDNA): (Journal of the Serbian Chemical Society (2012) 77:1 (257-258))",
pages = "258-257",
number = "2",
volume = "77",
url = "conv_590"
}
Abughren, M., Popović, M., Dimitrijević, R., Burazer, L., Grozdanović, M., Atanasković-Marković, M.,& Gavrović-Jankulović, M.. (2012). Erratum: Complementary-DNA (cDNA): (Journal of the Serbian Chemical Society (2012) 77:1 (257-258)). in Journal of the Serbian Chemical Society
Srpsko hemijsko društvo, Beograd., 77(2), 257-258.
conv_590
Abughren M, Popović M, Dimitrijević R, Burazer L, Grozdanović M, Atanasković-Marković M, Gavrović-Jankulović M. Erratum: Complementary-DNA (cDNA): (Journal of the Serbian Chemical Society (2012) 77:1 (257-258)). in Journal of the Serbian Chemical Society. 2012;77(2):257-258.
conv_590 .
Abughren, Mohamed, Popović, Milica, Dimitrijević, Rajna, Burazer, Lidija, Grozdanović, Milica, Atanasković-Marković, Marina, Gavrović-Jankulović, Marija, "Erratum: Complementary-DNA (cDNA): (Journal of the Serbian Chemical Society (2012) 77:1 (257-258))" in Journal of the Serbian Chemical Society, 77, no. 2 (2012):257-258,
conv_590 .

Impact of Dermatophagoides pteronyssinus mite body raw material on house dust mite allergy diagnosis in a Serbian population

Burazer, Lidija; Milovanović, K.; Milovanović, Mina; Vučković, Olga; Ćirković-Veličković, Tanja; Gavrović-Jankulović, Marija

(Wiley, Hoboken, 2011)

TY  - JOUR
AU  - Burazer, Lidija
AU  - Milovanović, K.
AU  - Milovanović, Mina
AU  - Vučković, Olga
AU  - Ćirković-Veličković, Tanja
AU  - Gavrović-Jankulović, Marija
PY  - 2011
UR  - http://intor.torlakinstitut.com/handle/123456789/320
AB  - House dust mite (HDM) allergy has different clinical and immunological patterns in different geographic regions. The impact of raw material of commercial Dermatophadoides pteronyssinus (Acari: Pyroglyphidae) mite bodies on the quality of allergen extracts for allergy diagnosis in the Serbian population has not been previously evaluated. House dust mite bodies obtained from manufacturers in Europe, South America and Australia were used in the preparation of allergen extracts for in vivo diagnosis and serological analysis in a group of 14 HDM-allergic adults. In the group of mite-allergic patients, there was no statistically significant difference in skin test reactivity (Wilcoxon matched pairs test) among the three HDM body extract preparations. In a CAP inhibition assay, two extracts (A and C) achieved maximum inhibition of  gt  90%, whereas extract B demonstrated a different inhibition slope and lower inhibition potential (80%). However, a remarkable difference in immunoglobulin E reactivity using Western blot analysis with individual patients' sera was observed in one of the preparations (extract B). These findings emphasize the need for the careful selection of starting material for the preparation of HDM diagnostic reagents intended for use in patients from geographically distinct regions as these preparations can have implications on the selection criteria for patient-tailored immunotherapy of HDM allergy.
PB  - Wiley, Hoboken
T2  - Medical and Veterinary Entomology
T1  - Impact of Dermatophagoides pteronyssinus mite body raw material on house dust mite allergy diagnosis in a Serbian population
EP  - 83
IS  - 1
SP  - 77
VL  - 25
DO  - 10.1111/j.1365-2915.2010.00906.x
UR  - conv_262
ER  - 
@article{
author = "Burazer, Lidija and Milovanović, K. and Milovanović, Mina and Vučković, Olga and Ćirković-Veličković, Tanja and Gavrović-Jankulović, Marija",
year = "2011",
abstract = "House dust mite (HDM) allergy has different clinical and immunological patterns in different geographic regions. The impact of raw material of commercial Dermatophadoides pteronyssinus (Acari: Pyroglyphidae) mite bodies on the quality of allergen extracts for allergy diagnosis in the Serbian population has not been previously evaluated. House dust mite bodies obtained from manufacturers in Europe, South America and Australia were used in the preparation of allergen extracts for in vivo diagnosis and serological analysis in a group of 14 HDM-allergic adults. In the group of mite-allergic patients, there was no statistically significant difference in skin test reactivity (Wilcoxon matched pairs test) among the three HDM body extract preparations. In a CAP inhibition assay, two extracts (A and C) achieved maximum inhibition of  gt  90%, whereas extract B demonstrated a different inhibition slope and lower inhibition potential (80%). However, a remarkable difference in immunoglobulin E reactivity using Western blot analysis with individual patients' sera was observed in one of the preparations (extract B). These findings emphasize the need for the careful selection of starting material for the preparation of HDM diagnostic reagents intended for use in patients from geographically distinct regions as these preparations can have implications on the selection criteria for patient-tailored immunotherapy of HDM allergy.",
publisher = "Wiley, Hoboken",
journal = "Medical and Veterinary Entomology",
title = "Impact of Dermatophagoides pteronyssinus mite body raw material on house dust mite allergy diagnosis in a Serbian population",
pages = "83-77",
number = "1",
volume = "25",
doi = "10.1111/j.1365-2915.2010.00906.x",
url = "conv_262"
}
Burazer, L., Milovanović, K., Milovanović, M., Vučković, O., Ćirković-Veličković, T.,& Gavrović-Jankulović, M.. (2011). Impact of Dermatophagoides pteronyssinus mite body raw material on house dust mite allergy diagnosis in a Serbian population. in Medical and Veterinary Entomology
Wiley, Hoboken., 25(1), 77-83.
https://doi.org/10.1111/j.1365-2915.2010.00906.x
conv_262
Burazer L, Milovanović K, Milovanović M, Vučković O, Ćirković-Veličković T, Gavrović-Jankulović M. Impact of Dermatophagoides pteronyssinus mite body raw material on house dust mite allergy diagnosis in a Serbian population. in Medical and Veterinary Entomology. 2011;25(1):77-83.
doi:10.1111/j.1365-2915.2010.00906.x
conv_262 .
Burazer, Lidija, Milovanović, K., Milovanović, Mina, Vučković, Olga, Ćirković-Veličković, Tanja, Gavrović-Jankulović, Marija, "Impact of Dermatophagoides pteronyssinus mite body raw material on house dust mite allergy diagnosis in a Serbian population" in Medical and Veterinary Entomology, 25, no. 1 (2011):77-83,
https://doi.org/10.1111/j.1365-2915.2010.00906.x .,
conv_262 .
6
6
9