TY  - JOUR
AU  - Dragačević, Luka
AU  - Lopandić, Zorana
AU  - Gavrović-Jankulović, Marija
AU  - Živković, Irena
AU  - Blagojević, Veljko
AU  - Polović, Natalija
AU  - Minić, Rajna
PY  - 2022
UR  - http://intor.torlakinstitut.com/handle/123456789/621
AB  - The surface of microorganisms is covered with carbohydrates, which makes them unique, self-sustaining glycan probes. Lectins are able to bind to these probes, and this interaction can be exploited for selecting microorganisms or novel lectins. To examine lectin-microorganism interactions, we have previously developed an enzyme-linked lectin sorbent assay (ELLSA) with whole bacterial cells. To further test the validity of this methodology, here we compare it with flow cytometry. For this purpose, we used biotinylated recombinantly produced lectin from Musa acuminata (BanLec), this lectin’s recombinantly produced chimera with green fluorescent protein (BanLec-eGFP) and a lectin from Ricinus communis (RCA120), both biotinylated and FITC labeled. Parallel testing showed equivalent results for the two methods, in terms of the presence or absence of binding, with signal intensity yielding high Pearson correlation coefficient of 0.8 for BanLec and 0.95 for RCA120. The ELLSA method demonstrated multiple advantages, such as reliability and convenience for high-throughput analysis; it also required less lectin and yielded more consistent results. As such, ELLSA proved to be a useful tool for profiling microbial glycan structures or testing novel lectins.
PB  - Springer
T2  - Applied Biochemistry and Biotechnology
T1  - Comparison of Enzyme-Linked Lectin Sorbent Assay and Flow Cytometry for Profiling Microbial Glycans
EP  - 2060
SP  - 2047
VL  - 194
DO  - 10.1007/s12010-021-03772-w
ER  - 

@article{
author = "Dragačević, Luka and Lopandić, Zorana and Gavrović-Jankulović, Marija and Živković, Irena and Blagojević, Veljko and Polović, Natalija and Minić, Rajna",
year = "2022",
abstract = "The surface of microorganisms is covered with carbohydrates, which makes them unique, self-sustaining glycan probes. Lectins are able to bind to these probes, and this interaction can be exploited for selecting microorganisms or novel lectins. To examine lectin-microorganism interactions, we have previously developed an enzyme-linked lectin sorbent assay (ELLSA) with whole bacterial cells. To further test the validity of this methodology, here we compare it with flow cytometry. For this purpose, we used biotinylated recombinantly produced lectin from Musa acuminata (BanLec), this lectin’s recombinantly produced chimera with green fluorescent protein (BanLec-eGFP) and a lectin from Ricinus communis (RCA120), both biotinylated and FITC labeled. Parallel testing showed equivalent results for the two methods, in terms of the presence or absence of binding, with signal intensity yielding high Pearson correlation coefficient of 0.8 for BanLec and 0.95 for RCA120. The ELLSA method demonstrated multiple advantages, such as reliability and convenience for high-throughput analysis; it also required less lectin and yielded more consistent results. As such, ELLSA proved to be a useful tool for profiling microbial glycan structures or testing novel lectins.",
publisher = "Springer",
journal = "Applied Biochemistry and Biotechnology",
title = "Comparison of Enzyme-Linked Lectin Sorbent Assay and Flow Cytometry for Profiling Microbial Glycans",
pages = "2060-2047",
volume = "194",
doi = "10.1007/s12010-021-03772-w"
}

Dragačević, L., Lopandić, Z., Gavrović-Jankulović, M., Živković, I., Blagojević, V., Polović, N.,& Minić, R.. (2022). Comparison of Enzyme-Linked Lectin Sorbent Assay and Flow Cytometry for Profiling Microbial Glycans. in Applied Biochemistry and Biotechnology
Springer., 194, 2047-2060.
https://doi.org/10.1007/s12010-021-03772-w

Dragačević L, Lopandić Z, Gavrović-Jankulović M, Živković I, Blagojević V, Polović N, Minić R. Comparison of Enzyme-Linked Lectin Sorbent Assay and Flow Cytometry for Profiling Microbial Glycans. in Applied Biochemistry and Biotechnology. 2022;194:2047-2060.
doi:10.1007/s12010-021-03772-w .

Dragačević, Luka, Lopandić, Zorana, Gavrović-Jankulović, Marija, Živković, Irena, Blagojević, Veljko, Polović, Natalija, Minić, Rajna, "Comparison of Enzyme-Linked Lectin Sorbent Assay and Flow Cytometry for Profiling Microbial Glycans" in Applied Biochemistry and Biotechnology, 194 (2022):2047-2060,
https://doi.org/10.1007/s12010-021-03772-w . .

TY  - JOUR
AU  - Protić-Rosić, Isidora
AU  - Nešić, Andrijana
AU  - Lukić, Ivana
AU  - Miljković, Radmila
AU  - Popović, Dragan
AU  - Atanasković-Marković, Marina
AU  - Stojanović, Marijana
AU  - Gavrović-Jankulović, Marija
PY  - 2021
UR  - http://intor.torlakinstitut.com/handle/123456789/630
AB  - Allergen-specific immunotherapy (AIT) is a desensitizing treatment for allergic diseases that corrects the underlined pathological immune response to innocuous protein antigens, called allergens. Recombinant allergens employed in the AIT allowed the production of well-defined formulations that possessed consistent quality but were often less efficient than natural allergen extracts. Combining recombinant allergens with an adjuvant or immunomodulatory agent could improve AIT efficacy. This study aimed to perform structural and functional characterization of newly designed recombinant chimera composed of the Bet v 1, the major birch pollen allergen, and Banana Lectin (BanLec), TLR2, and CD14 binding protein, for the application in AIT. rBet v 1-BanLec chimera was designed in silico and expressed as a soluble fraction in Escherichia coli. Purified rBet v 1-BanLec (33.4 kDa) retained BanLec-associated biological activity of carbohydrate-binding and preserved IgE reactive epitopes of Bet v 1. The chimera revealed secondary structures with predominant β sheets. The immunomodulatory capacity of rBet v 1-BanLec tested on macrophages showed changes in myeloperoxidase activity, reduced NO production, and significant alterations in the production of cytokines when compared to both rBanLec and rBet v 1. Comparing to rBet v 1, rBet v 1-BanLec was demonstrated to be more efficient promoter of IL-10 production as well as weaker inducer of NO production and secretion of pro-inflammatory cytokines TNFα, and IL-6. The ability of rBet v 1-BanLec to promote IL-10 in together with the preserved 3D structure of Bet v 1 part implies that the construct might exert a beneficial effect in the allergen-specific immunotherapy.
PB  - Elsevier
T2  - Molecular Immunology
T1  - Recombinant Bet v 1-BanLec chimera modulates functional characteristics of peritoneal murine macrophages by promoting IL-10 secretion
EP  - 67
SP  - 58
VL  - 138
DO  - 10.1016/j.molimm.2021.06.015
ER  - 

@article{
author = "Protić-Rosić, Isidora and Nešić, Andrijana and Lukić, Ivana and Miljković, Radmila and Popović, Dragan and Atanasković-Marković, Marina and Stojanović, Marijana and Gavrović-Jankulović, Marija",
year = "2021",
abstract = "Allergen-specific immunotherapy (AIT) is a desensitizing treatment for allergic diseases that corrects the underlined pathological immune response to innocuous protein antigens, called allergens. Recombinant allergens employed in the AIT allowed the production of well-defined formulations that possessed consistent quality but were often less efficient than natural allergen extracts. Combining recombinant allergens with an adjuvant or immunomodulatory agent could improve AIT efficacy. This study aimed to perform structural and functional characterization of newly designed recombinant chimera composed of the Bet v 1, the major birch pollen allergen, and Banana Lectin (BanLec), TLR2, and CD14 binding protein, for the application in AIT. rBet v 1-BanLec chimera was designed in silico and expressed as a soluble fraction in Escherichia coli. Purified rBet v 1-BanLec (33.4 kDa) retained BanLec-associated biological activity of carbohydrate-binding and preserved IgE reactive epitopes of Bet v 1. The chimera revealed secondary structures with predominant β sheets. The immunomodulatory capacity of rBet v 1-BanLec tested on macrophages showed changes in myeloperoxidase activity, reduced NO production, and significant alterations in the production of cytokines when compared to both rBanLec and rBet v 1. Comparing to rBet v 1, rBet v 1-BanLec was demonstrated to be more efficient promoter of IL-10 production as well as weaker inducer of NO production and secretion of pro-inflammatory cytokines TNFα, and IL-6. The ability of rBet v 1-BanLec to promote IL-10 in together with the preserved 3D structure of Bet v 1 part implies that the construct might exert a beneficial effect in the allergen-specific immunotherapy.",
publisher = "Elsevier",
journal = "Molecular Immunology",
title = "Recombinant Bet v 1-BanLec chimera modulates functional characteristics of peritoneal murine macrophages by promoting IL-10 secretion",
pages = "67-58",
volume = "138",
doi = "10.1016/j.molimm.2021.06.015"
}

Protić-Rosić, I., Nešić, A., Lukić, I., Miljković, R., Popović, D., Atanasković-Marković, M., Stojanović, M.,& Gavrović-Jankulović, M.. (2021). Recombinant Bet v 1-BanLec chimera modulates functional characteristics of peritoneal murine macrophages by promoting IL-10 secretion. in Molecular Immunology
Elsevier., 138, 58-67.
https://doi.org/10.1016/j.molimm.2021.06.015

Protić-Rosić I, Nešić A, Lukić I, Miljković R, Popović D, Atanasković-Marković M, Stojanović M, Gavrović-Jankulović M. Recombinant Bet v 1-BanLec chimera modulates functional characteristics of peritoneal murine macrophages by promoting IL-10 secretion. in Molecular Immunology. 2021;138:58-67.
doi:10.1016/j.molimm.2021.06.015 .

Protić-Rosić, Isidora, Nešić, Andrijana, Lukić, Ivana, Miljković, Radmila, Popović, Dragan, Atanasković-Marković, Marina, Stojanović, Marijana, Gavrović-Jankulović, Marija, "Recombinant Bet v 1-BanLec chimera modulates functional characteristics of peritoneal murine macrophages by promoting IL-10 secretion" in Molecular Immunology, 138 (2021):58-67,
https://doi.org/10.1016/j.molimm.2021.06.015 . .

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
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"
}

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

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 .

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 . .

TY  - JOUR
AU  - Dragačević, Luka
AU  - Đorđević, Brižita
AU  - Gavrović-Jankulović, Marija
AU  - Ilić, Vesna
AU  - Kanazir, Danijela
AU  - Minić, Rajna
PY  - 2020
UR  - http://intor.torlakinstitut.com/handle/123456789/563
AB  - The surface of microorganisms is covered with polysaccharide structures which are in immediate contact with receptor structures on host's cells and antibodies. The interaction between microorganisms and their host is dependent on surface glycosylation and in this study we have tested the interaction of plant lectins with different microorganisms. Enzyme-linked lectin sorbent assay - ELLSA was used to test the binding of recombinant Musa acuminata lectin - BL to 27 selected microorganisms and 7 other lectins were used for comparison: Soy bean agglutinin - SBA, Lens culinaris lectin - LCA, Wheat germ agglutinin - WGA, RCA(120) - Ricinus communis agglutinin, Con A - from Canavalia ensiformis, Sambucus nigra agglutinin - SNA I and Maackia amurensis agglutinin - MAA. The goal was to define the microorganisms' surface glycosylation by means of interaction with the selected plant lectins and to make a comparison with BL. Among the tested lectins most selective binding was observed for RCA(120) which preferentially bound Lactobacillus casei DG. Recombinant banana lectin showed specific binding to all of the tested fungal species. The binding of BL to Candida albicans was further tested with fluorescence microscopy and flow cytometry and it was concluded that this lectin can differentiate ss-glucan rich surfaces. The binding of BL to S. boulardii could be inhibited with ss-glucan from yeast with IC50 1.81 mu g mL(-1) and to P. roqueforti with 1.10 mu g mL(-1). This unique specificity of BL could be exploited for screening purposes and potentially for the detection of ss-glucan in solutions.
PB  - Springer, Dordrecht
T2  - Glycoconjugate Journal
T1  - ELLSA based profiling of surface glycosylation in microorganisms reveals that ss-glucan rich yeasts' surfaces are selectively recognized with recombinant banana lectin
EP  - 105
IS  - 1
SP  - 95
VL  - 37
DO  - 10.1007/s10719-019-09898-8
ER  - 

@article{
author = "Dragačević, Luka and Đorđević, Brižita and Gavrović-Jankulović, Marija and Ilić, Vesna and Kanazir, Danijela and Minić, Rajna",
year = "2020",
abstract = "The surface of microorganisms is covered with polysaccharide structures which are in immediate contact with receptor structures on host's cells and antibodies. The interaction between microorganisms and their host is dependent on surface glycosylation and in this study we have tested the interaction of plant lectins with different microorganisms. Enzyme-linked lectin sorbent assay - ELLSA was used to test the binding of recombinant Musa acuminata lectin - BL to 27 selected microorganisms and 7 other lectins were used for comparison: Soy bean agglutinin - SBA, Lens culinaris lectin - LCA, Wheat germ agglutinin - WGA, RCA(120) - Ricinus communis agglutinin, Con A - from Canavalia ensiformis, Sambucus nigra agglutinin - SNA I and Maackia amurensis agglutinin - MAA. The goal was to define the microorganisms' surface glycosylation by means of interaction with the selected plant lectins and to make a comparison with BL. Among the tested lectins most selective binding was observed for RCA(120) which preferentially bound Lactobacillus casei DG. Recombinant banana lectin showed specific binding to all of the tested fungal species. The binding of BL to Candida albicans was further tested with fluorescence microscopy and flow cytometry and it was concluded that this lectin can differentiate ss-glucan rich surfaces. The binding of BL to S. boulardii could be inhibited with ss-glucan from yeast with IC50 1.81 mu g mL(-1) and to P. roqueforti with 1.10 mu g mL(-1). This unique specificity of BL could be exploited for screening purposes and potentially for the detection of ss-glucan in solutions.",
publisher = "Springer, Dordrecht",
journal = "Glycoconjugate Journal",
title = "ELLSA based profiling of surface glycosylation in microorganisms reveals that ss-glucan rich yeasts' surfaces are selectively recognized with recombinant banana lectin",
pages = "105-95",
number = "1",
volume = "37",
doi = "10.1007/s10719-019-09898-8"
}

Dragačević, L., Đorđević, B., Gavrović-Jankulović, M., Ilić, V., Kanazir, D.,& Minić, R.. (2020). ELLSA based profiling of surface glycosylation in microorganisms reveals that ss-glucan rich yeasts' surfaces are selectively recognized with recombinant banana lectin. in Glycoconjugate Journal
Springer, Dordrecht., 37(1), 95-105.
https://doi.org/10.1007/s10719-019-09898-8

Dragačević L, Đorđević B, Gavrović-Jankulović M, Ilić V, Kanazir D, Minić R. ELLSA based profiling of surface glycosylation in microorganisms reveals that ss-glucan rich yeasts' surfaces are selectively recognized with recombinant banana lectin. in Glycoconjugate Journal. 2020;37(1):95-105.
doi:10.1007/s10719-019-09898-8 .

Dragačević, Luka, Đorđević, Brižita, Gavrović-Jankulović, Marija, Ilić, Vesna, Kanazir, Danijela, Minić, Rajna, "ELLSA based profiling of surface glycosylation in microorganisms reveals that ss-glucan rich yeasts' surfaces are selectively recognized with recombinant banana lectin" in Glycoconjugate Journal, 37, no. 1 (2020):95-105,
https://doi.org/10.1007/s10719-019-09898-8 . .

TY  - CONF
AU  - Dragačević, Luka
AU  - Đorđević, Brižita
AU  - Gavrović-Jankulović, Marija
AU  - Ilić, Vesna
AU  - Minić, Rajna
PY  - 2020
UR  - http://intor.torlakinstitut.com/handle/123456789/567
PB  - Lippincott Williams & Wilkins, Philadelphia
C3  - Journal of Clinical Gastroenterology
T1  - Typing of Surface Glycosilation of Microorganisms by Lectins with in House Elisa
EP  - S13
SP  - S13
VL  - 54
UR  - https://hdl.handle.net/21.15107/rcub_intor_567
ER  - 

@conference{
author = "Dragačević, Luka and Đorđević, Brižita and Gavrović-Jankulović, Marija and Ilić, Vesna and Minić, Rajna",
year = "2020",
publisher = "Lippincott Williams & Wilkins, Philadelphia",
journal = "Journal of Clinical Gastroenterology",
title = "Typing of Surface Glycosilation of Microorganisms by Lectins with in House Elisa",
pages = "S13-S13",
volume = "54",
url = "https://hdl.handle.net/21.15107/rcub_intor_567"
}

Dragačević, L., Đorđević, B., Gavrović-Jankulović, M., Ilić, V.,& Minić, R.. (2020). Typing of Surface Glycosilation of Microorganisms by Lectins with in House Elisa. in Journal of Clinical Gastroenterology
Lippincott Williams & Wilkins, Philadelphia., 54, S13-S13.
https://hdl.handle.net/21.15107/rcub_intor_567

Dragačević L, Đorđević B, Gavrović-Jankulović M, Ilić V, Minić R. Typing of Surface Glycosilation of Microorganisms by Lectins with in House Elisa. in Journal of Clinical Gastroenterology. 2020;54:S13-S13.
https://hdl.handle.net/21.15107/rcub_intor_567 .

Dragačević, Luka, Đorđević, Brižita, Gavrović-Jankulović, Marija, Ilić, Vesna, Minić, Rajna, "Typing of Surface Glycosilation of Microorganisms by Lectins with in House Elisa" in Journal of Clinical Gastroenterology, 54 (2020):S13-S13,
https://hdl.handle.net/21.15107/rcub_intor_567 .

TY  - JOUR
AU  - Mrkić, Ivan
AU  - Minić, Rajna
AU  - Popović, Dragan
AU  - Živković, Irena
AU  - Gavrović-Jankulović, Marija
PY  - 2018
UR  - http://intor.torlakinstitut.com/handle/123456789/515
AB  - Aim To investigate the immunomodulatory potential of a chimera composed of the receptor-binding domain of hemagglutinin 1 (H1s) from Influenza virus and Der p 2 (D2) allergen for allergen-specific immunotherapy of house-dust mite allergy (HDM). Main methods: H1sD2 chimera and D2 allergen were produced by genetic engineering in E. coli. Recombinant antigens were extracted from inclusion bodies by urea, then refolded and purified by immobilized-metal affinity chromatography (IMAC). Purity was verified by 2D-PAGE and secondary structures were assessed by CD spectroscopy. IgE reactivity of H1sD2 and D2 was tested in western blot with sera from 8 persons with clinical history of HDM allergy. Immunogenicity of H1sD2 and D2 were analyzed in Balb/c mice. Cytokine profile was analyzed by ELISA after stimulation of mouse spleen cells with H1sD2 and D2. Leukocyte population abundance of cells isolated from spleen and lymph node was assessed by flow cytometry. Key findings: Purified recombinant proteins H1sD2 (42 kDa) and D2 (15 kDa) revealed well defined secondary structures, and preserved IgE reactive epitopes. Analysis of supernatants of mouse spleen cells after stimulation with H1sD2 and D2, revealed a qualitatively different cytokine profile from H1sD2 immunized mouse cells (increase in IL10). CD8+ cells were decreased in the lymph node of D2 immunized mice, whereas H1sD2 immunization led to an increase of CD8+ cells in both the lymph node and the spleen. Significance: H1sD2 chimera attenuates Der p 2-inherent Th2 response and directs the immune response toward Th1 and Treg phenotype.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Life Sciences
T1  - Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy
EP  - 165
SP  - 158
VL  - 213
DO  - 10.1016/j.lfs.2018.10.036
ER  - 

@article{
author = "Mrkić, Ivan and Minić, Rajna and Popović, Dragan and Živković, Irena and Gavrović-Jankulović, Marija",
year = "2018",
abstract = "Aim To investigate the immunomodulatory potential of a chimera composed of the receptor-binding domain of hemagglutinin 1 (H1s) from Influenza virus and Der p 2 (D2) allergen for allergen-specific immunotherapy of house-dust mite allergy (HDM). Main methods: H1sD2 chimera and D2 allergen were produced by genetic engineering in E. coli. Recombinant antigens were extracted from inclusion bodies by urea, then refolded and purified by immobilized-metal affinity chromatography (IMAC). Purity was verified by 2D-PAGE and secondary structures were assessed by CD spectroscopy. IgE reactivity of H1sD2 and D2 was tested in western blot with sera from 8 persons with clinical history of HDM allergy. Immunogenicity of H1sD2 and D2 were analyzed in Balb/c mice. Cytokine profile was analyzed by ELISA after stimulation of mouse spleen cells with H1sD2 and D2. Leukocyte population abundance of cells isolated from spleen and lymph node was assessed by flow cytometry. Key findings: Purified recombinant proteins H1sD2 (42 kDa) and D2 (15 kDa) revealed well defined secondary structures, and preserved IgE reactive epitopes. Analysis of supernatants of mouse spleen cells after stimulation with H1sD2 and D2, revealed a qualitatively different cytokine profile from H1sD2 immunized mouse cells (increase in IL10). CD8+ cells were decreased in the lymph node of D2 immunized mice, whereas H1sD2 immunization led to an increase of CD8+ cells in both the lymph node and the spleen. Significance: H1sD2 chimera attenuates Der p 2-inherent Th2 response and directs the immune response toward Th1 and Treg phenotype.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Life Sciences",
title = "Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy",
pages = "165-158",
volume = "213",
doi = "10.1016/j.lfs.2018.10.036"
}

Mrkić, I., Minić, R., Popović, D., Živković, I.,& Gavrović-Jankulović, M.. (2018). Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy. in Life Sciences
Pergamon-Elsevier Science Ltd, Oxford., 213, 158-165.
https://doi.org/10.1016/j.lfs.2018.10.036

Mrkić I, Minić R, Popović D, Živković I, Gavrović-Jankulović M. Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy. in Life Sciences. 2018;213:158-165.
doi:10.1016/j.lfs.2018.10.036 .

Mrkić, Ivan, Minić, Rajna, Popović, Dragan, Živković, Irena, Gavrović-Jankulović, Marija, "Newly designed hemagglutinin-Der p 2 chimera is a potential candidate for allergen specific immunotherapy" in Life Sciences, 213 (2018):158-165,
https://doi.org/10.1016/j.lfs.2018.10.036 . .

TY  - JOUR
AU  - Marinković, Emilija
AU  - Đokić, Radmila
AU  - Lukić, Ivana
AU  - Filipović, Ana
AU  - Inić-Kanada, Aleksandra
AU  - Kosanović, Dejana
AU  - Gavrović-Jankulović, Marija
AU  - Stojanović, Marijana
PY  - 2017
UR  - http://intor.torlakinstitut.com/handle/123456789/493
AB  - We demonstrated that a recombinant banana lectin (rBanLec), which structural characteristics and physiological impacts highly resemble those reported for its natural counterparts, binds murine peritoneal macrophages and specifically modulates their functional characteristics. By using rBanLec in concentrations ranging from 1 mu g to 10 mu g to stimulate resident (RMs) and thioglycollate-elicited (TGMs) peritoneal macrophages from BALB/c and C57BL/6 mice, we have shown that effects of rBanLec stimulation depend on its concentration but also on the functional status of macrophages and their genetic background. rBanLec, in a positive dose-dependent manner, promotes the proliferation of TGMs from both BALB/c and C57BL/6 mice, while its mitogenic influence on RMs is significantly lower (BALB/c mice) or not detectable (C57BL/6 mice). In all peritoneal macrophages, irrespective of their type and genetic background, rBanLec, in a positive dose dependent manner, enhances the secretion of IL-10. rBanLec stimulation of RMs from both BALB/c and C57BL/6 resulted in a positive dose-dependent promotion of proinflammatory phenotype (enhancement of NO production and IL-12 and TNF alpha secretion, reduction of arginase activity). Positive dose-dependent skewing toward proinflammatory phenotype was also observed in TGMs from C57BL/6 mice. However, the enhancement of rBanLec stimulation promotes skewing of TGMs from BALB/c mice towards anti-inflammatory profile (reduction of NO production and IL-12 secretion, enhancement of arginase activity and TGF alpha and IL-4 secretion). Moreover, we established that rBanLec binds oligosaccharide structures of TLR2 and CD14 and that blocking of signaling via these receptors significantly impairs the production of TNFa and NO in BALB/c macrophages. Since the outcome of rBanLec stimulation depends on rBanLec concentration as well as on the functional characteristics of its target cells and their genetic background, further studies are needed to investigate its effects under physiological and specific pathological conditions.
PB  - Public Library Science, San Francisco
T2  - PLoS One
T1  - Modulation of functional characteristics of resident and thioglycollate-elicited peritoneal murine macrophages by a recombinant banana lectin
IS  - 2
VL  - 12
DO  - 10.1371/journal.pone.0172469
ER  - 

@article{
author = "Marinković, Emilija and Đokić, Radmila and Lukić, Ivana and Filipović, Ana and Inić-Kanada, Aleksandra and Kosanović, Dejana and Gavrović-Jankulović, Marija and Stojanović, Marijana",
year = "2017",
abstract = "We demonstrated that a recombinant banana lectin (rBanLec), which structural characteristics and physiological impacts highly resemble those reported for its natural counterparts, binds murine peritoneal macrophages and specifically modulates their functional characteristics. By using rBanLec in concentrations ranging from 1 mu g to 10 mu g to stimulate resident (RMs) and thioglycollate-elicited (TGMs) peritoneal macrophages from BALB/c and C57BL/6 mice, we have shown that effects of rBanLec stimulation depend on its concentration but also on the functional status of macrophages and their genetic background. rBanLec, in a positive dose-dependent manner, promotes the proliferation of TGMs from both BALB/c and C57BL/6 mice, while its mitogenic influence on RMs is significantly lower (BALB/c mice) or not detectable (C57BL/6 mice). In all peritoneal macrophages, irrespective of their type and genetic background, rBanLec, in a positive dose dependent manner, enhances the secretion of IL-10. rBanLec stimulation of RMs from both BALB/c and C57BL/6 resulted in a positive dose-dependent promotion of proinflammatory phenotype (enhancement of NO production and IL-12 and TNF alpha secretion, reduction of arginase activity). Positive dose-dependent skewing toward proinflammatory phenotype was also observed in TGMs from C57BL/6 mice. However, the enhancement of rBanLec stimulation promotes skewing of TGMs from BALB/c mice towards anti-inflammatory profile (reduction of NO production and IL-12 secretion, enhancement of arginase activity and TGF alpha and IL-4 secretion). Moreover, we established that rBanLec binds oligosaccharide structures of TLR2 and CD14 and that blocking of signaling via these receptors significantly impairs the production of TNFa and NO in BALB/c macrophages. Since the outcome of rBanLec stimulation depends on rBanLec concentration as well as on the functional characteristics of its target cells and their genetic background, further studies are needed to investigate its effects under physiological and specific pathological conditions.",
publisher = "Public Library Science, San Francisco",
journal = "PLoS One",
title = "Modulation of functional characteristics of resident and thioglycollate-elicited peritoneal murine macrophages by a recombinant banana lectin",
number = "2",
volume = "12",
doi = "10.1371/journal.pone.0172469"
}

Marinković, E., Đokić, R., Lukić, I., Filipović, A., Inić-Kanada, A., Kosanović, D., Gavrović-Jankulović, M.,& Stojanović, M.. (2017). Modulation of functional characteristics of resident and thioglycollate-elicited peritoneal murine macrophages by a recombinant banana lectin. in PLoS One
Public Library Science, San Francisco., 12(2).
https://doi.org/10.1371/journal.pone.0172469

Marinković E, Đokić R, Lukić I, Filipović A, Inić-Kanada A, Kosanović D, Gavrović-Jankulović M, Stojanović M. Modulation of functional characteristics of resident and thioglycollate-elicited peritoneal murine macrophages by a recombinant banana lectin. in PLoS One. 2017;12(2).
doi:10.1371/journal.pone.0172469 .

Marinković, Emilija, Đokić, Radmila, Lukić, Ivana, Filipović, Ana, Inić-Kanada, Aleksandra, Kosanović, Dejana, Gavrović-Jankulović, Marija, Stojanović, Marijana, "Modulation of functional characteristics of resident and thioglycollate-elicited peritoneal murine macrophages by a recombinant banana lectin" in PLoS One, 12, no. 2 (2017),
https://doi.org/10.1371/journal.pone.0172469 . .

TY  - JOUR
AU  - Mrkić, Ivan
AU  - Minić, Rajna
AU  - Bulat, Tanja
AU  - Aradska, Jana
AU  - Atanasković-Marković, Marina
AU  - Drakulić, Branko
AU  - Gavrović-Jankulović, Marija
PY  - 2017
UR  - http://intor.torlakinstitut.com/handle/123456789/485
AB  - BACKGROUND: Group 1 and group 2 allergens from house dust mite are the major elicitors of respiratory allergic diseases and the main candidates for immunotherapy. RESULTS: The potential therapeutic role of a chimera composed of recombinant Der p 2 (D2) linked to Influenza A virus hemagglutinin 1 (H1) for intranasal application was created, expressed and tested in a mouse model. H1D2 and D2 were produced by genetic engineering in Escherichia coli and their primary structure was confirmed by mass fingerprint. Both antigens preserved IgE reactivity in immunoblot with serum from seven house dust mite allergic persons. Balb/c mice were sensitized with D2 allergen in alum and subsequently received H1D2 or D2, intranasally. The reduced levels of serum D2 specific IgE, together with the increased serum specific IgG and IgA were detected in both groups which received H1D2 and D2 intranasally. A higher level of effector CD4+CD25+ spleen lymphocytes was found only in the group of mice which received i.n. H1D2. CONCLUSION: H1D2 chimera can have therapeutic potential in Der p 2 allergic persons as dual vaccine which, beside protective allergen specific, can provide protective antibodies against Influenza A virus hemagglutinin 1. (C) 2016 Society of Chemical Industry
PB  - Wiley, Hoboken
T2  - Journal of Chemical Technology and Biotechnology
T1  - Modulation of the specific immune response in Balb/cmice by intranasal application of recombinant H1D2 chimera
EP  - 1335
IS  - 6
SP  - 1328
VL  - 92
DO  - 10.1002/jctb.5127
ER  - 

@article{
author = "Mrkić, Ivan and Minić, Rajna and Bulat, Tanja and Aradska, Jana and Atanasković-Marković, Marina and Drakulić, Branko and Gavrović-Jankulović, Marija",
year = "2017",
abstract = "BACKGROUND: Group 1 and group 2 allergens from house dust mite are the major elicitors of respiratory allergic diseases and the main candidates for immunotherapy. RESULTS: The potential therapeutic role of a chimera composed of recombinant Der p 2 (D2) linked to Influenza A virus hemagglutinin 1 (H1) for intranasal application was created, expressed and tested in a mouse model. H1D2 and D2 were produced by genetic engineering in Escherichia coli and their primary structure was confirmed by mass fingerprint. Both antigens preserved IgE reactivity in immunoblot with serum from seven house dust mite allergic persons. Balb/c mice were sensitized with D2 allergen in alum and subsequently received H1D2 or D2, intranasally. The reduced levels of serum D2 specific IgE, together with the increased serum specific IgG and IgA were detected in both groups which received H1D2 and D2 intranasally. A higher level of effector CD4+CD25+ spleen lymphocytes was found only in the group of mice which received i.n. H1D2. CONCLUSION: H1D2 chimera can have therapeutic potential in Der p 2 allergic persons as dual vaccine which, beside protective allergen specific, can provide protective antibodies against Influenza A virus hemagglutinin 1. (C) 2016 Society of Chemical Industry",
publisher = "Wiley, Hoboken",
journal = "Journal of Chemical Technology and Biotechnology",
title = "Modulation of the specific immune response in Balb/cmice by intranasal application of recombinant H1D2 chimera",
pages = "1335-1328",
number = "6",
volume = "92",
doi = "10.1002/jctb.5127"
}

Mrkić, I., Minić, R., Bulat, T., Aradska, J., Atanasković-Marković, M., Drakulić, B.,& Gavrović-Jankulović, M.. (2017). Modulation of the specific immune response in Balb/cmice by intranasal application of recombinant H1D2 chimera. in Journal of Chemical Technology and Biotechnology
Wiley, Hoboken., 92(6), 1328-1335.
https://doi.org/10.1002/jctb.5127

Mrkić I, Minić R, Bulat T, Aradska J, Atanasković-Marković M, Drakulić B, Gavrović-Jankulović M. Modulation of the specific immune response in Balb/cmice by intranasal application of recombinant H1D2 chimera. in Journal of Chemical Technology and Biotechnology. 2017;92(6):1328-1335.
doi:10.1002/jctb.5127 .

Mrkić, Ivan, Minić, Rajna, Bulat, Tanja, Aradska, Jana, Atanasković-Marković, Marina, Drakulić, Branko, Gavrović-Jankulović, Marija, "Modulation of the specific immune response in Balb/cmice by intranasal application of recombinant H1D2 chimera" in Journal of Chemical Technology and Biotechnology, 92, no. 6 (2017):1328-1335,
https://doi.org/10.1002/jctb.5127 . .

TY  - CONF
AU  - Marinković, Emilija
AU  - Đokić, Radmila
AU  - Filipović, Ana
AU  - Lukić, Ivana
AU  - Kosanović, Dejana
AU  - Inić-Kanada, Aleksandra
AU  - Gavrović-Jankulović, Marija
AU  - Stojanović, Marijana
PY  - 2017
UR  - http://intor.torlakinstitut.com/handle/123456789/478
PB  - Wiley, Hoboken
C3  - FEBS Journal
T1  - Prophylactic effect of recombinant banana lectin on TNBS-induced colitis in BALB/c mice
EP  - 125
SP  - 124
VL  - 284
UR  - https://hdl.handle.net/21.15107/rcub_intor_478
ER  - 

@conference{
author = "Marinković, Emilija and Đokić, Radmila and Filipović, Ana and Lukić, Ivana and Kosanović, Dejana and Inić-Kanada, Aleksandra and Gavrović-Jankulović, Marija and Stojanović, Marijana",
year = "2017",
publisher = "Wiley, Hoboken",
journal = "FEBS Journal",
title = "Prophylactic effect of recombinant banana lectin on TNBS-induced colitis in BALB/c mice",
pages = "125-124",
volume = "284",
url = "https://hdl.handle.net/21.15107/rcub_intor_478"
}

Marinković, E., Đokić, R., Filipović, A., Lukić, I., Kosanović, D., Inić-Kanada, A., Gavrović-Jankulović, M.,& Stojanović, M.. (2017). Prophylactic effect of recombinant banana lectin on TNBS-induced colitis in BALB/c mice. in FEBS Journal
Wiley, Hoboken., 284, 124-125.
https://hdl.handle.net/21.15107/rcub_intor_478

Marinković E, Đokić R, Filipović A, Lukić I, Kosanović D, Inić-Kanada A, Gavrović-Jankulović M, Stojanović M. Prophylactic effect of recombinant banana lectin on TNBS-induced colitis in BALB/c mice. in FEBS Journal. 2017;284:124-125.
https://hdl.handle.net/21.15107/rcub_intor_478 .

Marinković, Emilija, Đokić, Radmila, Filipović, Ana, Lukić, Ivana, Kosanović, Dejana, Inić-Kanada, Aleksandra, Gavrović-Jankulović, Marija, Stojanović, Marijana, "Prophylactic effect of recombinant banana lectin on TNBS-induced colitis in BALB/c mice" in FEBS Journal, 284 (2017):124-125,
https://hdl.handle.net/21.15107/rcub_intor_478 .

TY  - JOUR
AU  - Marinković, Emilija
AU  - Lukić, Ivana
AU  - Kosanović, Dejana
AU  - Inić-Kanada, Aleksandra
AU  - Gavrović-Jankulović, Marija
AU  - Stojanović, Marijana
PY  - 2016
UR  - http://intor.torlakinstitut.com/handle/123456789/471
AB  - Recombinant banana lectin isoform (rBanLec) attaches specifically to the mucosal surface, crosses the epithelial barrier and then directly affects the immune response in mouse colon. Structural characteristics, specificity and physiological impacts of rBanLec reported until now highly resemble those of its natural counterpart. Here, we demonstrated that a dose dependent stimulation of the colon with rBanLec skewed the immune response towards Th1/Th17 direction and this effect was counterbalanced by the rise in IL-10 production. Qualitative and quantitative characteristics of the established cytokine network were dependent on the applied rBanLec concentration. In addition, rBanLec enhanced local NO production and myeloperoxidase activity and promoted an increase in local IgA and IgG production. Stimulation with rBanLec can be beneficial in prevention of pathologies raised due to inappropriate cell-mediated immune response as well as in prevention of the pathogen invasion via the colon. (C) 2015 Elsevier Ltd. All rights reserved.
PB  - Elsevier, Amsterdam
T2  - Journal of Functional Foods
T1  - Recombinantly produced banana lectin isoform promotes balanced pro-inflammatory response in the colon
EP  - 78
SP  - 68
VL  - 20
DO  - 10.1016/j.jff.2015.10.019
ER  - 

@article{
author = "Marinković, Emilija and Lukić, Ivana and Kosanović, Dejana and Inić-Kanada, Aleksandra and Gavrović-Jankulović, Marija and Stojanović, Marijana",
year = "2016",
abstract = "Recombinant banana lectin isoform (rBanLec) attaches specifically to the mucosal surface, crosses the epithelial barrier and then directly affects the immune response in mouse colon. Structural characteristics, specificity and physiological impacts of rBanLec reported until now highly resemble those of its natural counterpart. Here, we demonstrated that a dose dependent stimulation of the colon with rBanLec skewed the immune response towards Th1/Th17 direction and this effect was counterbalanced by the rise in IL-10 production. Qualitative and quantitative characteristics of the established cytokine network were dependent on the applied rBanLec concentration. In addition, rBanLec enhanced local NO production and myeloperoxidase activity and promoted an increase in local IgA and IgG production. Stimulation with rBanLec can be beneficial in prevention of pathologies raised due to inappropriate cell-mediated immune response as well as in prevention of the pathogen invasion via the colon. (C) 2015 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier, Amsterdam",
journal = "Journal of Functional Foods",
title = "Recombinantly produced banana lectin isoform promotes balanced pro-inflammatory response in the colon",
pages = "78-68",
volume = "20",
doi = "10.1016/j.jff.2015.10.019"
}

Marinković, E., Lukić, I., Kosanović, D., Inić-Kanada, A., Gavrović-Jankulović, M.,& Stojanović, M.. (2016). Recombinantly produced banana lectin isoform promotes balanced pro-inflammatory response in the colon. in Journal of Functional Foods
Elsevier, Amsterdam., 20, 68-78.
https://doi.org/10.1016/j.jff.2015.10.019

Marinković E, Lukić I, Kosanović D, Inić-Kanada A, Gavrović-Jankulović M, Stojanović M. Recombinantly produced banana lectin isoform promotes balanced pro-inflammatory response in the colon. in Journal of Functional Foods. 2016;20:68-78.
doi:10.1016/j.jff.2015.10.019 .

Marinković, Emilija, Lukić, Ivana, Kosanović, Dejana, Inić-Kanada, Aleksandra, Gavrović-Jankulović, Marija, Stojanović, Marijana, "Recombinantly produced banana lectin isoform promotes balanced pro-inflammatory response in the colon" in Journal of Functional Foods, 20 (2016):68-78,
https://doi.org/10.1016/j.jff.2015.10.019 . .

TY  - JOUR
AU  - Minić, Rajna
AU  - Gavrović-Jankulović, Marija
AU  - Petrušić, Vladimir
AU  - Živković, Irena
AU  - Eijsink, Vincent G.H.
AU  - Dimitrijević, Ljiljana
AU  - Mathiesen, Geir
PY  - 2015
UR  - http://intor.torlakinstitut.com/handle/123456789/447
AB  - Group I grass pollen allergens are major contributors to grass pollen-related seasonal allergic rhinitis, and as such a primary target for allergen specific immunotherapy. In this study the potential therapeutic role of oral application of Lactobacillus plantarum WCFS1, directing cell wall attachment of the recombinant Fes p1 allergen, from Festuca pratensis was tested in a mouse model of Fes p1 allergy. For surface expression of Fes p1 allergen in L. plantarum WCFS1 pSIP system with inducible expression was used. Balb/c mice were sensitized with Fes p1 protein in alum and subsequently received live recombinant L. plantarum orally. Antibody levels (IgE, total IgG, IgG1, IgG2a, and IgA) were determined by ELISA. Differential eosinophil count in peripheral blood was performed. Reduced peripheral blood eosinophilia and increased serum IgG2A levels was detected in both groups which received live L. plantarum orally. Specific serum IgA levels were increased only in mice treated with the recombinant bacteria. Oral application of L. plantarum WCFS1 has a beneficial therapeutic effect in a mouse model of Fes p1 allergy. Cell surface expression of Fes p1 allergen potentiates this phenomenon in an allergen specific way. (C) 2015 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
T2  - Journal of Biotechnology
T1  - Effects of orally applied Fes p1-displaying L. plantarum WCFS1 on Fes p1 induced allergy in mice
EP  - 28
SP  - 23
VL  - 199
DO  - 10.1016/j.jbiotec.2015.01.028
ER  - 

@article{
author = "Minić, Rajna and Gavrović-Jankulović, Marija and Petrušić, Vladimir and Živković, Irena and Eijsink, Vincent G.H. and Dimitrijević, Ljiljana and Mathiesen, Geir",
year = "2015",
abstract = "Group I grass pollen allergens are major contributors to grass pollen-related seasonal allergic rhinitis, and as such a primary target for allergen specific immunotherapy. In this study the potential therapeutic role of oral application of Lactobacillus plantarum WCFS1, directing cell wall attachment of the recombinant Fes p1 allergen, from Festuca pratensis was tested in a mouse model of Fes p1 allergy. For surface expression of Fes p1 allergen in L. plantarum WCFS1 pSIP system with inducible expression was used. Balb/c mice were sensitized with Fes p1 protein in alum and subsequently received live recombinant L. plantarum orally. Antibody levels (IgE, total IgG, IgG1, IgG2a, and IgA) were determined by ELISA. Differential eosinophil count in peripheral blood was performed. Reduced peripheral blood eosinophilia and increased serum IgG2A levels was detected in both groups which received live L. plantarum orally. Specific serum IgA levels were increased only in mice treated with the recombinant bacteria. Oral application of L. plantarum WCFS1 has a beneficial therapeutic effect in a mouse model of Fes p1 allergy. Cell surface expression of Fes p1 allergen potentiates this phenomenon in an allergen specific way. (C) 2015 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Journal of Biotechnology",
title = "Effects of orally applied Fes p1-displaying L. plantarum WCFS1 on Fes p1 induced allergy in mice",
pages = "28-23",
volume = "199",
doi = "10.1016/j.jbiotec.2015.01.028"
}

Minić, R., Gavrović-Jankulović, M., Petrušić, V., Živković, I., Eijsink, V. G.H., Dimitrijević, L.,& Mathiesen, G.. (2015). Effects of orally applied Fes p1-displaying L. plantarum WCFS1 on Fes p1 induced allergy in mice. in Journal of Biotechnology
Elsevier Science Bv, Amsterdam., 199, 23-28.
https://doi.org/10.1016/j.jbiotec.2015.01.028

Minić R, Gavrović-Jankulović M, Petrušić V, Živković I, Eijsink VG, Dimitrijević L, Mathiesen G. Effects of orally applied Fes p1-displaying L. plantarum WCFS1 on Fes p1 induced allergy in mice. in Journal of Biotechnology. 2015;199:23-28.
doi:10.1016/j.jbiotec.2015.01.028 .

Minić, Rajna, Gavrović-Jankulović, Marija, Petrušić, Vladimir, Živković, Irena, Eijsink, Vincent G.H., Dimitrijević, Ljiljana, Mathiesen, Geir, "Effects of orally applied Fes p1-displaying L. plantarum WCFS1 on Fes p1 induced allergy in mice" in Journal of Biotechnology, 199 (2015):23-28,
https://doi.org/10.1016/j.jbiotec.2015.01.028 . .

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
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"
}

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

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 .

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 . .

TY  - JOUR
AU  - Grozdanović, Milica
AU  - Ostojić, Sanja
AU  - Aleksić, Ivana
AU  - Anđelković, Uroš
AU  - Petersen, Arnd
AU  - Gavrović-Jankulović, Marija
PY  - 2014
UR  - http://intor.torlakinstitut.com/handle/123456789/411
AB  - BACKGROUND: Actinidin is a cysteine protease and major allergen from kiwi fruit. When purified under specific native conditions, actinidin preparations from fresh kiwi fruit contain both an active and inactive form of this enzyme. In this study, biochemical and immunological properties upon simulated gastro-intestinal digestion, as well as thermal stability, were investigated for both active and E-64-inhibited actinidin. RESULTS: Active actinidin retained its primary structure and proteolytic activity after 2 h of simulated gastric digestion, followed by 2 h of intestinal digestion, as assessed by SDS-PAGE, zymography and mass spectroscopy. Immunological reactivity of active actinidin was also preserved, as tested by immunoelectrophoresis. The E-64 inhibited actinidin was fully degraded after 1 h of pepsin treatment. Differential scanning calorimetry showed that active actinidin has one transition maximum temperature (T-m) at 73.9 degrees C, whereas in the E-64-actinidin complex the two actinidin domains unfolded independently, with the first domain having a T-m value of only 61 degrees C. CONCLUSION: Active actinidin is capable of reaching the intestinal mucosa in a proteolytically active and immunogenic state. Inhibitor binding induces changes in the actinidin molecule that go beyond inhibition of proteolytic activity, also influencing the digestion stability and T-m values of actinidin, features important in the characterisation of food allergens. (C) 2014 Society of Chemical Industry
PB  - Wiley, Hoboken
T2  - Journal of the Science of Food and Agriculture
T1  - Active actinidin retains function upon gastro-intestinal digestion and is more thermostable than the E-64-inhibited counterpart
EP  - 3052
IS  - 14
SP  - 3046
VL  - 94
DO  - 10.1002/jsfa.6656
ER  - 

@article{
author = "Grozdanović, Milica and Ostojić, Sanja and Aleksić, Ivana and Anđelković, Uroš and Petersen, Arnd and Gavrović-Jankulović, Marija",
year = "2014",
abstract = "BACKGROUND: Actinidin is a cysteine protease and major allergen from kiwi fruit. When purified under specific native conditions, actinidin preparations from fresh kiwi fruit contain both an active and inactive form of this enzyme. In this study, biochemical and immunological properties upon simulated gastro-intestinal digestion, as well as thermal stability, were investigated for both active and E-64-inhibited actinidin. RESULTS: Active actinidin retained its primary structure and proteolytic activity after 2 h of simulated gastric digestion, followed by 2 h of intestinal digestion, as assessed by SDS-PAGE, zymography and mass spectroscopy. Immunological reactivity of active actinidin was also preserved, as tested by immunoelectrophoresis. The E-64 inhibited actinidin was fully degraded after 1 h of pepsin treatment. Differential scanning calorimetry showed that active actinidin has one transition maximum temperature (T-m) at 73.9 degrees C, whereas in the E-64-actinidin complex the two actinidin domains unfolded independently, with the first domain having a T-m value of only 61 degrees C. CONCLUSION: Active actinidin is capable of reaching the intestinal mucosa in a proteolytically active and immunogenic state. Inhibitor binding induces changes in the actinidin molecule that go beyond inhibition of proteolytic activity, also influencing the digestion stability and T-m values of actinidin, features important in the characterisation of food allergens. (C) 2014 Society of Chemical Industry",
publisher = "Wiley, Hoboken",
journal = "Journal of the Science of Food and Agriculture",
title = "Active actinidin retains function upon gastro-intestinal digestion and is more thermostable than the E-64-inhibited counterpart",
pages = "3052-3046",
number = "14",
volume = "94",
doi = "10.1002/jsfa.6656"
}

Grozdanović, M., Ostojić, S., Aleksić, I., Anđelković, U., Petersen, A.,& Gavrović-Jankulović, M.. (2014). Active actinidin retains function upon gastro-intestinal digestion and is more thermostable than the E-64-inhibited counterpart. in Journal of the Science of Food and Agriculture
Wiley, Hoboken., 94(14), 3046-3052.
https://doi.org/10.1002/jsfa.6656

Grozdanović M, Ostojić S, Aleksić I, Anđelković U, Petersen A, Gavrović-Jankulović M. Active actinidin retains function upon gastro-intestinal digestion and is more thermostable than the E-64-inhibited counterpart. in Journal of the Science of Food and Agriculture. 2014;94(14):3046-3052.
doi:10.1002/jsfa.6656 .

Grozdanović, Milica, Ostojić, Sanja, Aleksić, Ivana, Anđelković, Uroš, Petersen, Arnd, Gavrović-Jankulović, Marija, "Active actinidin retains function upon gastro-intestinal digestion and is more thermostable than the E-64-inhibited counterpart" in Journal of the Science of Food and Agriculture, 94, no. 14 (2014):3046-3052,
https://doi.org/10.1002/jsfa.6656 . .

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
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"
}

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

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 .

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 . .

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
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"
}

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

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 .

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 . .

TY  - JOUR
AU  - Popović, Milica
AU  - Anđelković, Uroš
AU  - Grozdanović, Milica
AU  - Aleksić, Ivana
AU  - Gavrović-Jankulović, Marija
PY  - 2013
UR  - http://intor.torlakinstitut.com/handle/123456789/390
AB  - The need for replacing traditional pesticides with alternative agents for the management of agricultural pathogens is rising worldwide. In this study, a cysteine proteinase inhibitor (CPI), 11 kDa in size, was purified from green kiwifruit to homogeneity. We examined the growth inhibition of three plant pathogenic Gram-negative bacterial strains by kiwi CPI and attempted to elucidate the potential mechanism of the growth inhibition. CPI influenced the growth of phytopathogenic bacteria Agrobacterium tumefaciens (76.2 % growth inhibition using 15 mu M CPI), Burkholderia cepacia (75.6 % growth inhibition) and, to a lesser extent, Erwinia carotovora (44.4 % growth inhibition) by inhibiting proteinases that are excreted by these bacteria. Identification and characterization of natural plant defense molecules is the first step toward creation of improved methods for pest control based on naturally occurring molecules.
PB  - Springer, New York
T2  - Indian Journal of Microbiology
T1  - In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa)
EP  - 105
IS  - 1
SP  - 100
VL  - 53
DO  - 10.1007/s12088-012-0319-2
ER  - 

@article{
author = "Popović, Milica and Anđelković, Uroš and Grozdanović, Milica and Aleksić, Ivana and Gavrović-Jankulović, Marija",
year = "2013",
abstract = "The need for replacing traditional pesticides with alternative agents for the management of agricultural pathogens is rising worldwide. In this study, a cysteine proteinase inhibitor (CPI), 11 kDa in size, was purified from green kiwifruit to homogeneity. We examined the growth inhibition of three plant pathogenic Gram-negative bacterial strains by kiwi CPI and attempted to elucidate the potential mechanism of the growth inhibition. CPI influenced the growth of phytopathogenic bacteria Agrobacterium tumefaciens (76.2 % growth inhibition using 15 mu M CPI), Burkholderia cepacia (75.6 % growth inhibition) and, to a lesser extent, Erwinia carotovora (44.4 % growth inhibition) by inhibiting proteinases that are excreted by these bacteria. Identification and characterization of natural plant defense molecules is the first step toward creation of improved methods for pest control based on naturally occurring molecules.",
publisher = "Springer, New York",
journal = "Indian Journal of Microbiology",
title = "In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa)",
pages = "105-100",
number = "1",
volume = "53",
doi = "10.1007/s12088-012-0319-2"
}

Popović, M., Anđelković, U., Grozdanović, M., Aleksić, I.,& Gavrović-Jankulović, M.. (2013). In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa). in Indian Journal of Microbiology
Springer, New York., 53(1), 100-105.
https://doi.org/10.1007/s12088-012-0319-2

Popović M, Anđelković U, Grozdanović M, Aleksić I, Gavrović-Jankulović M. In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa). in Indian Journal of Microbiology. 2013;53(1):100-105.
doi:10.1007/s12088-012-0319-2 .

Popović, Milica, Anđelković, Uroš, Grozdanović, Milica, Aleksić, Ivana, Gavrović-Jankulović, Marija, "In Vitro Antibacterial Activity of Cysteine Protease Inhibitor from Kiwifruit (Actinidia deliciosa)" in Indian Journal of Microbiology, 53, no. 1 (2013):100-105,
https://doi.org/10.1007/s12088-012-0319-2 . .

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  - https://hdl.handle.net/21.15107/rcub_intor_380
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 = "https://hdl.handle.net/21.15107/rcub_intor_380"
}

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.
https://hdl.handle.net/21.15107/rcub_intor_380

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.
https://hdl.handle.net/21.15107/rcub_intor_380 .

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,
https://hdl.handle.net/21.15107/rcub_intor_380 .

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  - https://hdl.handle.net/21.15107/rcub_intor_364
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 = "https://hdl.handle.net/21.15107/rcub_intor_364"
}

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.
https://hdl.handle.net/21.15107/rcub_intor_364

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.
https://hdl.handle.net/21.15107/rcub_intor_364 .

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,
https://hdl.handle.net/21.15107/rcub_intor_364 .

TY  - JOUR
AU  - Dimitrijević, Rajna
AU  - Stojanović, Marijana
AU  - Micić, M.
AU  - Dimitrijević, Ljiljana
AU  - Gavrović-Jankulović, Marija
PY  - 2012
UR  - http://intor.torlakinstitut.com/handle/123456789/354
AB  - To explore the potential usage of recombinant banana lectin as an immunostimulator it was of interest to analyze the effect it exerted in vivo in mice, upon two different routes of exposure. By Western blotting analysis of the gastric and intestinal luminal content it was found that recombinant banana lectin is stable in vivo in the mouse digestive tract, where it specifically interacts with the mucosal surfaces which can be inhibited by the addition of glucose. Its attachment to mice jejunum has been confirmed by immunofluorescence. In addition, it was able to induce systemic immunity, evidenced by specific antibody production, by oral application, a property that might be exploited for the induction of systemic immune responses. (c) 2012 Elsevier Ltd. All rights reserved.
PB  - Elsevier, Amsterdam
T2  - Journal of Functional Foods
T1  - Recombinant banana lectin as mucosal immunostimulator
EP  - 641
IS  - 3
SP  - 636
VL  - 4
DO  - 10.1016/j.jff.2012.04.003
ER  - 

@article{
author = "Dimitrijević, Rajna and Stojanović, Marijana and Micić, M. and Dimitrijević, Ljiljana and Gavrović-Jankulović, Marija",
year = "2012",
abstract = "To explore the potential usage of recombinant banana lectin as an immunostimulator it was of interest to analyze the effect it exerted in vivo in mice, upon two different routes of exposure. By Western blotting analysis of the gastric and intestinal luminal content it was found that recombinant banana lectin is stable in vivo in the mouse digestive tract, where it specifically interacts with the mucosal surfaces which can be inhibited by the addition of glucose. Its attachment to mice jejunum has been confirmed by immunofluorescence. In addition, it was able to induce systemic immunity, evidenced by specific antibody production, by oral application, a property that might be exploited for the induction of systemic immune responses. (c) 2012 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier, Amsterdam",
journal = "Journal of Functional Foods",
title = "Recombinant banana lectin as mucosal immunostimulator",
pages = "641-636",
number = "3",
volume = "4",
doi = "10.1016/j.jff.2012.04.003"
}

Dimitrijević, R., Stojanović, M., Micić, M., Dimitrijević, L.,& Gavrović-Jankulović, M.. (2012). Recombinant banana lectin as mucosal immunostimulator. in Journal of Functional Foods
Elsevier, Amsterdam., 4(3), 636-641.
https://doi.org/10.1016/j.jff.2012.04.003

Dimitrijević R, Stojanović M, Micić M, Dimitrijević L, Gavrović-Jankulović M. Recombinant banana lectin as mucosal immunostimulator. in Journal of Functional Foods. 2012;4(3):636-641.
doi:10.1016/j.jff.2012.04.003 .

Dimitrijević, Rajna, Stojanović, Marijana, Micić, M., Dimitrijević, Ljiljana, Gavrović-Jankulović, Marija, "Recombinant banana lectin as mucosal immunostimulator" in Journal of Functional Foods, 4, no. 3 (2012):636-641,
https://doi.org/10.1016/j.jff.2012.04.003 . .

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
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"
}

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

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 .

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 . .

TY  - JOUR
AU  - Aleksić, Ivana
AU  - Popović, Milica
AU  - Dimitrijević, Rajna
AU  - Anđelković, Uroš
AU  - Vassilopoulou, Emilia
AU  - Sinaniotis, Athanassios
AU  - Atanasković-Marković, Marina
AU  - Lindner, Buko
AU  - Petersen, Arnd
AU  - Papadopoulos, Nikolaos G.
AU  - Gavrović-Jankulović, Marija
PY  - 2012
UR  - http://intor.torlakinstitut.com/handle/123456789/362
AB  - Scope Banana fruit has become an important cause of fruit allergy in the recent years. Among the five registered IUIS allergens, Mus a 1 and Mus a 2 have been characterized in detail. In this study, molecular characterization and evaluation of the allergenic properties of beta-1,3-glucanase from banana (Musa acuminata), denoted as Mus a 5, were performed Methods and results: The gene of Mus a 5 was cloned and sequenced. The obtained cDNA revealed a novel Mus a 5 isoform with an open reading frame encoding a protein of 340 amino acids comprising a putative signal peptide of 28 amino acid residues. By MALDI-TOF analysis Mus a 5 isolated from banana fruit revealed a molecular mass of 33 451 +/- 67 Da. Two Mus a 5 isoforms (pI 7.7 and 8.0) were detected by 2D immunoblot with an identical N-terminal sequence. By mass fingerprint, 76 and 83% of the primary structure was confirmed for the two mature Mus a 5 isoforms, respectively. IgE reactivity to Mus a 5 was found in 74% of patients sensitized to banana fruit. Upregulation of basophil activation markers CD63 and CD203c was achieved with Mus a 5 in a concentration-dependent manner. Conclusion: Mus a 5 is a functional allergen and a candidate for the component-resolved allergy diagnosis of banana allergy.
PB  - Wiley, Hoboken
T2  - Molecular Nutrition and Food Research
T1  - Molecular and immunological characterization of Mus a 5 allergen from banana fruit
EP  - 453
IS  - 3
SP  - 446
VL  - 56
DO  - 10.1002/mnfr.201100541
ER  - 

@article{
author = "Aleksić, Ivana and Popović, Milica and Dimitrijević, Rajna and Anđelković, Uroš and Vassilopoulou, Emilia and Sinaniotis, Athanassios and Atanasković-Marković, Marina and Lindner, Buko and Petersen, Arnd and Papadopoulos, Nikolaos G. and Gavrović-Jankulović, Marija",
year = "2012",
abstract = "Scope Banana fruit has become an important cause of fruit allergy in the recent years. Among the five registered IUIS allergens, Mus a 1 and Mus a 2 have been characterized in detail. In this study, molecular characterization and evaluation of the allergenic properties of beta-1,3-glucanase from banana (Musa acuminata), denoted as Mus a 5, were performed Methods and results: The gene of Mus a 5 was cloned and sequenced. The obtained cDNA revealed a novel Mus a 5 isoform with an open reading frame encoding a protein of 340 amino acids comprising a putative signal peptide of 28 amino acid residues. By MALDI-TOF analysis Mus a 5 isolated from banana fruit revealed a molecular mass of 33 451 +/- 67 Da. Two Mus a 5 isoforms (pI 7.7 and 8.0) were detected by 2D immunoblot with an identical N-terminal sequence. By mass fingerprint, 76 and 83% of the primary structure was confirmed for the two mature Mus a 5 isoforms, respectively. IgE reactivity to Mus a 5 was found in 74% of patients sensitized to banana fruit. Upregulation of basophil activation markers CD63 and CD203c was achieved with Mus a 5 in a concentration-dependent manner. Conclusion: Mus a 5 is a functional allergen and a candidate for the component-resolved allergy diagnosis of banana allergy.",
publisher = "Wiley, Hoboken",
journal = "Molecular Nutrition and Food Research",
title = "Molecular and immunological characterization of Mus a 5 allergen from banana fruit",
pages = "453-446",
number = "3",
volume = "56",
doi = "10.1002/mnfr.201100541"
}

Aleksić, I., Popović, M., Dimitrijević, R., Anđelković, U., Vassilopoulou, E., Sinaniotis, A., Atanasković-Marković, M., Lindner, B., Petersen, A., Papadopoulos, N. G.,& Gavrović-Jankulović, M.. (2012). Molecular and immunological characterization of Mus a 5 allergen from banana fruit. in Molecular Nutrition and Food Research
Wiley, Hoboken., 56(3), 446-453.
https://doi.org/10.1002/mnfr.201100541

Aleksić I, Popović M, Dimitrijević R, Anđelković U, Vassilopoulou E, Sinaniotis A, Atanasković-Marković M, Lindner B, Petersen A, Papadopoulos NG, Gavrović-Jankulović M. Molecular and immunological characterization of Mus a 5 allergen from banana fruit. in Molecular Nutrition and Food Research. 2012;56(3):446-453.
doi:10.1002/mnfr.201100541 .

Aleksić, Ivana, Popović, Milica, Dimitrijević, Rajna, Anđelković, Uroš, Vassilopoulou, Emilia, Sinaniotis, Athanassios, Atanasković-Marković, Marina, Lindner, Buko, Petersen, Arnd, Papadopoulos, Nikolaos G., Gavrović-Jankulović, Marija, "Molecular and immunological characterization of Mus a 5 allergen from banana fruit" in Molecular Nutrition and Food Research, 56, no. 3 (2012):446-453,
https://doi.org/10.1002/mnfr.201100541 . .

TY  - JOUR
AU  - Atanasković-Marković, Marina
AU  - Gavrović-Jankulović, Marija
AU  - Janković, Srđa
AU  - Blagojević, Gordan
AU  - Ćirković-Veličković, Tanja
AU  - Milojević, Irina
AU  - Simić, Dušica
AU  - Nestorovic, Branimir
PY  - 2012
UR  - http://intor.torlakinstitut.com/handle/123456789/342
AB  - Introduction. In spite of the wide usage of corticosteroids for the treatment of a plethora of diseases, sometimes they can induce immediate hypersensitivity reactions, which are however uncommon. Case Outline. We report a case of immediate allergic reaction induced by intravenous methylprednisolone given before operation for surgical repair of an arm contracture as a sequel of burns, which the child had tolerated a month before. Six weeks later the patient repeated the anaphylactic reaction during skin testing to methylprednisolone. In addition, basophile activation test with methylprednisolone (BAT) was positive. Conclusion. This case report describes a patient who experienced intraoperative anaphylaxis and anaphylactic reaction induced by skin testing. This is the first report on induction of both anaphylactic reactions by methylprednisolone in the same child. Clinical findings, positive BAT and positive skin tests with methylprednisolone imply that the child developed type-I hypersensitivity. The lack of cross-reactivity with other corticosteroids emphasizes that the reactions were caused by the steroid molecule.
AB  - Uvod. Uprkos širokoj primeni kortikosteroida u lečenju od različitih bolesti, oni ponekad mogu izazvati ranu alergijsku reakciju. Prikaz bolesnika. Kod dvanaestogodišnjeg dečaka došlo je do rane alergijske reakcije izazvane intravenskom primenom metilprednizolona neposredno pre hirurške intervencije, tačnije, korekcije kontrakture šake koja se javila kao komplikacija opekotine. Mesec dana pre pojave alergijske reakcije dete je primalo metilprednizolon i dobro ga podnosilo. Šest nedelja posle operacije ponovo se javila anafilaktička reakcija tokom kožnog testiranja metilprednizolonom. Primenjen je i test aktivacije bazofila (BAT) ovim lekom, čiji je nalaz bio pozitivan. Zaključak. Ovo je prvi prikaz dve vrste anafilaktičke reakcije izazvane metilprednizolonom kod iste osobe. Klinička slika, pozitivni nalaz BAT i pozitivne kožne probe na metilprednizolon pokazuju da se kod deteta razvio prvi tip hipersenzitivne reakcije. Nedostatak unakrsne reaktivnosti s ostalim kortikosteroidima ukazuje na to da je alergijska reakcija izazvana steroidnim molekulom.
PB  - Srpsko lekarsko društvo, Beograd
T2  - Srpski arhiv za celokupno lekarstvo
T1  - Immediate allergic reaction to methylprednisolone with tolerance of other corticosteroids
T1  - Rana alergijska reakcija na metilprednizolon sa tolerancijom drugih kortikosteroida
EP  - 235
IS  - 3-4
SP  - 233
VL  - 140
DO  - 10.2298/SARH1204233A
ER  - 

@article{
author = "Atanasković-Marković, Marina and Gavrović-Jankulović, Marija and Janković, Srđa and Blagojević, Gordan and Ćirković-Veličković, Tanja and Milojević, Irina and Simić, Dušica and Nestorovic, Branimir",
year = "2012",
abstract = "Introduction. In spite of the wide usage of corticosteroids for the treatment of a plethora of diseases, sometimes they can induce immediate hypersensitivity reactions, which are however uncommon. Case Outline. We report a case of immediate allergic reaction induced by intravenous methylprednisolone given before operation for surgical repair of an arm contracture as a sequel of burns, which the child had tolerated a month before. Six weeks later the patient repeated the anaphylactic reaction during skin testing to methylprednisolone. In addition, basophile activation test with methylprednisolone (BAT) was positive. Conclusion. This case report describes a patient who experienced intraoperative anaphylaxis and anaphylactic reaction induced by skin testing. This is the first report on induction of both anaphylactic reactions by methylprednisolone in the same child. Clinical findings, positive BAT and positive skin tests with methylprednisolone imply that the child developed type-I hypersensitivity. The lack of cross-reactivity with other corticosteroids emphasizes that the reactions were caused by the steroid molecule., Uvod. Uprkos širokoj primeni kortikosteroida u lečenju od različitih bolesti, oni ponekad mogu izazvati ranu alergijsku reakciju. Prikaz bolesnika. Kod dvanaestogodišnjeg dečaka došlo je do rane alergijske reakcije izazvane intravenskom primenom metilprednizolona neposredno pre hirurške intervencije, tačnije, korekcije kontrakture šake koja se javila kao komplikacija opekotine. Mesec dana pre pojave alergijske reakcije dete je primalo metilprednizolon i dobro ga podnosilo. Šest nedelja posle operacije ponovo se javila anafilaktička reakcija tokom kožnog testiranja metilprednizolonom. Primenjen je i test aktivacije bazofila (BAT) ovim lekom, čiji je nalaz bio pozitivan. Zaključak. Ovo je prvi prikaz dve vrste anafilaktičke reakcije izazvane metilprednizolonom kod iste osobe. Klinička slika, pozitivni nalaz BAT i pozitivne kožne probe na metilprednizolon pokazuju da se kod deteta razvio prvi tip hipersenzitivne reakcije. Nedostatak unakrsne reaktivnosti s ostalim kortikosteroidima ukazuje na to da je alergijska reakcija izazvana steroidnim molekulom.",
publisher = "Srpsko lekarsko društvo, Beograd",
journal = "Srpski arhiv za celokupno lekarstvo",
title = "Immediate allergic reaction to methylprednisolone with tolerance of other corticosteroids, Rana alergijska reakcija na metilprednizolon sa tolerancijom drugih kortikosteroida",
pages = "235-233",
number = "3-4",
volume = "140",
doi = "10.2298/SARH1204233A"
}

Atanasković-Marković, M., Gavrović-Jankulović, M., Janković, S., Blagojević, G., Ćirković-Veličković, T., Milojević, I., Simić, D.,& Nestorovic, B.. (2012). Immediate allergic reaction to methylprednisolone with tolerance of other corticosteroids. in Srpski arhiv za celokupno lekarstvo
Srpsko lekarsko društvo, Beograd., 140(3-4), 233-235.
https://doi.org/10.2298/SARH1204233A

Atanasković-Marković M, Gavrović-Jankulović M, Janković S, Blagojević G, Ćirković-Veličković T, Milojević I, Simić D, Nestorovic B. Immediate allergic reaction to methylprednisolone with tolerance of other corticosteroids. in Srpski arhiv za celokupno lekarstvo. 2012;140(3-4):233-235.
doi:10.2298/SARH1204233A .

Atanasković-Marković, Marina, Gavrović-Jankulović, Marija, Janković, Srđa, Blagojević, Gordan, Ćirković-Veličković, Tanja, Milojević, Irina, Simić, Dušica, Nestorovic, Branimir, "Immediate allergic reaction to methylprednisolone with tolerance of other corticosteroids" in Srpski arhiv za celokupno lekarstvo, 140, no. 3-4 (2012):233-235,
https://doi.org/10.2298/SARH1204233A . .

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
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"
}

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

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 .

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 . .

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  - https://hdl.handle.net/21.15107/rcub_intor_365
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 = "https://hdl.handle.net/21.15107/rcub_intor_365"
}

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.
https://hdl.handle.net/21.15107/rcub_intor_365

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.
https://hdl.handle.net/21.15107/rcub_intor_365 .

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,
https://hdl.handle.net/21.15107/rcub_intor_365 .

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
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"
}

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

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 .

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 . .