Atanasković-Marković, Marina

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orcid::0000-0003-1354-6072
  • Atanasković-Marković, Marina (23)
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Author's Bibliography

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

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

(MDPI, Basel, 2020)

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

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

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

(Wiley, Hoboken, 2018)

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

Modulation of the specific immune response in Balb/cmice by intranasal application of recombinant H1D2 chimera

Mrkić, Ivan; Minić, Rajna; Bulat, Tanja; Aradska, Jana; Atanasković-Marković, Marina; Drakulić, Branko; Gavrović-Jankulović, Marija

(Wiley, Hoboken, 2017)

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
UR  - conv_413
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",
url = "conv_413"
}
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
conv_413
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
conv_413 .
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 .,
conv_413 .
3
2
3

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

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

(Royal Soc Chemistry, Cambridge, 2016)

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

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

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

(Srpsko hemijsko društvo, Beograd, 2012)

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

Optimization of the heterologous expression of banana glucanase in Escherichia coli

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

(Srpsko hemijsko društvo, Beograd, 2012)

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

Molecular and immunological characterization of Mus a 5 allergen from banana fruit

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

(Wiley, Hoboken, 2012)

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
UR  - conv_286
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",
url = "conv_286"
}
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
conv_286
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
conv_286 .
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 .,
conv_286 .
18
19
21

Immediate allergic reaction to methylprednisolone with tolerance of other corticosteroids

Atanasković-Marković, Marina; Gavrović-Jankulović, Marija; Janković, Srđa; Blagojević, Gordan; Ćirković-Veličković, Tanja; Milojević, Irina; Simić, Dušica; Nestorovic, Branimir

(Srpsko lekarsko društvo, Beograd, 2012)

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
UR  - conv_39
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",
url = "conv_39"
}
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
conv_39
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
conv_39 .
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 .,
conv_39 .
8
6

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

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

(Pergamon-Elsevier Science Ltd, Oxford, 2012)

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

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

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

(Srpsko hemijsko društvo, Beograd, 2012)

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

Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein

Stanić, Dragana; Monogioudi, Evanthia; Dilek, Ercili; Radosavljević, Jelena; Atanasković-Marković, Marina; Vučković, Olga; Raija, Lantto; Mattinen, Maija; Buchert, Johanna; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2010)

TY  - JOUR
AU  - Stanić, Dragana
AU  - Monogioudi, Evanthia
AU  - Dilek, Ercili
AU  - Radosavljević, Jelena
AU  - Atanasković-Marković, Marina
AU  - Vučković, Olga
AU  - Raija, Lantto
AU  - Mattinen, Maija
AU  - Buchert, Johanna
AU  - Ćirković-Veličković, Tanja
PY  - 2010
UR  - http://intor.torlakinstitut.com/handle/123456789/294
AB  - Crosslinking enzymes are frequently used in bioprocessing of dairy products. The aim of this study was to examine the effects of enzymatic crosslinking on IgE binding, allergenicity and digestion stability of beta-casein (CN). beta-CN was crosslinked by transglutaminase, tyrosinase, mushroom tyrosinase/caffeic acid and laccase/caffeic acid. The IgE binding to beta-CN was compared in vitro by CAP inhibition assay, ELISA inhibition as well as ex vivo by basophil activation assay. Crosslinked CNs were digested by simulated gastric fluid for 15 and 60 min and obtained digests analyzed for their ability to inhibit IgE binding by CAP inhibition assay and SDS-PAGE. The ability of crosslinked CNs to activate basophils was significantly reduced in seven patients in the case of CN crosslinked by laccase and moderately reduced in the case of tyrosinase/caffeic acid crosslinked CN (in two cow's milk allergy patients tested with different allergen concentrations). The response to various crosslinked CNs differed individually among patients' sera tested by ELISA inhibition assay. The presence of caffeic acid hampered digestion by pepsin, and this effect was most pronounced for the tyrosinase/caffeic acid crosslinked CN. The laccase/caffeic acid and mushroom tyrosinase/caffeic acid had the highest potential in mitigating IgE binding and allergenicity of the beta-CN out of all investigated enzymes. The presence of a small phenolic compound also increased digestion stability of beta-CN.
PB  - Wiley, Hoboken
T2  - Molecular Nutrition and Food Research
T1  - Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein
EP  - 1284
IS  - 9
SP  - 1273
VL  - 54
DO  - 10.1002/mnfr.200900184
UR  - conv_258
ER  - 
@article{
author = "Stanić, Dragana and Monogioudi, Evanthia and Dilek, Ercili and Radosavljević, Jelena and Atanasković-Marković, Marina and Vučković, Olga and Raija, Lantto and Mattinen, Maija and Buchert, Johanna and Ćirković-Veličković, Tanja",
year = "2010",
abstract = "Crosslinking enzymes are frequently used in bioprocessing of dairy products. The aim of this study was to examine the effects of enzymatic crosslinking on IgE binding, allergenicity and digestion stability of beta-casein (CN). beta-CN was crosslinked by transglutaminase, tyrosinase, mushroom tyrosinase/caffeic acid and laccase/caffeic acid. The IgE binding to beta-CN was compared in vitro by CAP inhibition assay, ELISA inhibition as well as ex vivo by basophil activation assay. Crosslinked CNs were digested by simulated gastric fluid for 15 and 60 min and obtained digests analyzed for their ability to inhibit IgE binding by CAP inhibition assay and SDS-PAGE. The ability of crosslinked CNs to activate basophils was significantly reduced in seven patients in the case of CN crosslinked by laccase and moderately reduced in the case of tyrosinase/caffeic acid crosslinked CN (in two cow's milk allergy patients tested with different allergen concentrations). The response to various crosslinked CNs differed individually among patients' sera tested by ELISA inhibition assay. The presence of caffeic acid hampered digestion by pepsin, and this effect was most pronounced for the tyrosinase/caffeic acid crosslinked CN. The laccase/caffeic acid and mushroom tyrosinase/caffeic acid had the highest potential in mitigating IgE binding and allergenicity of the beta-CN out of all investigated enzymes. The presence of a small phenolic compound also increased digestion stability of beta-CN.",
publisher = "Wiley, Hoboken",
journal = "Molecular Nutrition and Food Research",
title = "Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein",
pages = "1284-1273",
number = "9",
volume = "54",
doi = "10.1002/mnfr.200900184",
url = "conv_258"
}
Stanić, D., Monogioudi, E., Dilek, E., Radosavljević, J., Atanasković-Marković, M., Vučković, O., Raija, L., Mattinen, M., Buchert, J.,& Ćirković-Veličković, T.. (2010). Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein. in Molecular Nutrition and Food Research
Wiley, Hoboken., 54(9), 1273-1284.
https://doi.org/10.1002/mnfr.200900184
conv_258
Stanić D, Monogioudi E, Dilek E, Radosavljević J, Atanasković-Marković M, Vučković O, Raija L, Mattinen M, Buchert J, Ćirković-Veličković T. Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein. in Molecular Nutrition and Food Research. 2010;54(9):1273-1284.
doi:10.1002/mnfr.200900184
conv_258 .
Stanić, Dragana, Monogioudi, Evanthia, Dilek, Ercili, Radosavljević, Jelena, Atanasković-Marković, Marina, Vučković, Olga, Raija, Lantto, Mattinen, Maija, Buchert, Johanna, Ćirković-Veličković, Tanja, "Digestibility and allergenicity assessment of enzymatically crosslinked beta-casein" in Molecular Nutrition and Food Research, 54, no. 9 (2010):1273-1284,
https://doi.org/10.1002/mnfr.200900184 .,
conv_258 .
6
69
66
68

Isolation and characterization of the 68 kD allergen from house dust mite Dermatophagoides pteronyssinus

Milovanović, Katarina; Burazer, Lidija; Vučković, Olga; Atanasković-Marković, Marina; Ćirković-Veličković, Tanja; Jankov, Ratko; Gavrović-Jankulović, Marija

(Srpsko hemijsko društvo, Beograd, 2009)

TY  - JOUR
AU  - Milovanović, Katarina
AU  - Burazer, Lidija
AU  - Vučković, Olga
AU  - Atanasković-Marković, Marina
AU  - Ćirković-Veličković, Tanja
AU  - Jankov, Ratko
AU  - Gavrović-Jankulović, Marija
PY  - 2009
UR  - http://intor.torlakinstitut.com/handle/123456789/285
AB  - House dust mites (HDM) represent a major source of allergens, contributing to the increasing incidence of type I hypersensitivity disease worldwide. Over 30 different IgE-binding proteins from the HDM extract were detected. Although group 1 and 2 have been identified as major allergens, due to the safety and efficacy of allergy diagnosis and immunotherapy, there is a need to carefully evaluate the clinical relevance of other allergens present in the HDM extract. In regard to this, a high molecular mass allergen of about 68 kD was purified from the HDM extract using a combination of gel permeation chromatography and reversed-phase chromatography. The IgG and IgE reactivity of the purified protein were preserved during the purification process, as confirmed by Western blot analysis with polyclonal rabbit antibodies and dot blot analysis with a pool of sera from subjects with house dust mite allergy, respectively. In addition, the IgE reactivity was confirmed using ELISA testing with nine patient sera. The biological potency of the 68 kD allergen was confirmed by skin prick testing in five allergic subjects, suggesting that the high molecular mass allergen is a good candidate for component-resolved diagnosis of house dust mite allergy and eventual therapeutic treatment.
AB  - Grinje iz kućne prašine predstavljaju jedan od glavnih izvora alergena koji su u značajnoj meri doprineli porastu prvog tipa preosetljivosti. Preko 30 IgE-vezujućih proteina iz kućne prašine je detektovano do danas. Alergeni grupe 1 i 2 označeni su kao glavni alergeni kućne prašine. Međutim, da bi se poboljšala sigurnost i efikasnost dijagnoze i terapije alergijskih oboljenja izazvanih grinjama iz kućne prašine, neophodno je odrediti klinički značaj svih alergena iz ovog alergenskog izvora. U ovom radu izolovan je alergen visoke molekulske mase od 68 kD iz ekstrakta kućne prašine kombinovanjem gel-permeacione hromatografije i reversno-fazne hromatografije. IgG i IgE reaktivnost prečišćenog proteina je proverena u 'Western blot'-u i 'dot blot'-u sa poliklonskim zečijim antitelima na ekstrakt kućne prašine i 'pool'-om seruma osoba alergičnih na kućnu prašinu, redom. 64 % pacijenata je pokazalo IgE reaktivnost na prečišćeni protein u ELISA testu. Biološka reaktivnost prečišćenog alergena je potvrđena u kožnim probama na pet pacijenata, ukazujući da je prečišćen alergen dobar kandidat za dijagnozu alergije na kućnu prašinu pojedinačnim komponentama i eventualni terapeutski tretman.
PB  - Srpsko hemijsko društvo, Beograd
T2  - Journal of the Serbian Chemical Society
T1  - Isolation and characterization of the 68 kD allergen from house dust mite Dermatophagoides pteronyssinus
T1  - Izolovanje i karakterizacija 68 kD alergena iz ekstrakta kućnih grinja
EP  - 522
IS  - 5
SP  - 513
VL  - 74
DO  - 10.2298/JSC0905513M
UR  - conv_22
ER  - 
@article{
author = "Milovanović, Katarina and Burazer, Lidija and Vučković, Olga and Atanasković-Marković, Marina and Ćirković-Veličković, Tanja and Jankov, Ratko and Gavrović-Jankulović, Marija",
year = "2009",
abstract = "House dust mites (HDM) represent a major source of allergens, contributing to the increasing incidence of type I hypersensitivity disease worldwide. Over 30 different IgE-binding proteins from the HDM extract were detected. Although group 1 and 2 have been identified as major allergens, due to the safety and efficacy of allergy diagnosis and immunotherapy, there is a need to carefully evaluate the clinical relevance of other allergens present in the HDM extract. In regard to this, a high molecular mass allergen of about 68 kD was purified from the HDM extract using a combination of gel permeation chromatography and reversed-phase chromatography. The IgG and IgE reactivity of the purified protein were preserved during the purification process, as confirmed by Western blot analysis with polyclonal rabbit antibodies and dot blot analysis with a pool of sera from subjects with house dust mite allergy, respectively. In addition, the IgE reactivity was confirmed using ELISA testing with nine patient sera. The biological potency of the 68 kD allergen was confirmed by skin prick testing in five allergic subjects, suggesting that the high molecular mass allergen is a good candidate for component-resolved diagnosis of house dust mite allergy and eventual therapeutic treatment., Grinje iz kućne prašine predstavljaju jedan od glavnih izvora alergena koji su u značajnoj meri doprineli porastu prvog tipa preosetljivosti. Preko 30 IgE-vezujućih proteina iz kućne prašine je detektovano do danas. Alergeni grupe 1 i 2 označeni su kao glavni alergeni kućne prašine. Međutim, da bi se poboljšala sigurnost i efikasnost dijagnoze i terapije alergijskih oboljenja izazvanih grinjama iz kućne prašine, neophodno je odrediti klinički značaj svih alergena iz ovog alergenskog izvora. U ovom radu izolovan je alergen visoke molekulske mase od 68 kD iz ekstrakta kućne prašine kombinovanjem gel-permeacione hromatografije i reversno-fazne hromatografije. IgG i IgE reaktivnost prečišćenog proteina je proverena u 'Western blot'-u i 'dot blot'-u sa poliklonskim zečijim antitelima na ekstrakt kućne prašine i 'pool'-om seruma osoba alergičnih na kućnu prašinu, redom. 64 % pacijenata je pokazalo IgE reaktivnost na prečišćeni protein u ELISA testu. Biološka reaktivnost prečišćenog alergena je potvrđena u kožnim probama na pet pacijenata, ukazujući da je prečišćen alergen dobar kandidat za dijagnozu alergije na kućnu prašinu pojedinačnim komponentama i eventualni terapeutski tretman.",
publisher = "Srpsko hemijsko društvo, Beograd",
journal = "Journal of the Serbian Chemical Society",
title = "Isolation and characterization of the 68 kD allergen from house dust mite Dermatophagoides pteronyssinus, Izolovanje i karakterizacija 68 kD alergena iz ekstrakta kućnih grinja",
pages = "522-513",
number = "5",
volume = "74",
doi = "10.2298/JSC0905513M",
url = "conv_22"
}
Milovanović, K., Burazer, L., Vučković, O., Atanasković-Marković, M., Ćirković-Veličković, T., Jankov, R.,& Gavrović-Jankulović, M.. (2009). Isolation and characterization of the 68 kD allergen from house dust mite Dermatophagoides pteronyssinus. in Journal of the Serbian Chemical Society
Srpsko hemijsko društvo, Beograd., 74(5), 513-522.
https://doi.org/10.2298/JSC0905513M
conv_22
Milovanović K, Burazer L, Vučković O, Atanasković-Marković M, Ćirković-Veličković T, Jankov R, Gavrović-Jankulović M. Isolation and characterization of the 68 kD allergen from house dust mite Dermatophagoides pteronyssinus. in Journal of the Serbian Chemical Society. 2009;74(5):513-522.
doi:10.2298/JSC0905513M
conv_22 .
Milovanović, Katarina, Burazer, Lidija, Vučković, Olga, Atanasković-Marković, Marina, Ćirković-Veličković, Tanja, Jankov, Ratko, Gavrović-Jankulović, Marija, "Isolation and characterization of the 68 kD allergen from house dust mite Dermatophagoides pteronyssinus" in Journal of the Serbian Chemical Society, 74, no. 5 (2009):513-522,
https://doi.org/10.2298/JSC0905513M .,
conv_22 .
1
1

Genetically engineered Phl p 1 is a suitable diagnostic marker for in vivo allergy diagnosis of timothy grass pollen allergy

Milovanović, Mina; Atanasković-Marković, Marina; Vučković, Olga; Becker, Wolf-Meinhard; Petersen, Arnd; Gavrović-Jankulović, Marija

(Wiley-Blackwell Publishing, Inc, Malden, 2009)

TY  - CONF
AU  - Milovanović, Mina
AU  - Atanasković-Marković, Marina
AU  - Vučković, Olga
AU  - Becker, Wolf-Meinhard
AU  - Petersen, Arnd
AU  - Gavrović-Jankulović, Marija
PY  - 2009
UR  - http://intor.torlakinstitut.com/handle/123456789/271
PB  - Wiley-Blackwell Publishing, Inc, Malden
C3  - Allergy
T1  - Genetically engineered Phl p 1 is a suitable diagnostic marker for in vivo allergy diagnosis of timothy grass pollen allergy
EP  - 80
SP  - 80
VL  - 64
UR  - conv_233
ER  - 
@conference{
author = "Milovanović, Mina and Atanasković-Marković, Marina and Vučković, Olga and Becker, Wolf-Meinhard and Petersen, Arnd and Gavrović-Jankulović, Marija",
year = "2009",
publisher = "Wiley-Blackwell Publishing, Inc, Malden",
journal = "Allergy",
title = "Genetically engineered Phl p 1 is a suitable diagnostic marker for in vivo allergy diagnosis of timothy grass pollen allergy",
pages = "80-80",
volume = "64",
url = "conv_233"
}
Milovanović, M., Atanasković-Marković, M., Vučković, O., Becker, W., Petersen, A.,& Gavrović-Jankulović, M.. (2009). Genetically engineered Phl p 1 is a suitable diagnostic marker for in vivo allergy diagnosis of timothy grass pollen allergy. in Allergy
Wiley-Blackwell Publishing, Inc, Malden., 64, 80-80.
conv_233
Milovanović M, Atanasković-Marković M, Vučković O, Becker W, Petersen A, Gavrović-Jankulović M. Genetically engineered Phl p 1 is a suitable diagnostic marker for in vivo allergy diagnosis of timothy grass pollen allergy. in Allergy. 2009;64:80-80.
conv_233 .
Milovanović, Mina, Atanasković-Marković, Marina, Vučković, Olga, Becker, Wolf-Meinhard, Petersen, Arnd, Gavrović-Jankulović, Marija, "Genetically engineered Phl p 1 is a suitable diagnostic marker for in vivo allergy diagnosis of timothy grass pollen allergy" in Allergy, 64 (2009):80-80,
conv_233 .

Intraoperative anaphylactic shock in a child with no history of type I hypersensitivity

Atanasković-Marković, Marina; Gavrović-Jankulović, Marija; Veličković, Tanja; Vučković, Olga; Ivanovski, P.; Nestorovic, Branimir; Čuturilo, G.; Simić, D.

(2008)

TY  - JOUR
AU  - Atanasković-Marković, Marina
AU  - Gavrović-Jankulović, Marija
AU  - Veličković, Tanja
AU  - Vučković, Olga
AU  - Ivanovski, P.
AU  - Nestorovic, Branimir
AU  - Čuturilo, G.
AU  - Simić, D.
PY  - 2008
UR  - http://intor.torlakinstitut.com/handle/123456789/264
AB  - Natural rubber latex is the second most implicated agent in intraoperative anaphylactic reactions. This report describes a case of intraoperative anaphylaxis occurring in a non-atopic fourteen-year-old girl undergoing multiple surgical procedures, but without spina bifida, in which latex surgical gloves were the main culprit for the anaphylactic reactions. Clinical manifestations of an anaphylactic reaction were also experienced during the examination of the possible cause of intraoperative anaphylaxis by skin prick testing with a latex allergen extract. Skin tests with anesthetics were negative. Specific IgE to latex was positive at 92.9 kUA/L (class 5). The molecular basis for the reported intraoperative anaphylaxis was ascribed to three low-molecular mass latex allergens (10-15 kD) detected in the brand of latex surgical gloves used during the operation. Given the potential of a dramatic outcome, latex allergy testing as a regular preoperative measure may contribute to the reduction of anaphylactic reactions during surgical interventions.
T2  - Iranian Journal of Allergy, Asthma and Immunology
T1  - Intraoperative anaphylactic shock in a child with no history of type I hypersensitivity
EP  - 99
IS  - 2
SP  - 97
VL  - 7
UR  - conv_561
ER  - 
@article{
author = "Atanasković-Marković, Marina and Gavrović-Jankulović, Marija and Veličković, Tanja and Vučković, Olga and Ivanovski, P. and Nestorovic, Branimir and Čuturilo, G. and Simić, D.",
year = "2008",
abstract = "Natural rubber latex is the second most implicated agent in intraoperative anaphylactic reactions. This report describes a case of intraoperative anaphylaxis occurring in a non-atopic fourteen-year-old girl undergoing multiple surgical procedures, but without spina bifida, in which latex surgical gloves were the main culprit for the anaphylactic reactions. Clinical manifestations of an anaphylactic reaction were also experienced during the examination of the possible cause of intraoperative anaphylaxis by skin prick testing with a latex allergen extract. Skin tests with anesthetics were negative. Specific IgE to latex was positive at 92.9 kUA/L (class 5). The molecular basis for the reported intraoperative anaphylaxis was ascribed to three low-molecular mass latex allergens (10-15 kD) detected in the brand of latex surgical gloves used during the operation. Given the potential of a dramatic outcome, latex allergy testing as a regular preoperative measure may contribute to the reduction of anaphylactic reactions during surgical interventions.",
journal = "Iranian Journal of Allergy, Asthma and Immunology",
title = "Intraoperative anaphylactic shock in a child with no history of type I hypersensitivity",
pages = "99-97",
number = "2",
volume = "7",
url = "conv_561"
}
Atanasković-Marković, M., Gavrović-Jankulović, M., Veličković, T., Vučković, O., Ivanovski, P., Nestorovic, B., Čuturilo, G.,& Simić, D.. (2008). Intraoperative anaphylactic shock in a child with no history of type I hypersensitivity. in Iranian Journal of Allergy, Asthma and Immunology, 7(2), 97-99.
conv_561
Atanasković-Marković M, Gavrović-Jankulović M, Veličković T, Vučković O, Ivanovski P, Nestorovic B, Čuturilo G, Simić D. Intraoperative anaphylactic shock in a child with no history of type I hypersensitivity. in Iranian Journal of Allergy, Asthma and Immunology. 2008;7(2):97-99.
conv_561 .
Atanasković-Marković, Marina, Gavrović-Jankulović, Marija, Veličković, Tanja, Vučković, Olga, Ivanovski, P., Nestorovic, Branimir, Čuturilo, G., Simić, D., "Intraoperative anaphylactic shock in a child with no history of type I hypersensitivity" in Iranian Journal of Allergy, Asthma and Immunology, 7, no. 2 (2008):97-99,
conv_561 .
2

A recombinant kiwi cystatin is a novel reagent for evaluation of the clinical relevance on phytocystatins in kiwi fruit allergy

Popović, Milica; Burazer, Lidija; Atanasković-Marković, Marina; Milovanović, Mina; Ćirković-Veličković, Tanja; Petersen, Arnd; Jankov, Ratko; Becker, Wolf-Meinhard; Gavrović-Jankulović, Marija

(Blackwell Publishing, Oxford, 2008)

TY  - CONF
AU  - Popović, Milica
AU  - Burazer, Lidija
AU  - Atanasković-Marković, Marina
AU  - Milovanović, Mina
AU  - Ćirković-Veličković, Tanja
AU  - Petersen, Arnd
AU  - Jankov, Ratko
AU  - Becker, Wolf-Meinhard
AU  - Gavrović-Jankulović, Marija
PY  - 2008
UR  - http://intor.torlakinstitut.com/handle/123456789/255
PB  - Blackwell Publishing, Oxford
C3  - Allergy
T1  - A recombinant kiwi cystatin is a novel reagent for evaluation of the clinical relevance on phytocystatins in kiwi fruit allergy
EP  - 573
SP  - 573
VL  - 63
UR  - conv_211
ER  - 
@conference{
author = "Popović, Milica and Burazer, Lidija and Atanasković-Marković, Marina and Milovanović, Mina and Ćirković-Veličković, Tanja and Petersen, Arnd and Jankov, Ratko and Becker, Wolf-Meinhard and Gavrović-Jankulović, Marija",
year = "2008",
publisher = "Blackwell Publishing, Oxford",
journal = "Allergy",
title = "A recombinant kiwi cystatin is a novel reagent for evaluation of the clinical relevance on phytocystatins in kiwi fruit allergy",
pages = "573-573",
volume = "63",
url = "conv_211"
}
Popović, M., Burazer, L., Atanasković-Marković, M., Milovanović, M., Ćirković-Veličković, T., Petersen, A., Jankov, R., Becker, W.,& Gavrović-Jankulović, M.. (2008). A recombinant kiwi cystatin is a novel reagent for evaluation of the clinical relevance on phytocystatins in kiwi fruit allergy. in Allergy
Blackwell Publishing, Oxford., 63, 573-573.
conv_211
Popović M, Burazer L, Atanasković-Marković M, Milovanović M, Ćirković-Veličković T, Petersen A, Jankov R, Becker W, Gavrović-Jankulović M. A recombinant kiwi cystatin is a novel reagent for evaluation of the clinical relevance on phytocystatins in kiwi fruit allergy. in Allergy. 2008;63:573-573.
conv_211 .
Popović, Milica, Burazer, Lidija, Atanasković-Marković, Marina, Milovanović, Mina, Ćirković-Veličković, Tanja, Petersen, Arnd, Jankov, Ratko, Becker, Wolf-Meinhard, Gavrović-Jankulović, Marija, "A recombinant kiwi cystatin is a novel reagent for evaluation of the clinical relevance on phytocystatins in kiwi fruit allergy" in Allergy, 63 (2008):573-573,
conv_211 .

Chemical modification of major mugwort pollen allergen Art v1 by citraconylation and cis-aconitylation

Stanić, Dragana; Milovanović, Mina; Atanasković-Marković, Marina; Burazer, Lidija; Jankov, Ratko; Ćirković-Veličković, Tanja

(Wiley-Blackwell, Malden, 2008)

TY  - CONF
AU  - Stanić, Dragana
AU  - Milovanović, Mina
AU  - Atanasković-Marković, Marina
AU  - Burazer, Lidija
AU  - Jankov, Ratko
AU  - Ćirković-Veličković, Tanja
PY  - 2008
UR  - http://intor.torlakinstitut.com/handle/123456789/254
PB  - Wiley-Blackwell, Malden
C3  - Allergy
T1  - Chemical modification of major mugwort pollen allergen Art v1 by citraconylation and cis-aconitylation
EP  - 496
SP  - 496
VL  - 63
UR  - conv_210
ER  - 
@conference{
author = "Stanić, Dragana and Milovanović, Mina and Atanasković-Marković, Marina and Burazer, Lidija and Jankov, Ratko and Ćirković-Veličković, Tanja",
year = "2008",
publisher = "Wiley-Blackwell, Malden",
journal = "Allergy",
title = "Chemical modification of major mugwort pollen allergen Art v1 by citraconylation and cis-aconitylation",
pages = "496-496",
volume = "63",
url = "conv_210"
}
Stanić, D., Milovanović, M., Atanasković-Marković, M., Burazer, L., Jankov, R.,& Ćirković-Veličković, T.. (2008). Chemical modification of major mugwort pollen allergen Art v1 by citraconylation and cis-aconitylation. in Allergy
Wiley-Blackwell, Malden., 63, 496-496.
conv_210
Stanić D, Milovanović M, Atanasković-Marković M, Burazer L, Jankov R, Ćirković-Veličković T. Chemical modification of major mugwort pollen allergen Art v1 by citraconylation and cis-aconitylation. in Allergy. 2008;63:496-496.
conv_210 .
Stanić, Dragana, Milovanović, Mina, Atanasković-Marković, Marina, Burazer, Lidija, Jankov, Ratko, Ćirković-Veličković, Tanja, "Chemical modification of major mugwort pollen allergen Art v1 by citraconylation and cis-aconitylation" in Allergy, 63 (2008):496-496,
conv_210 .

A matrix effect in pectin-rich fruits hampers digestion of allergen by pepsin in vivo and in vitro

Polović, Natalija; Blanuša, Milan; Gavrović-Jankulović, Marija; Atanasković-Marković, Marina; Burazer, Lidija; Jankov, Ratko; Veličković, Tanja

(2007)

TY  - JOUR
AU  - Polović, Natalija
AU  - Blanuša, Milan
AU  - Gavrović-Jankulović, Marija
AU  - Atanasković-Marković, Marina
AU  - Burazer, Lidija
AU  - Jankov, Ratko
AU  - Veličković, Tanja
PY  - 2007
UR  - http://intor.torlakinstitut.com/handle/123456789/225
AB  - Background: It is a general belief that a food allergen should be stable to gastric digestion. Various acidic plant polysaccharides, including pectin, are ubiquitous in fruit matrixes and can form hydrogels under low-pH conditions. Objective: The purpose of this study was to investigate the effect of hydrogel forming polysaccharide-rich fruit matrixes on in vivo gastric and in vitro pepsic digestion of fruit allergens. Methods: Fruit extract proteins (kiwi, banana, apple and cherry) and a purified major kiwi allergen Act c 2 were digested with simulated gastric fluid in accordance with the US Pharmacopeia. In vivo experiments on kiwi fruit digestion were performed on four healthy non-atopic volunteers by examining the gastric content 1 h after ingestion of kiwi fruit. The Act c 2 and kiwi proteins were detected in immunoblots using monoclonal anti-Act c 2 antibodies and rabbit polyclonal antisera. Results: Crude fruit extracts were resistant to digestion by pepsin when compared with commonly prepared extracts. In the gastric content of all volunteers, following kiwi fruit ingestion and immunoblotting, intact Act c 2 was detected with anti-Act c 2 monoclonal antibodies, while kiwi proteins of higher molecular weights were detected using rabbit polyclonal antisera. Addition of apple fruit pectin (1.5% and 3%) to the purified kiwi allergen was able to protect it from pepsin digestion in vitro. Conclusion: The matrix effect in pectin-rich fruits can influence the digestibility of food proteins and thereby the process of allergic sensitization in atopic individuals.
T2  - Clinical and Experimental Allergy
T1  - A matrix effect in pectin-rich fruits hampers digestion of allergen by pepsin in vivo and in vitro
EP  - 771
IS  - 5
SP  - 764
VL  - 37
DO  - 10.1111/j.1365-2222.2007.02703.x
UR  - conv_508
ER  - 
@article{
author = "Polović, Natalija and Blanuša, Milan and Gavrović-Jankulović, Marija and Atanasković-Marković, Marina and Burazer, Lidija and Jankov, Ratko and Veličković, Tanja",
year = "2007",
abstract = "Background: It is a general belief that a food allergen should be stable to gastric digestion. Various acidic plant polysaccharides, including pectin, are ubiquitous in fruit matrixes and can form hydrogels under low-pH conditions. Objective: The purpose of this study was to investigate the effect of hydrogel forming polysaccharide-rich fruit matrixes on in vivo gastric and in vitro pepsic digestion of fruit allergens. Methods: Fruit extract proteins (kiwi, banana, apple and cherry) and a purified major kiwi allergen Act c 2 were digested with simulated gastric fluid in accordance with the US Pharmacopeia. In vivo experiments on kiwi fruit digestion were performed on four healthy non-atopic volunteers by examining the gastric content 1 h after ingestion of kiwi fruit. The Act c 2 and kiwi proteins were detected in immunoblots using monoclonal anti-Act c 2 antibodies and rabbit polyclonal antisera. Results: Crude fruit extracts were resistant to digestion by pepsin when compared with commonly prepared extracts. In the gastric content of all volunteers, following kiwi fruit ingestion and immunoblotting, intact Act c 2 was detected with anti-Act c 2 monoclonal antibodies, while kiwi proteins of higher molecular weights were detected using rabbit polyclonal antisera. Addition of apple fruit pectin (1.5% and 3%) to the purified kiwi allergen was able to protect it from pepsin digestion in vitro. Conclusion: The matrix effect in pectin-rich fruits can influence the digestibility of food proteins and thereby the process of allergic sensitization in atopic individuals.",
journal = "Clinical and Experimental Allergy",
title = "A matrix effect in pectin-rich fruits hampers digestion of allergen by pepsin in vivo and in vitro",
pages = "771-764",
number = "5",
volume = "37",
doi = "10.1111/j.1365-2222.2007.02703.x",
url = "conv_508"
}
Polović, N., Blanuša, M., Gavrović-Jankulović, M., Atanasković-Marković, M., Burazer, L., Jankov, R.,& Veličković, T.. (2007). A matrix effect in pectin-rich fruits hampers digestion of allergen by pepsin in vivo and in vitro. in Clinical and Experimental Allergy, 37(5), 764-771.
https://doi.org/10.1111/j.1365-2222.2007.02703.x
conv_508
Polović N, Blanuša M, Gavrović-Jankulović M, Atanasković-Marković M, Burazer L, Jankov R, Veličković T. A matrix effect in pectin-rich fruits hampers digestion of allergen by pepsin in vivo and in vitro. in Clinical and Experimental Allergy. 2007;37(5):764-771.
doi:10.1111/j.1365-2222.2007.02703.x
conv_508 .
Polović, Natalija, Blanuša, Milan, Gavrović-Jankulović, Marija, Atanasković-Marković, Marina, Burazer, Lidija, Jankov, Ratko, Veličković, Tanja, "A matrix effect in pectin-rich fruits hampers digestion of allergen by pepsin in vivo and in vitro" in Clinical and Experimental Allergy, 37, no. 5 (2007):764-771,
https://doi.org/10.1111/j.1365-2222.2007.02703.x .,
conv_508 .
58
45
54

Intraoperative anaphylactic shock in a child with undiagnosed latex allergy

Atanasković-Marković, Marina; Gavrović-Jankulović, Marija; Ćirković-Veličković, Tanja; Međo, B.; Kukolj, D.; Nestorovic, Branimir; Vučković, Olga

(Blackwell Publishing, Oxford, 2007)

TY  - CONF
AU  - Atanasković-Marković, Marina
AU  - Gavrović-Jankulović, Marija
AU  - Ćirković-Veličković, Tanja
AU  - Međo, B.
AU  - Kukolj, D.
AU  - Nestorovic, Branimir
AU  - Vučković, Olga
PY  - 2007
UR  - http://intor.torlakinstitut.com/handle/123456789/235
PB  - Blackwell Publishing, Oxford
C3  - Allergy
T1  - Intraoperative anaphylactic shock in a child with undiagnosed latex allergy
EP  - 80
SP  - 80
VL  - 62
UR  - conv_196
ER  - 
@conference{
author = "Atanasković-Marković, Marina and Gavrović-Jankulović, Marija and Ćirković-Veličković, Tanja and Međo, B. and Kukolj, D. and Nestorovic, Branimir and Vučković, Olga",
year = "2007",
publisher = "Blackwell Publishing, Oxford",
journal = "Allergy",
title = "Intraoperative anaphylactic shock in a child with undiagnosed latex allergy",
pages = "80-80",
volume = "62",
url = "conv_196"
}
Atanasković-Marković, M., Gavrović-Jankulović, M., Ćirković-Veličković, T., Međo, B., Kukolj, D., Nestorovic, B.,& Vučković, O.. (2007). Intraoperative anaphylactic shock in a child with undiagnosed latex allergy. in Allergy
Blackwell Publishing, Oxford., 62, 80-80.
conv_196
Atanasković-Marković M, Gavrović-Jankulović M, Ćirković-Veličković T, Međo B, Kukolj D, Nestorovic B, Vučković O. Intraoperative anaphylactic shock in a child with undiagnosed latex allergy. in Allergy. 2007;62:80-80.
conv_196 .
Atanasković-Marković, Marina, Gavrović-Jankulović, Marija, Ćirković-Veličković, Tanja, Međo, B., Kukolj, D., Nestorovic, Branimir, Vučković, Olga, "Intraoperative anaphylactic shock in a child with undiagnosed latex allergy" in Allergy, 62 (2007):80-80,
conv_196 .

Authors reply to beta-lactam allergy in children

Atanasković-Marković, Marina; Ćirković-Veličković, Tanja; Gavrović-Jankulović, Marija; Vučković, Olga; Nestorovic, Branimir

(Blackwell Munksgaard, 2006)

TY  - JOUR
AU  - Atanasković-Marković, Marina
AU  - Ćirković-Veličković, Tanja
AU  - Gavrović-Jankulović, Marija
AU  - Vučković, Olga
AU  - Nestorovic, Branimir
PY  - 2006
UR  - http://intor.torlakinstitut.com/handle/123456789/214
PB  - Blackwell Munksgaard
T2  - Pediatric Allergy and Immunology
T1  - Authors reply to beta-lactam allergy in children
EP  - 640
IS  - 8
SP  - 639
VL  - 17
DO  - 10.1111/j.1399-3038.2006.00462.x
UR  - conv_593
ER  - 
@article{
author = "Atanasković-Marković, Marina and Ćirković-Veličković, Tanja and Gavrović-Jankulović, Marija and Vučković, Olga and Nestorovic, Branimir",
year = "2006",
publisher = "Blackwell Munksgaard",
journal = "Pediatric Allergy and Immunology",
title = "Authors reply to beta-lactam allergy in children",
pages = "640-639",
number = "8",
volume = "17",
doi = "10.1111/j.1399-3038.2006.00462.x",
url = "conv_593"
}
Atanasković-Marković, M., Ćirković-Veličković, T., Gavrović-Jankulović, M., Vučković, O.,& Nestorovic, B.. (2006). Authors reply to beta-lactam allergy in children. in Pediatric Allergy and Immunology
Blackwell Munksgaard., 17(8), 639-640.
https://doi.org/10.1111/j.1399-3038.2006.00462.x
conv_593
Atanasković-Marković M, Ćirković-Veličković T, Gavrović-Jankulović M, Vučković O, Nestorovic B. Authors reply to beta-lactam allergy in children. in Pediatric Allergy and Immunology. 2006;17(8):639-640.
doi:10.1111/j.1399-3038.2006.00462.x
conv_593 .
Atanasković-Marković, Marina, Ćirković-Veličković, Tanja, Gavrović-Jankulović, Marija, Vučković, Olga, Nestorovic, Branimir, "Authors reply to beta-lactam allergy in children" in Pediatric Allergy and Immunology, 17, no. 8 (2006):639-640,
https://doi.org/10.1111/j.1399-3038.2006.00462.x .,
conv_593 .
1

Artemisia vulgaris pollen allergoids digestibility in the simulated conditions of the gastrointestinal tract

Ćirković-Veličković, Tanja; Polović, Natalija; Gavrović-Jankulović, Marija; Burazer, Lidija; Đergović-Petrović, Danica; Vučković, Olga; Drobnjak, Olika; Šporčić, Zorica; Atanasković-Marković, Marina; Jankov, Ratko

(Srpsko hemijsko društvo, Beograd, 2006)

TY  - JOUR
AU  - Ćirković-Veličković, Tanja
AU  - Polović, Natalija
AU  - Gavrović-Jankulović, Marija
AU  - Burazer, Lidija
AU  - Đergović-Petrović, Danica
AU  - Vučković, Olga
AU  - Drobnjak, Olika
AU  - Šporčić, Zorica
AU  - Atanasković-Marković, Marina
AU  - Jankov, Ratko
PY  - 2006
UR  - http://intor.torlakinstitut.com/handle/123456789/220
AB  - Chemically modified allergens (allergoids) have found use in both traditional and novel forms of immunotherapy of allergic disorders. Novel forms of immunotherapy include local allergen delivery, via the gastrointestinal tract. This study conveys the gastrointestinal stability of three types of mugwort pollen allergoids under simulated conditions of the gut. Allergoids of the pollen extract of Artemisia vulgaris were obtained by means of potassium cyanate, succinic and maleic anhydride. Gastrointestinal tract conditions (saliva, and gastric fluid) were simulated in accordance with the EU Pharmacopoeia. The biochemical and immunochemical properties of the derivatives following exposure to different conditions were monitored by determining the number of residual amino groups with 2,4,6-trinitrobenzenesulfonic acid, SDS PAGE, immunoblotting and inhibition of mugwort-specific IgE. Exposure to saliva fluid for 2 min did not influence the biochemical and immunochemical properties of the derivatives. In the very acidic conditions of the simulated gastric fluid, the degree of demaleylation and desuccinylation, even after 4 h exposure, was low, ranging from 10 to 30 %. The digestion patterns with pepsin proceeded rapidly in both the unmodified and modified samples. In all four cases, a highly resistant IgE-binding protein the Mwof which was about 28-35 kD, was present. Within the physiological conditions, no new IgE binding epitopes were revealed, as demonstrated by immunoblot and CAP inhibition of the mugwort specific IgE binding. An important conclusion of this study is the stability of the modified derivatives in the gastrointestinal tract of patients, within physiological conditions. The means that they are suitable for use in much higher concentrations in local forms of immunotherapy than unmodified ones.
AB  - U ovom radu su prikazani rezultati ispitivanja stabilnosti tri tipa alergoida polena pelina u simuliranom želudačnom soku. Koristeći kalijum-cijanat anhidrid ćilibarne i anhidrid maleinske kiseline, napravljeni su alergoidi polena pelina (Artemisia vulgaris). Saliva i želudačni sok su simulirani na osnovu evropske farmakopeje. Biohemijske i imunohemijske osobine derivata posle izlaganja različitim uslovima, praćene su: određivanjem broja slobodnih amino grupa u reakciji sa TNBS, SDS PAG elektroforezom, imunoblotom i određivanjem pelin-specifičnog imunoglobulina E (IgE). Izlaganje salivi u trajanju od 2 minuta ne utiče na biohemijske i imunohemijske osobine derivata. U kiseloj sredini želudačnog soka ne dolazi do značajnog demaleilovawa i desukcinilovanja. Čak i posle četvoročasovnog izlaganja, taj procenat je u opsegu 10-30 %. Alergoidi pelina se trenutno digestuju pepsinom, sa izuzetkom visoko rezistentne proteinske trake molekulske mase 28-35 kD, koja odgovara važnom IgE-vezujućem proteinu polena pelina. Imunoblotom i CAP-inhibicijom je pokazano da, u okviru fizioloških uslova, ne dolazi do stvaranja novih IgE-vezujućih epitopa. Hemijska stabilnost modifikovanih derivata u simuliranim uslovima želudačnog soka omogućuje da se tokom imunoterapije mogu primenjivati veće doze alergoida nego nemodifikovanog ekstrakta polena pelina.
PB  - Srpsko hemijsko društvo, Beograd
T2  - Journal of the Serbian Chemical Society
T1  - Artemisia vulgaris pollen allergoids digestibility in the simulated conditions of the gastrointestinal tract
T1  - Digestibilnost alergoida polena pelina u simuliranim uslovima gastrointestinalnog trakta
EP  - 888
IS  - 8-9
SP  - 879
VL  - 71
DO  - 10.2298/JSC0609879C
UR  - conv_19
ER  - 
@article{
author = "Ćirković-Veličković, Tanja and Polović, Natalija and Gavrović-Jankulović, Marija and Burazer, Lidija and Đergović-Petrović, Danica and Vučković, Olga and Drobnjak, Olika and Šporčić, Zorica and Atanasković-Marković, Marina and Jankov, Ratko",
year = "2006",
abstract = "Chemically modified allergens (allergoids) have found use in both traditional and novel forms of immunotherapy of allergic disorders. Novel forms of immunotherapy include local allergen delivery, via the gastrointestinal tract. This study conveys the gastrointestinal stability of three types of mugwort pollen allergoids under simulated conditions of the gut. Allergoids of the pollen extract of Artemisia vulgaris were obtained by means of potassium cyanate, succinic and maleic anhydride. Gastrointestinal tract conditions (saliva, and gastric fluid) were simulated in accordance with the EU Pharmacopoeia. The biochemical and immunochemical properties of the derivatives following exposure to different conditions were monitored by determining the number of residual amino groups with 2,4,6-trinitrobenzenesulfonic acid, SDS PAGE, immunoblotting and inhibition of mugwort-specific IgE. Exposure to saliva fluid for 2 min did not influence the biochemical and immunochemical properties of the derivatives. In the very acidic conditions of the simulated gastric fluid, the degree of demaleylation and desuccinylation, even after 4 h exposure, was low, ranging from 10 to 30 %. The digestion patterns with pepsin proceeded rapidly in both the unmodified and modified samples. In all four cases, a highly resistant IgE-binding protein the Mwof which was about 28-35 kD, was present. Within the physiological conditions, no new IgE binding epitopes were revealed, as demonstrated by immunoblot and CAP inhibition of the mugwort specific IgE binding. An important conclusion of this study is the stability of the modified derivatives in the gastrointestinal tract of patients, within physiological conditions. The means that they are suitable for use in much higher concentrations in local forms of immunotherapy than unmodified ones., U ovom radu su prikazani rezultati ispitivanja stabilnosti tri tipa alergoida polena pelina u simuliranom želudačnom soku. Koristeći kalijum-cijanat anhidrid ćilibarne i anhidrid maleinske kiseline, napravljeni su alergoidi polena pelina (Artemisia vulgaris). Saliva i želudačni sok su simulirani na osnovu evropske farmakopeje. Biohemijske i imunohemijske osobine derivata posle izlaganja različitim uslovima, praćene su: određivanjem broja slobodnih amino grupa u reakciji sa TNBS, SDS PAG elektroforezom, imunoblotom i određivanjem pelin-specifičnog imunoglobulina E (IgE). Izlaganje salivi u trajanju od 2 minuta ne utiče na biohemijske i imunohemijske osobine derivata. U kiseloj sredini želudačnog soka ne dolazi do značajnog demaleilovawa i desukcinilovanja. Čak i posle četvoročasovnog izlaganja, taj procenat je u opsegu 10-30 %. Alergoidi pelina se trenutno digestuju pepsinom, sa izuzetkom visoko rezistentne proteinske trake molekulske mase 28-35 kD, koja odgovara važnom IgE-vezujućem proteinu polena pelina. Imunoblotom i CAP-inhibicijom je pokazano da, u okviru fizioloških uslova, ne dolazi do stvaranja novih IgE-vezujućih epitopa. Hemijska stabilnost modifikovanih derivata u simuliranim uslovima želudačnog soka omogućuje da se tokom imunoterapije mogu primenjivati veće doze alergoida nego nemodifikovanog ekstrakta polena pelina.",
publisher = "Srpsko hemijsko društvo, Beograd",
journal = "Journal of the Serbian Chemical Society",
title = "Artemisia vulgaris pollen allergoids digestibility in the simulated conditions of the gastrointestinal tract, Digestibilnost alergoida polena pelina u simuliranim uslovima gastrointestinalnog trakta",
pages = "888-879",
number = "8-9",
volume = "71",
doi = "10.2298/JSC0609879C",
url = "conv_19"
}
Ćirković-Veličković, T., Polović, N., Gavrović-Jankulović, M., Burazer, L., Đergović-Petrović, D., Vučković, O., Drobnjak, O., Šporčić, Z., Atanasković-Marković, M.,& Jankov, R.. (2006). Artemisia vulgaris pollen allergoids digestibility in the simulated conditions of the gastrointestinal tract. in Journal of the Serbian Chemical Society
Srpsko hemijsko društvo, Beograd., 71(8-9), 879-888.
https://doi.org/10.2298/JSC0609879C
conv_19
Ćirković-Veličković T, Polović N, Gavrović-Jankulović M, Burazer L, Đergović-Petrović D, Vučković O, Drobnjak O, Šporčić Z, Atanasković-Marković M, Jankov R. Artemisia vulgaris pollen allergoids digestibility in the simulated conditions of the gastrointestinal tract. in Journal of the Serbian Chemical Society. 2006;71(8-9):879-888.
doi:10.2298/JSC0609879C
conv_19 .
Ćirković-Veličković, Tanja, Polović, Natalija, Gavrović-Jankulović, Marija, Burazer, Lidija, Đergović-Petrović, Danica, Vučković, Olga, Drobnjak, Olika, Šporčić, Zorica, Atanasković-Marković, Marina, Jankov, Ratko, "Artemisia vulgaris pollen allergoids digestibility in the simulated conditions of the gastrointestinal tract" in Journal of the Serbian Chemical Society, 71, no. 8-9 (2006):879-888,
https://doi.org/10.2298/JSC0609879C .,
conv_19 .
1

Immediate allergic reactions to cephalosporins and penicillins and their cross-reactivity in children

Atanasković-Marković, Marina; Veličković, Tanja; Gavrović-Jankulović, Marija; Vučković, Olga; Nestorovic, Branimir

(Blackwell Munksgaard, 2005)

TY  - JOUR
AU  - Atanasković-Marković, Marina
AU  - Veličković, Tanja
AU  - Gavrović-Jankulović, Marija
AU  - Vučković, Olga
AU  - Nestorovic, Branimir
PY  - 2005
UR  - http://intor.torlakinstitut.com/handle/123456789/203
AB  - Penicillins and cephalosporins are the most important betalactams inducing IgE-mediated reactions. The safety of administering cephalosporins to penicillin-allergic children is a particular problem, because cephalosporin allergenic determinants have not been properly identified. A study was undertaken to evaluate the frequency of anaphylactic reactions to cephalosporins and penicillins and their cross-reactivity in a pediatric population. A prospective survey was conducted in a group of 1170 children with suspected immediate allergic reactions to cephalosporins and/or penicillins, which were examined during a period of 8 yr. In vivo (skin tests and challenges) and in vitro tests (for specific IgE) were performed with standard concentration of penicillins and cephalosporins. When 1170 children with a clinical history of allergy to penicillins and/or cephalosporins were tested in vivo for immediate hypersensitivity to betalactams, 58.3% cases overall were found to be skin or challenge test positive. Among them, 94.4% patients were positive to penicillins and 35.3% to cephalosporins. The frequency of positive reactions in the in vivo testing was in the range from 36.4% to 88.1% for penicillins and from 0.3% to 29.2% for cephalosporins. However, 31.5% of the penicillin allergic children cross-reacted to some cephalosporin. If a child was allergic to a cephalosporin, the frequency of positive reactions to penicillin was 84.2%. The cross-reactivity between cephalosporins and penicillins varied between 0.3% and 23.9%. The cross-reactivity among different generations of cephalosporins varied between 0% and 68.8%, being the highest for first and second-generation cephalosporins and 0% for third generation cephalosporins. The frequency of immediate allergic reactions to cephalosporins is considerably lower compared to penicillins, and the degree of cross-reactivity between cephalosporins and penicillins depends on the generation of cephalosporins, being higher with earlier generation cephalosporins. The cross-reactivity among cephalosporins is lower compared to cross-reactivity between penicillins and cephalosporins.
PB  - Blackwell Munksgaard
T2  - Pediatric Allergy and Immunology
T1  - Immediate allergic reactions to cephalosporins and penicillins and their cross-reactivity in children
EP  - 347
IS  - 4
SP  - 341
VL  - 16
DO  - 10.1111/j.1399-3038.2005.00280.x
UR  - conv_506
ER  - 
@article{
author = "Atanasković-Marković, Marina and Veličković, Tanja and Gavrović-Jankulović, Marija and Vučković, Olga and Nestorovic, Branimir",
year = "2005",
abstract = "Penicillins and cephalosporins are the most important betalactams inducing IgE-mediated reactions. The safety of administering cephalosporins to penicillin-allergic children is a particular problem, because cephalosporin allergenic determinants have not been properly identified. A study was undertaken to evaluate the frequency of anaphylactic reactions to cephalosporins and penicillins and their cross-reactivity in a pediatric population. A prospective survey was conducted in a group of 1170 children with suspected immediate allergic reactions to cephalosporins and/or penicillins, which were examined during a period of 8 yr. In vivo (skin tests and challenges) and in vitro tests (for specific IgE) were performed with standard concentration of penicillins and cephalosporins. When 1170 children with a clinical history of allergy to penicillins and/or cephalosporins were tested in vivo for immediate hypersensitivity to betalactams, 58.3% cases overall were found to be skin or challenge test positive. Among them, 94.4% patients were positive to penicillins and 35.3% to cephalosporins. The frequency of positive reactions in the in vivo testing was in the range from 36.4% to 88.1% for penicillins and from 0.3% to 29.2% for cephalosporins. However, 31.5% of the penicillin allergic children cross-reacted to some cephalosporin. If a child was allergic to a cephalosporin, the frequency of positive reactions to penicillin was 84.2%. The cross-reactivity between cephalosporins and penicillins varied between 0.3% and 23.9%. The cross-reactivity among different generations of cephalosporins varied between 0% and 68.8%, being the highest for first and second-generation cephalosporins and 0% for third generation cephalosporins. The frequency of immediate allergic reactions to cephalosporins is considerably lower compared to penicillins, and the degree of cross-reactivity between cephalosporins and penicillins depends on the generation of cephalosporins, being higher with earlier generation cephalosporins. The cross-reactivity among cephalosporins is lower compared to cross-reactivity between penicillins and cephalosporins.",
publisher = "Blackwell Munksgaard",
journal = "Pediatric Allergy and Immunology",
title = "Immediate allergic reactions to cephalosporins and penicillins and their cross-reactivity in children",
pages = "347-341",
number = "4",
volume = "16",
doi = "10.1111/j.1399-3038.2005.00280.x",
url = "conv_506"
}
Atanasković-Marković, M., Veličković, T., Gavrović-Jankulović, M., Vučković, O.,& Nestorovic, B.. (2005). Immediate allergic reactions to cephalosporins and penicillins and their cross-reactivity in children. in Pediatric Allergy and Immunology
Blackwell Munksgaard., 16(4), 341-347.
https://doi.org/10.1111/j.1399-3038.2005.00280.x
conv_506
Atanasković-Marković M, Veličković T, Gavrović-Jankulović M, Vučković O, Nestorovic B. Immediate allergic reactions to cephalosporins and penicillins and their cross-reactivity in children. in Pediatric Allergy and Immunology. 2005;16(4):341-347.
doi:10.1111/j.1399-3038.2005.00280.x
conv_506 .
Atanasković-Marković, Marina, Veličković, Tanja, Gavrović-Jankulović, Marija, Vučković, Olga, Nestorovic, Branimir, "Immediate allergic reactions to cephalosporins and penicillins and their cross-reactivity in children" in Pediatric Allergy and Immunology, 16, no. 4 (2005):341-347,
https://doi.org/10.1111/j.1399-3038.2005.00280.x .,
conv_506 .
9
86
75
92

Allergenic potency of kiwi fruit during fruit development

Gavrović-Jankulović, Marija; Polović, Natalija; Prisić, S.; Jankov, Ratko; Atanasković-Marković, Marina; Vučković, Olga; Ćirković-Veličković, Tanja

(Taylor & Francis Ltd, Abingdon, 2005)

TY  - JOUR
AU  - Gavrović-Jankulović, Marija
AU  - Polović, Natalija
AU  - Prisić, S.
AU  - Jankov, Ratko
AU  - Atanasković-Marković, Marina
AU  - Vučković, Olga
AU  - Ćirković-Veličković, Tanja
PY  - 2005
UR  - http://intor.torlakinstitut.com/handle/123456789/201
AB  - Food allergies, including kiwi fruit allergy, have been the subject of extensive research in the last few years. The aim of this study was to examine a possible relationship between the developmental stage of kiwi fruit and its allergenic potency. The protein and allergen patterns of kiwi fruit extracts in September, October, November and December fruit in the period from 2000-2002 were analysed. One of the factors that may contribute to the difficulties in proposing well-defined and standardized fruit extracts should also be the time of fruit harvesting. In this particular case, when the kiwi fruit was edible throughout November and December, we showed discrepancies in allergen content and potencies both in qualitative and quantitative terms. Two major allergens of kiwi fruit, Act c 1 and Act c 2, mainly accounted for the highest allergenic potential of November kiwi extract in vivo and in vitro. Not only the content of major allergens, but also the ratio of different proteins and even isoforms of the same allergen (Act c 2) change with fruit ripening. These findings should be taken into account during preparation of extracts for allergy diagnosis.
PB  - Taylor & Francis Ltd, Abingdon
T2  - Food and Agricultural Immunology
T1  - Allergenic potency of kiwi fruit during fruit development
EP  - 128
IS  - 2
SP  - 117
VL  - 16
DO  - 10.1080/09540100500090804
UR  - conv_174
ER  - 
@article{
author = "Gavrović-Jankulović, Marija and Polović, Natalija and Prisić, S. and Jankov, Ratko and Atanasković-Marković, Marina and Vučković, Olga and Ćirković-Veličković, Tanja",
year = "2005",
abstract = "Food allergies, including kiwi fruit allergy, have been the subject of extensive research in the last few years. The aim of this study was to examine a possible relationship between the developmental stage of kiwi fruit and its allergenic potency. The protein and allergen patterns of kiwi fruit extracts in September, October, November and December fruit in the period from 2000-2002 were analysed. One of the factors that may contribute to the difficulties in proposing well-defined and standardized fruit extracts should also be the time of fruit harvesting. In this particular case, when the kiwi fruit was edible throughout November and December, we showed discrepancies in allergen content and potencies both in qualitative and quantitative terms. Two major allergens of kiwi fruit, Act c 1 and Act c 2, mainly accounted for the highest allergenic potential of November kiwi extract in vivo and in vitro. Not only the content of major allergens, but also the ratio of different proteins and even isoforms of the same allergen (Act c 2) change with fruit ripening. These findings should be taken into account during preparation of extracts for allergy diagnosis.",
publisher = "Taylor & Francis Ltd, Abingdon",
journal = "Food and Agricultural Immunology",
title = "Allergenic potency of kiwi fruit during fruit development",
pages = "128-117",
number = "2",
volume = "16",
doi = "10.1080/09540100500090804",
url = "conv_174"
}
Gavrović-Jankulović, M., Polović, N., Prisić, S., Jankov, R., Atanasković-Marković, M., Vučković, O.,& Ćirković-Veličković, T.. (2005). Allergenic potency of kiwi fruit during fruit development. in Food and Agricultural Immunology
Taylor & Francis Ltd, Abingdon., 16(2), 117-128.
https://doi.org/10.1080/09540100500090804
conv_174
Gavrović-Jankulović M, Polović N, Prisić S, Jankov R, Atanasković-Marković M, Vučković O, Ćirković-Veličković T. Allergenic potency of kiwi fruit during fruit development. in Food and Agricultural Immunology. 2005;16(2):117-128.
doi:10.1080/09540100500090804
conv_174 .
Gavrović-Jankulović, Marija, Polović, Natalija, Prisić, S., Jankov, Ratko, Atanasković-Marković, Marina, Vučković, Olga, Ćirković-Veličković, Tanja, "Allergenic potency of kiwi fruit during fruit development" in Food and Agricultural Immunology, 16, no. 2 (2005):117-128,
https://doi.org/10.1080/09540100500090804 .,
conv_174 .
29
28
32

Isolation and biochemical characterization of a thaumatin-like kiwi allergen

Gavrović-Jankulović, Marija; Ćirković, Tanja; Vučković, Olga; Atanasković-Marković, Marina; Petersen, Arnd; Gojgić, G.; Burazer, Lidija; Jankov, Ratko

(Mosby-Elsevier, New York, 2002)

TY  - JOUR
AU  - Gavrović-Jankulović, Marija
AU  - Ćirković, Tanja
AU  - Vučković, Olga
AU  - Atanasković-Marković, Marina
AU  - Petersen, Arnd
AU  - Gojgić, G.
AU  - Burazer, Lidija
AU  - Jankov, Ratko
PY  - 2002
UR  - http://intor.torlakinstitut.com/handle/123456789/150
AB  - Background: Kiwi fruit allergy, as well as its association with hypersensitivity to other foods and to pollen, has been extensively reported in the last few years. Several IgE-binding components have been detected in kiwi extract, but only one 30-kd allergen has been isolated; it was identified as actinidin (Act c 1). Recently, we have reported a 24-kd kiwi protein to be a potential major allergen in a group of patients with oral allergy syndrome (OAS). Objective: The aim of this study was to purify and characterize the 24-kd kiwi allergen biochemically. Methods: Seven polysensitized patients with OAS to kiwi were used in this study. The kiwi allergen was isolated by using a combination of gel permeation, ion exchange, and immobilized metal ion affinity chromatography. Its biochemical characterization included determination of its isoelectric point, molecular weight, N-terminal sequencing, concanavalin A-binding ability, digestibility in simulated gastric fluid, and antifungal activity. Western blotting, 2-dimensional PAGE immunoblotting, and skin prick tests were performed to characterize the isolated protein immunochemically. Results: All 7 patients recognized the isolated 24-kd kiwi protein as an allergen. The isolated protein consisted of 2 isoforms with isoelectric points of 9.4 and 9.5 migrated as one protein band of 20 kd after SDS-PAGE under nonreducing conditions or at 24 kd under reducing conditions. The partial N-terminal sequence revealed that it is a thaumatin-like protein (TLP) with concanavalin A-binding ability. The protein showed antifungal activity toward Saccharomyces carlsbergensis, and Candida albicans. The protein was degraded by the simulated gastric fluid within 1 minute. Both isoforms bound IgE from a pool of sera in a 2-dimensional PAGE inummoblot. The TLP elicited positive skin prick test responses in 4 (80%) of 5 patients with OAS. Conclusion: This study reported isolation and full characterization of a new kiwi allergen, TLP (isoelectric points of 9.4 and 9.5 and molecular weight of 24 kd), which belongs to the family of pathogenesis-related proteins. The isolated protein expressed antifungal activity toward S carlsbergensis and C albicans.
PB  - Mosby-Elsevier, New York
T2  - Journal of Allergy and Clinical Immunology
T1  - Isolation and biochemical characterization of a thaumatin-like kiwi allergen
EP  - 810
IS  - 5
SP  - 805
VL  - 110
DO  - 10.1067/mai.2002.128947
UR  - conv_136
ER  - 
@article{
author = "Gavrović-Jankulović, Marija and Ćirković, Tanja and Vučković, Olga and Atanasković-Marković, Marina and Petersen, Arnd and Gojgić, G. and Burazer, Lidija and Jankov, Ratko",
year = "2002",
abstract = "Background: Kiwi fruit allergy, as well as its association with hypersensitivity to other foods and to pollen, has been extensively reported in the last few years. Several IgE-binding components have been detected in kiwi extract, but only one 30-kd allergen has been isolated; it was identified as actinidin (Act c 1). Recently, we have reported a 24-kd kiwi protein to be a potential major allergen in a group of patients with oral allergy syndrome (OAS). Objective: The aim of this study was to purify and characterize the 24-kd kiwi allergen biochemically. Methods: Seven polysensitized patients with OAS to kiwi were used in this study. The kiwi allergen was isolated by using a combination of gel permeation, ion exchange, and immobilized metal ion affinity chromatography. Its biochemical characterization included determination of its isoelectric point, molecular weight, N-terminal sequencing, concanavalin A-binding ability, digestibility in simulated gastric fluid, and antifungal activity. Western blotting, 2-dimensional PAGE immunoblotting, and skin prick tests were performed to characterize the isolated protein immunochemically. Results: All 7 patients recognized the isolated 24-kd kiwi protein as an allergen. The isolated protein consisted of 2 isoforms with isoelectric points of 9.4 and 9.5 migrated as one protein band of 20 kd after SDS-PAGE under nonreducing conditions or at 24 kd under reducing conditions. The partial N-terminal sequence revealed that it is a thaumatin-like protein (TLP) with concanavalin A-binding ability. The protein showed antifungal activity toward Saccharomyces carlsbergensis, and Candida albicans. The protein was degraded by the simulated gastric fluid within 1 minute. Both isoforms bound IgE from a pool of sera in a 2-dimensional PAGE inummoblot. The TLP elicited positive skin prick test responses in 4 (80%) of 5 patients with OAS. Conclusion: This study reported isolation and full characterization of a new kiwi allergen, TLP (isoelectric points of 9.4 and 9.5 and molecular weight of 24 kd), which belongs to the family of pathogenesis-related proteins. The isolated protein expressed antifungal activity toward S carlsbergensis and C albicans.",
publisher = "Mosby-Elsevier, New York",
journal = "Journal of Allergy and Clinical Immunology",
title = "Isolation and biochemical characterization of a thaumatin-like kiwi allergen",
pages = "810-805",
number = "5",
volume = "110",
doi = "10.1067/mai.2002.128947",
url = "conv_136"
}
Gavrović-Jankulović, M., Ćirković, T., Vučković, O., Atanasković-Marković, M., Petersen, A., Gojgić, G., Burazer, L.,& Jankov, R.. (2002). Isolation and biochemical characterization of a thaumatin-like kiwi allergen. in Journal of Allergy and Clinical Immunology
Mosby-Elsevier, New York., 110(5), 805-810.
https://doi.org/10.1067/mai.2002.128947
conv_136
Gavrović-Jankulović M, Ćirković T, Vučković O, Atanasković-Marković M, Petersen A, Gojgić G, Burazer L, Jankov R. Isolation and biochemical characterization of a thaumatin-like kiwi allergen. in Journal of Allergy and Clinical Immunology. 2002;110(5):805-810.
doi:10.1067/mai.2002.128947
conv_136 .
Gavrović-Jankulović, Marija, Ćirković, Tanja, Vučković, Olga, Atanasković-Marković, Marina, Petersen, Arnd, Gojgić, G., Burazer, Lidija, Jankov, Ratko, "Isolation and biochemical characterization of a thaumatin-like kiwi allergen" in Journal of Allergy and Clinical Immunology, 110, no. 5 (2002):805-810,
https://doi.org/10.1067/mai.2002.128947 .,
conv_136 .
3
99
94
109