TY  - CONF
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Hoffmann-Sommergruber, Karin
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://intor.torlakinstitut.com/handle/123456789/755
AB  - Background: In vitro pepsin digestion is important factor when assessing protein foodallergenicity. Roasted hazelnut is more common in human nutrition than a raw hazelnut;however, all studies were focused on Cor a 9 allergen obtained from a raw hazelnut. Thereare only two studies employing in vitro INFOGEST digestion harmonized protocol onhazelnut with its full matrix. The aim of this study was to assess immunoreactivity of rawand roasted hazelnut gastric digests and to compare secondary/tertiary structure of Cor a 9allergen purified from these two sources.Methods: Digestion resistant protein fragments were analysed by 1D/2D electrophoresis.Following digestion, IgE binding from patients’ pooled sera and by specific antibodies, wereassessed in ELISA and immunoblot. CD spectroscopy was applied for Cor a 9 structuralanalyses.Results: Cor a 11 and acidic forms of Cor a 9 were more prone to pepsin proteolysis, yettheir large fragments survived partially. Cor a 8 was protected by lipids, retaining capabilityto bind its specific antibody. Roasting did not significantly affect secondary structure of themost abundant hazelnut allergen, Cor a 9.Conclusion: Roasting of hazelnut seems to boost IgE binding derived from pooled sera ofhazelnut allergic patients with oral-gastric allergen digests.
PB  - INFOGEST Cost action, INRAE, Teagasc LTD.
C3  - Virtual International Conference on Food Digestion 6th and 7th May, 2021
T1  - Allergome of oral-gastric in vitro digest of roasted hazelnut shows stronger IgE binding compared to the raw counterpart
EP  - 62
SP  - 62
UR  - https://hdl.handle.net/21.15107/rcub_intor_755
ER  - 

@conference{
author = "Prodić, Ivana and Smiljanić, Katarina and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Background: In vitro pepsin digestion is important factor when assessing protein foodallergenicity. Roasted hazelnut is more common in human nutrition than a raw hazelnut;however, all studies were focused on Cor a 9 allergen obtained from a raw hazelnut. Thereare only two studies employing in vitro INFOGEST digestion harmonized protocol onhazelnut with its full matrix. The aim of this study was to assess immunoreactivity of rawand roasted hazelnut gastric digests and to compare secondary/tertiary structure of Cor a 9allergen purified from these two sources.Methods: Digestion resistant protein fragments were analysed by 1D/2D electrophoresis.Following digestion, IgE binding from patients’ pooled sera and by specific antibodies, wereassessed in ELISA and immunoblot. CD spectroscopy was applied for Cor a 9 structuralanalyses.Results: Cor a 11 and acidic forms of Cor a 9 were more prone to pepsin proteolysis, yettheir large fragments survived partially. Cor a 8 was protected by lipids, retaining capabilityto bind its specific antibody. Roasting did not significantly affect secondary structure of themost abundant hazelnut allergen, Cor a 9.Conclusion: Roasting of hazelnut seems to boost IgE binding derived from pooled sera ofhazelnut allergic patients with oral-gastric allergen digests.",
publisher = "INFOGEST Cost action, INRAE, Teagasc LTD.",
journal = "Virtual International Conference on Food Digestion 6th and 7th May, 2021",
title = "Allergome of oral-gastric in vitro digest of roasted hazelnut shows stronger IgE binding compared to the raw counterpart",
pages = "62-62",
url = "https://hdl.handle.net/21.15107/rcub_intor_755"
}

Prodić, I., Smiljanić, K., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2021). Allergome of oral-gastric in vitro digest of roasted hazelnut shows stronger IgE binding compared to the raw counterpart. in Virtual International Conference on Food Digestion 6th and 7th May, 2021
INFOGEST Cost action, INRAE, Teagasc LTD.., 62-62.
https://hdl.handle.net/21.15107/rcub_intor_755

Prodić I, Smiljanić K, Hoffmann-Sommergruber K, Ćirković-Veličković T. Allergome of oral-gastric in vitro digest of roasted hazelnut shows stronger IgE binding compared to the raw counterpart. in Virtual International Conference on Food Digestion 6th and 7th May, 2021. 2021;:62-62.
https://hdl.handle.net/21.15107/rcub_intor_755 .

Prodić, Ivana, Smiljanić, Katarina, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, "Allergome of oral-gastric in vitro digest of roasted hazelnut shows stronger IgE binding compared to the raw counterpart" in Virtual International Conference on Food Digestion 6th and 7th May, 2021 (2021):62-62,
https://hdl.handle.net/21.15107/rcub_intor_755 .

TY  - CONF
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Nagl, Christoph
AU  - Hoffmann-Sommergruber, Karin
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://intor.torlakinstitut.com/handle/123456789/753
AB  - Cor a 8 is a relevant allergen that can cause severe allergic reactions. It is a 115 amino acid protein with a molecular mass of 9 kDa and is a member of the non-specific lipida transfer protein family. This allergen is resistant to high temperatures, pH changes, gastric and intestinal enzymes. The main route of exposure is through ingestion. In order to examine its resistance to digestion, we have applied a popular 1.0 INFOGEST protocol [1], specialized for the complete food, which in vitro mimics physiologically relevant conditions of oral-gastric-intestinal digestion. The aim of this study was to compare Cor a 8 resistance to gastric digestion, from both, raw and roasted hazelnuts, before and upon pepsin (gastric) digestion. Stability of the Cor a 8 protein was investigated by simulation of oral and gastric digestion phases, performed with ground raw and roasted hazelnut kernels. Hazelnut proteins were extracted from the digestion mixture and analyzed by 1D and 2D SDS-PAGE, while raw and roasted Cor a 8 western blots were probed with specific anti-Cor a 8 antibodies in 1D and 2D immunoblots. The electrophoretic patterns of the raw and roasted extracts were similar. 1D SDS PAGE profiles demonstrated high stability of Cor a 8 against enzymatic treatments. Control samples of Cor a 8 from raw and roasted hazelnut extracts migrated as a single band at around 12 kDa in 1D immunoblot. However, in case of roasted hazelnut, the protein showed a slightly lower capacity to bind specific anti-Cor a 8 antibody, as compared to raw hazelnut extract. In 2D immunoblot, with higher resolution, specific antibody binding was decting a significant and noticeable smear in the basic region indicating a range of different protein variants. This was more pronounced detectable in the case of roasted sample upon digestion, pointing to a mix of variants in this allergen batch. It has been suggested that the allergenicity of the Cor a 8 is almost insensitive to temperature. The allergen is stable even after digestion and roasting processes up to 140˚C. We hypothesize that a lipid-rich food matrix delays extraction of proteins, thereby delaying their gastrointestinal digestion, which may affect allergen sensitizing capacity and clinical symptoms.
PB  - Sociedade Portuguesa de Química
C3  - Book of Abstracts of the XXI EuroFoodChem Congress
T1  - Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol
EP  - 126
SP  - 126
UR  - https://hdl.handle.net/21.15107/rcub_intor_753
ER  - 

@conference{
author = "Prodić, Ivana and Smiljanić, Katarina and Nagl, Christoph and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Cor a 8 is a relevant allergen that can cause severe allergic reactions. It is a 115 amino acid protein with a molecular mass of 9 kDa and is a member of the non-specific lipida transfer protein family. This allergen is resistant to high temperatures, pH changes, gastric and intestinal enzymes. The main route of exposure is through ingestion. In order to examine its resistance to digestion, we have applied a popular 1.0 INFOGEST protocol [1], specialized for the complete food, which in vitro mimics physiologically relevant conditions of oral-gastric-intestinal digestion. The aim of this study was to compare Cor a 8 resistance to gastric digestion, from both, raw and roasted hazelnuts, before and upon pepsin (gastric) digestion. Stability of the Cor a 8 protein was investigated by simulation of oral and gastric digestion phases, performed with ground raw and roasted hazelnut kernels. Hazelnut proteins were extracted from the digestion mixture and analyzed by 1D and 2D SDS-PAGE, while raw and roasted Cor a 8 western blots were probed with specific anti-Cor a 8 antibodies in 1D and 2D immunoblots. The electrophoretic patterns of the raw and roasted extracts were similar. 1D SDS PAGE profiles demonstrated high stability of Cor a 8 against enzymatic treatments. Control samples of Cor a 8 from raw and roasted hazelnut extracts migrated as a single band at around 12 kDa in 1D immunoblot. However, in case of roasted hazelnut, the protein showed a slightly lower capacity to bind specific anti-Cor a 8 antibody, as compared to raw hazelnut extract. In 2D immunoblot, with higher resolution, specific antibody binding was decting a significant and noticeable smear in the basic region indicating a range of different protein variants. This was more pronounced detectable in the case of roasted sample upon digestion, pointing to a mix of variants in this allergen batch. It has been suggested that the allergenicity of the Cor a 8 is almost insensitive to temperature. The allergen is stable even after digestion and roasting processes up to 140˚C. We hypothesize that a lipid-rich food matrix delays extraction of proteins, thereby delaying their gastrointestinal digestion, which may affect allergen sensitizing capacity and clinical symptoms.",
publisher = "Sociedade Portuguesa de Química",
journal = "Book of Abstracts of the XXI EuroFoodChem Congress",
title = "Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol",
pages = "126-126",
url = "https://hdl.handle.net/21.15107/rcub_intor_753"
}

Prodić, I., Smiljanić, K., Nagl, C., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2021). Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol. in Book of Abstracts of the XXI EuroFoodChem Congress
Sociedade Portuguesa de Química., 126-126.
https://hdl.handle.net/21.15107/rcub_intor_753

Prodić I, Smiljanić K, Nagl C, Hoffmann-Sommergruber K, Ćirković-Veličković T. Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol. in Book of Abstracts of the XXI EuroFoodChem Congress. 2021;:126-126.
https://hdl.handle.net/21.15107/rcub_intor_753 .

Prodić, Ivana, Smiljanić, Katarina, Nagl, Christoph, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, "Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol" in Book of Abstracts of the XXI EuroFoodChem Congress (2021):126-126,
https://hdl.handle.net/21.15107/rcub_intor_753 .

TY  - CONF
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Mihailović, Jelena
AU  - Hoffmann-Sommergruber, Karin
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://intor.torlakinstitut.com/handle/123456789/775
AB  - Brief introduction: Stability to gastric digestion represents a very important parameter of food protein allergenicity. Usually digestion experiments are carried out on purified proteins or protein extracts; however, use of solid food is far closer to the in vivo situation, taking into account food protein interactions with other food components, such as polyphenols and lipids.Objective: The aim of this study was to investigate and compare digestion stability and allergenicity of large and small peptides released after pepsin digestion of whole raw and roasted hazelnut kernels under standardized and physiologically relevant in vitro conditions.Methodology: In vitro simulated oral and gastric phase digestion was carried out with ground raw and roasted hazelnut kernels. Digested proteins were extracted from the mixture and analyzed by SDS-PAGE, 2D-PAGE, and compared with Image Master 2D Platinum 7.0. Western blot probed with allergic patients’ sera and specific antibodies for Cor a 8.Main findings: Several important hazelnut seed storage digestion resistant proteins and peptides have been identified and characterized. Most abundant hazelnut allergens were resolved on a 2DE map, for instance acidic and basic chains of Cor a 9, and Cor a11. Digestion-resistant peptides of Cor a 11 and Cor a 9 were able to bind IgE. Lipid transfer protein (Cor a 8) was highly resistant to gastric proteolysis. Conclusion: To conclude, roasted hazelnut is more prone to gastric digestion than raw, and cause milder IgE response in patients. Gastric phase digestion of raw and roasted hazelnut kernels results in partial extraction and digestion of Cor a 11 and Cor a 9 into digestion- resistant peptides with preserved IgE-binding epitopes. These results demonstrate substantial resistance of raw and roasted hazelnut allergens to gastric digestion since they remained mostly intact after 2 h of gastric (pepsin) digestion and retained their allergenicity.
PB  - Univerzitet u Beogradu - Hemijski fakultet
C3  - Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019
T1  - Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products
EP  - 25
SP  - 25
UR  - https://hdl.handle.net/21.15107/rcub_intor_775
ER  - 

@conference{
author = "Prodić, Ivana and Smiljanić, Katarina and Mihailović, Jelena and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "Brief introduction: Stability to gastric digestion represents a very important parameter of food protein allergenicity. Usually digestion experiments are carried out on purified proteins or protein extracts; however, use of solid food is far closer to the in vivo situation, taking into account food protein interactions with other food components, such as polyphenols and lipids.Objective: The aim of this study was to investigate and compare digestion stability and allergenicity of large and small peptides released after pepsin digestion of whole raw and roasted hazelnut kernels under standardized and physiologically relevant in vitro conditions.Methodology: In vitro simulated oral and gastric phase digestion was carried out with ground raw and roasted hazelnut kernels. Digested proteins were extracted from the mixture and analyzed by SDS-PAGE, 2D-PAGE, and compared with Image Master 2D Platinum 7.0. Western blot probed with allergic patients’ sera and specific antibodies for Cor a 8.Main findings: Several important hazelnut seed storage digestion resistant proteins and peptides have been identified and characterized. Most abundant hazelnut allergens were resolved on a 2DE map, for instance acidic and basic chains of Cor a 9, and Cor a11. Digestion-resistant peptides of Cor a 11 and Cor a 9 were able to bind IgE. Lipid transfer protein (Cor a 8) was highly resistant to gastric proteolysis. Conclusion: To conclude, roasted hazelnut is more prone to gastric digestion than raw, and cause milder IgE response in patients. Gastric phase digestion of raw and roasted hazelnut kernels results in partial extraction and digestion of Cor a 11 and Cor a 9 into digestion- resistant peptides with preserved IgE-binding epitopes. These results demonstrate substantial resistance of raw and roasted hazelnut allergens to gastric digestion since they remained mostly intact after 2 h of gastric (pepsin) digestion and retained their allergenicity.",
publisher = "Univerzitet u Beogradu - Hemijski fakultet",
journal = "Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019",
title = "Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products",
pages = "25-25",
url = "https://hdl.handle.net/21.15107/rcub_intor_775"
}

Prodić, I., Smiljanić, K., Mihailović, J., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2019). Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products. in Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019
Univerzitet u Beogradu - Hemijski fakultet., 25-25.
https://hdl.handle.net/21.15107/rcub_intor_775

Prodić I, Smiljanić K, Mihailović J, Hoffmann-Sommergruber K, Ćirković-Veličković T. Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products. in Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019. 2019;:25-25.
https://hdl.handle.net/21.15107/rcub_intor_775 .

Prodić, Ivana, Smiljanić, Katarina, Mihailović, Jelena, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, "Digestomics of raw and roasted hazelnut according to Infogest protocol and characterization of gastric-phase products" in Abstract Book of the 1st FoodEnTwin Workshop “Food and Environmental -Omics”, Belgrade, June 20-21, 2019 (2019):25-25,
https://hdl.handle.net/21.15107/rcub_intor_775 .

TY  - CONF
AU  - Prodić, Ivana
AU  - Dubiela, Pawel
AU  - Mihailović, Jelena
AU  - Stanić-Vučinić, Dragana
AU  - Smiljanić, Katarina
AU  - Hoffmann-Sommergruber, Karin
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://intor.torlakinstitut.com/handle/123456789/776
AB  - Background: Sensitization to non-specific lipid transfer protein (ns-LTPs) in plant foods is regarded as a risk factor for generalized allergic reactions. Stability to gastric digestion represents very important parameter of food proteins allergenicity. Usually studies of digestion were carried out on purified proteins, but has never been examined the influence of different food matrices on different allergens. Allergens from the nsLTP family are known to share a characteristic structure which is highly resistant to proteolysis, and therefore, IgE cross-reactivity of nsLTPs needs to be investigated in the environment such as complex food matrix.Objective: The aim of this research project is to reveal how proteins are digested (by Minekus protocol) within the natural food matrix and possible consequences on their allergenicity, with the special focus on ns-LTP.Methods: Pure nsLTPs from walnut were labelled with Alexa 633 and added to whole grain of grounded raw walnuts, incubated with human α-amylase, and pepsin, therefore mimicking the effects of oral and gastric digestion, in total duration of 2h. Proteins extracted from the mixture were analyzed by one-dimensional (1D) and two-dimensional SDS-PAGe, and respective 1D and 2D immunoblots.Results: Most proteins from pepsin digested walnut sample were more resistant to digestion according to 1D SDS PAGE. Pepsin digested raw walnut sample with nsLTP were assessed by 2D PAGE to compare profiles of the digested and control sample (no pepsin added). 2D SDSPAGE of digested and control walnut samples showed almost identical profiles, especially in the context of fluorescently labelled nsLTP allergens. These results demonstrate substantial resistance of nsLTP allergens to gastric digestion since they remained mostly intact after 2 h of gastric (pepsin) digestion.Conclusion: Further research is needed to be able to grade stability/resistance of selected food allergens to gastric digestion as a consequence of food matrix modulating effects. We propose that certain combinations of foods and allergens could provide additional protection or on the contrary ease the digestion, by comparing trends between control and digested samples and between different digested combinations as well.
PB  - IMPARAS Cost Action FA1402
C3  - Proceedings of the 4th International ImpARAS Conference, Portici (Naples), Italy, June 19-21, 2018
T1  - Digestomics of walnut and its nsLTPs allergens reveals their ultimate resistance to gastric digestion
EP  - 59
SP  - 59
UR  - https://hdl.handle.net/21.15107/rcub_intor_776
ER  - 

@conference{
author = "Prodić, Ivana and Dubiela, Pawel and Mihailović, Jelena and Stanić-Vučinić, Dragana and Smiljanić, Katarina and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "Background: Sensitization to non-specific lipid transfer protein (ns-LTPs) in plant foods is regarded as a risk factor for generalized allergic reactions. Stability to gastric digestion represents very important parameter of food proteins allergenicity. Usually studies of digestion were carried out on purified proteins, but has never been examined the influence of different food matrices on different allergens. Allergens from the nsLTP family are known to share a characteristic structure which is highly resistant to proteolysis, and therefore, IgE cross-reactivity of nsLTPs needs to be investigated in the environment such as complex food matrix.Objective: The aim of this research project is to reveal how proteins are digested (by Minekus protocol) within the natural food matrix and possible consequences on their allergenicity, with the special focus on ns-LTP.Methods: Pure nsLTPs from walnut were labelled with Alexa 633 and added to whole grain of grounded raw walnuts, incubated with human α-amylase, and pepsin, therefore mimicking the effects of oral and gastric digestion, in total duration of 2h. Proteins extracted from the mixture were analyzed by one-dimensional (1D) and two-dimensional SDS-PAGe, and respective 1D and 2D immunoblots.Results: Most proteins from pepsin digested walnut sample were more resistant to digestion according to 1D SDS PAGE. Pepsin digested raw walnut sample with nsLTP were assessed by 2D PAGE to compare profiles of the digested and control sample (no pepsin added). 2D SDSPAGE of digested and control walnut samples showed almost identical profiles, especially in the context of fluorescently labelled nsLTP allergens. These results demonstrate substantial resistance of nsLTP allergens to gastric digestion since they remained mostly intact after 2 h of gastric (pepsin) digestion.Conclusion: Further research is needed to be able to grade stability/resistance of selected food allergens to gastric digestion as a consequence of food matrix modulating effects. We propose that certain combinations of foods and allergens could provide additional protection or on the contrary ease the digestion, by comparing trends between control and digested samples and between different digested combinations as well.",
publisher = "IMPARAS Cost Action FA1402",
journal = "Proceedings of the 4th International ImpARAS Conference, Portici (Naples), Italy, June 19-21, 2018",
title = "Digestomics of walnut and its nsLTPs allergens reveals their ultimate resistance to gastric digestion",
pages = "59-59",
url = "https://hdl.handle.net/21.15107/rcub_intor_776"
}

Prodić, I., Dubiela, P., Mihailović, J., Stanić-Vučinić, D., Smiljanić, K., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2018). Digestomics of walnut and its nsLTPs allergens reveals their ultimate resistance to gastric digestion. in Proceedings of the 4th International ImpARAS Conference, Portici (Naples), Italy, June 19-21, 2018
IMPARAS Cost Action FA1402., 59-59.
https://hdl.handle.net/21.15107/rcub_intor_776

Prodić I, Dubiela P, Mihailović J, Stanić-Vučinić D, Smiljanić K, Hoffmann-Sommergruber K, Ćirković-Veličković T. Digestomics of walnut and its nsLTPs allergens reveals their ultimate resistance to gastric digestion. in Proceedings of the 4th International ImpARAS Conference, Portici (Naples), Italy, June 19-21, 2018. 2018;:59-59.
https://hdl.handle.net/21.15107/rcub_intor_776 .

Prodić, Ivana, Dubiela, Pawel, Mihailović, Jelena, Stanić-Vučinić, Dragana, Smiljanić, Katarina, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, "Digestomics of walnut and its nsLTPs allergens reveals their ultimate resistance to gastric digestion" in Proceedings of the 4th International ImpARAS Conference, Portici (Naples), Italy, June 19-21, 2018 (2018):59-59,
https://hdl.handle.net/21.15107/rcub_intor_776 .

TY  - JOUR
AU  - Popović, Milica
AU  - Milovanović, Mina
AU  - Burazer, Lidija
AU  - Vučković, Olga
AU  - Hoffmann-Sommergruber, Karin
AU  - Knulst, Andre C.
AU  - Lindner, Buko
AU  - Petersen, Arnd
AU  - Jankov, Ratko
AU  - Gavrović-Jankulović, Marija
PY  - 2010
UR  - http://intor.torlakinstitut.com/handle/123456789/305
AB  - Kiwifruit has become a frequent cause of fruit allergy in the recent years. The molecular basis of type I hypersensitivity to kiwifruit is attributed to 11 IUIS allergens, with Act d 1, Act d 2 and Act d 5 characterized in extenso. Evaluation of the allergenic properties of Act d 4, a cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa) was performed in this study. Identity of the purified glycoprotein was determined by Edman degradation and by mass fingerprint whereby more than 90% of the primary structure of the mature kiwifruit cystatin was confirmed. Using MALDI TOF analysis, molecular masses of 10902.5 and 11055.2 Da were detected for Act d 4, respectively. Positive skin prick reactivity with Act d 4 was induced in three kiwifruit allergic patients, as well as the upregulation of CD63 and CD203c molecules in the basophile activation assay. The IgE reactivity was detected in dot blot analysis while Western blot analysis was negative using sera from six kiwifruit patients, suggesting the presence of conformational IgE epitopes on the Act d 4 molecule. As activator of effector cells in type I hypersensitivity Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy.
PB  - Wiley, Hoboken
T2  - Molecular Nutrition and Food Research
T1  - Cysteine proteinase inhibitor Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy
EP  - 380
IS  - 3
SP  - 373
VL  - 54
DO  - 10.1002/mnfr.200900035
ER  - 

@article{
author = "Popović, Milica and Milovanović, Mina and Burazer, Lidija and Vučković, Olga and Hoffmann-Sommergruber, Karin and Knulst, Andre C. and Lindner, Buko and Petersen, Arnd and Jankov, Ratko and Gavrović-Jankulović, Marija",
year = "2010",
abstract = "Kiwifruit has become a frequent cause of fruit allergy in the recent years. The molecular basis of type I hypersensitivity to kiwifruit is attributed to 11 IUIS allergens, with Act d 1, Act d 2 and Act d 5 characterized in extenso. Evaluation of the allergenic properties of Act d 4, a cysteine proteinase inhibitor from green kiwifruit (Actinidia deliciosa) was performed in this study. Identity of the purified glycoprotein was determined by Edman degradation and by mass fingerprint whereby more than 90% of the primary structure of the mature kiwifruit cystatin was confirmed. Using MALDI TOF analysis, molecular masses of 10902.5 and 11055.2 Da were detected for Act d 4, respectively. Positive skin prick reactivity with Act d 4 was induced in three kiwifruit allergic patients, as well as the upregulation of CD63 and CD203c molecules in the basophile activation assay. The IgE reactivity was detected in dot blot analysis while Western blot analysis was negative using sera from six kiwifruit patients, suggesting the presence of conformational IgE epitopes on the Act d 4 molecule. As activator of effector cells in type I hypersensitivity Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy.",
publisher = "Wiley, Hoboken",
journal = "Molecular Nutrition and Food Research",
title = "Cysteine proteinase inhibitor Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy",
pages = "380-373",
number = "3",
volume = "54",
doi = "10.1002/mnfr.200900035"
}

Popović, M., Milovanović, M., Burazer, L., Vučković, O., Hoffmann-Sommergruber, K., Knulst, A. C., Lindner, B., Petersen, A., Jankov, R.,& Gavrović-Jankulović, M.. (2010). Cysteine proteinase inhibitor Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy. in Molecular Nutrition and Food Research
Wiley, Hoboken., 54(3), 373-380.
https://doi.org/10.1002/mnfr.200900035

Popović M, Milovanović M, Burazer L, Vučković O, Hoffmann-Sommergruber K, Knulst AC, Lindner B, Petersen A, Jankov R, Gavrović-Jankulović M. Cysteine proteinase inhibitor Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy. in Molecular Nutrition and Food Research. 2010;54(3):373-380.
doi:10.1002/mnfr.200900035 .

Popović, Milica, Milovanović, Mina, Burazer, Lidija, Vučković, Olga, Hoffmann-Sommergruber, Karin, Knulst, Andre C., Lindner, Buko, Petersen, Arnd, Jankov, Ratko, Gavrović-Jankulović, Marija, "Cysteine proteinase inhibitor Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy" in Molecular Nutrition and Food Research, 54, no. 3 (2010):373-380,
https://doi.org/10.1002/mnfr.200900035 . .

TY  - CONF
AU  - Popović, Milica
AU  - Milovanović, Mina
AU  - Burazer, Lidija
AU  - Vučković, Olga
AU  - Knulst, Andre C.
AU  - Hoffmann-Sommergruber, Karin
AU  - Lindner, Buko
AU  - Petersen, Arnd
AU  - Jankov, Ratko
AU  - Gavrović-Jankulović, Marija
PY  - 2009
UR  - http://intor.torlakinstitut.com/handle/123456789/276
PB  - Wiley-Blackwell Publishing, Inc, Malden
C3  - Allergy
T1  - Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy
EP  - 271
SP  - 270
VL  - 64
UR  - https://hdl.handle.net/21.15107/rcub_intor_276
ER  - 

@conference{
author = "Popović, Milica and Milovanović, Mina and Burazer, Lidija and Vučković, Olga and Knulst, Andre C. and Hoffmann-Sommergruber, Karin and Lindner, Buko and Petersen, Arnd and Jankov, Ratko and Gavrović-Jankulović, Marija",
year = "2009",
publisher = "Wiley-Blackwell Publishing, Inc, Malden",
journal = "Allergy",
title = "Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy",
pages = "271-270",
volume = "64",
url = "https://hdl.handle.net/21.15107/rcub_intor_276"
}

Popović, M., Milovanović, M., Burazer, L., Vučković, O., Knulst, A. C., Hoffmann-Sommergruber, K., Lindner, B., Petersen, A., Jankov, R.,& Gavrović-Jankulović, M.. (2009). Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy. in Allergy
Wiley-Blackwell Publishing, Inc, Malden., 64, 270-271.
https://hdl.handle.net/21.15107/rcub_intor_276

Popović M, Milovanović M, Burazer L, Vučković O, Knulst AC, Hoffmann-Sommergruber K, Lindner B, Petersen A, Jankov R, Gavrović-Jankulović M. Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy. in Allergy. 2009;64:270-271.
https://hdl.handle.net/21.15107/rcub_intor_276 .

Popović, Milica, Milovanović, Mina, Burazer, Lidija, Vučković, Olga, Knulst, Andre C., Hoffmann-Sommergruber, Karin, Lindner, Buko, Petersen, Arnd, Jankov, Ratko, Gavrović-Jankulović, Marija, "Act d 4 is a functional allergen contributing to the clinical symptoms of kiwifruit allergy" in Allergy, 64 (2009):270-271,
https://hdl.handle.net/21.15107/rcub_intor_276 .