TY  - DATA
AU  - Costa, Joana
AU  - Bavaro, Simona Lucia
AU  - Benedé, Sara
AU  - Diaz-Perales, Araceli
AU  - Bueno-Diaz, Cristina
AU  - Gelencser, Eva
AU  - Klueber, Julia
AU  - Larré, Colette
AU  - Lozano-Ojalvo, Daniel
AU  - Lupi, Roberta
AU  - Mafra, Isabel
AU  - Mazzucchelli, Gabriel
AU  - Molina, Elena
AU  - Monaci, Linda
AU  - Martín-Pedraza, Laura
AU  - Piras, Cristian
AU  - Rodrigues, Pedro M.
AU  - Roncada, Paola
AU  - Schrama, Denise
AU  - Ćirković-Veličković, Tanja
AU  - Verhoeckx, Kitty
AU  - Villa, Caterina
AU  - Kuehn, Annette
AU  - Hoffmann-Sommergruber, Karin
AU  - Holzhauser, Thomas
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4982
PB  - Springer
T2  - Clinical Reviews in Allergy & Immunology
T1  - Supplementary data for the article: Costa, J.; Bavaro, S. L.; Benedé, S.; Diaz-Perales, A.; Bueno-Diaz, C.; Gelencser, E.; Klueber, J.; Larré, C.; Lozano-Ojalvo, D.; Lupi, R.; Mafra, I.; Mazzucchelli, G.; Molina, E.; Monaci, L.; Martín-Pedraza, L.; Piras, C.; Rodrigues, P. M.; Roncada, P.; Schrama, D.; Cirkovic-Velickovic, T.; Verhoeckx, K.; Villa, C.; Kuehn, A.; Hoffmann-Sommergruber, K.; Holzhauser, T. Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens? Clinic Rev Allerg Immunol 2022, 62 (1), 37–63. https://doi.org/10.1007/s12016-020-08810-9.
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4982
ER  - 

@misc{
author = "Costa, Joana and Bavaro, Simona Lucia and Benedé, Sara and Diaz-Perales, Araceli and Bueno-Diaz, Cristina and Gelencser, Eva and Klueber, Julia and Larré, Colette and Lozano-Ojalvo, Daniel and Lupi, Roberta and Mafra, Isabel and Mazzucchelli, Gabriel and Molina, Elena and Monaci, Linda and Martín-Pedraza, Laura and Piras, Cristian and Rodrigues, Pedro M. and Roncada, Paola and Schrama, Denise and Ćirković-Veličković, Tanja and Verhoeckx, Kitty and Villa, Caterina and Kuehn, Annette and Hoffmann-Sommergruber, Karin and Holzhauser, Thomas",
year = "2022",
publisher = "Springer",
journal = "Clinical Reviews in Allergy & Immunology",
title = "Supplementary data for the article: Costa, J.; Bavaro, S. L.; Benedé, S.; Diaz-Perales, A.; Bueno-Diaz, C.; Gelencser, E.; Klueber, J.; Larré, C.; Lozano-Ojalvo, D.; Lupi, R.; Mafra, I.; Mazzucchelli, G.; Molina, E.; Monaci, L.; Martín-Pedraza, L.; Piras, C.; Rodrigues, P. M.; Roncada, P.; Schrama, D.; Cirkovic-Velickovic, T.; Verhoeckx, K.; Villa, C.; Kuehn, A.; Hoffmann-Sommergruber, K.; Holzhauser, T. Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens? Clinic Rev Allerg Immunol 2022, 62 (1), 37–63. https://doi.org/10.1007/s12016-020-08810-9.",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4982"
}

Costa, J., Bavaro, S. L., Benedé, S., Diaz-Perales, A., Bueno-Diaz, C., Gelencser, E., Klueber, J., Larré, C., Lozano-Ojalvo, D., Lupi, R., Mafra, I., Mazzucchelli, G., Molina, E., Monaci, L., Martín-Pedraza, L., Piras, C., Rodrigues, P. M., Roncada, P., Schrama, D., Ćirković-Veličković, T., Verhoeckx, K., Villa, C., Kuehn, A., Hoffmann-Sommergruber, K.,& Holzhauser, T.. (2022). Supplementary data for the article: Costa, J.; Bavaro, S. L.; Benedé, S.; Diaz-Perales, A.; Bueno-Diaz, C.; Gelencser, E.; Klueber, J.; Larré, C.; Lozano-Ojalvo, D.; Lupi, R.; Mafra, I.; Mazzucchelli, G.; Molina, E.; Monaci, L.; Martín-Pedraza, L.; Piras, C.; Rodrigues, P. M.; Roncada, P.; Schrama, D.; Cirkovic-Velickovic, T.; Verhoeckx, K.; Villa, C.; Kuehn, A.; Hoffmann-Sommergruber, K.; Holzhauser, T. Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens? Clinic Rev Allerg Immunol 2022, 62 (1), 37–63. https://doi.org/10.1007/s12016-020-08810-9.. in Clinical Reviews in Allergy & Immunology
Springer..
https://hdl.handle.net/21.15107/rcub_cherry_4982

Costa J, Bavaro SL, Benedé S, Diaz-Perales A, Bueno-Diaz C, Gelencser E, Klueber J, Larré C, Lozano-Ojalvo D, Lupi R, Mafra I, Mazzucchelli G, Molina E, Monaci L, Martín-Pedraza L, Piras C, Rodrigues PM, Roncada P, Schrama D, Ćirković-Veličković T, Verhoeckx K, Villa C, Kuehn A, Hoffmann-Sommergruber K, Holzhauser T. Supplementary data for the article: Costa, J.; Bavaro, S. L.; Benedé, S.; Diaz-Perales, A.; Bueno-Diaz, C.; Gelencser, E.; Klueber, J.; Larré, C.; Lozano-Ojalvo, D.; Lupi, R.; Mafra, I.; Mazzucchelli, G.; Molina, E.; Monaci, L.; Martín-Pedraza, L.; Piras, C.; Rodrigues, P. M.; Roncada, P.; Schrama, D.; Cirkovic-Velickovic, T.; Verhoeckx, K.; Villa, C.; Kuehn, A.; Hoffmann-Sommergruber, K.; Holzhauser, T. Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens? Clinic Rev Allerg Immunol 2022, 62 (1), 37–63. https://doi.org/10.1007/s12016-020-08810-9.. in Clinical Reviews in Allergy & Immunology. 2022;.
https://hdl.handle.net/21.15107/rcub_cherry_4982 .

Costa, Joana, Bavaro, Simona Lucia, Benedé, Sara, Diaz-Perales, Araceli, Bueno-Diaz, Cristina, Gelencser, Eva, Klueber, Julia, Larré, Colette, Lozano-Ojalvo, Daniel, Lupi, Roberta, Mafra, Isabel, Mazzucchelli, Gabriel, Molina, Elena, Monaci, Linda, Martín-Pedraza, Laura, Piras, Cristian, Rodrigues, Pedro M., Roncada, Paola, Schrama, Denise, Ćirković-Veličković, Tanja, Verhoeckx, Kitty, Villa, Caterina, Kuehn, Annette, Hoffmann-Sommergruber, Karin, Holzhauser, Thomas, "Supplementary data for the article: Costa, J.; Bavaro, S. L.; Benedé, S.; Diaz-Perales, A.; Bueno-Diaz, C.; Gelencser, E.; Klueber, J.; Larré, C.; Lozano-Ojalvo, D.; Lupi, R.; Mafra, I.; Mazzucchelli, G.; Molina, E.; Monaci, L.; Martín-Pedraza, L.; Piras, C.; Rodrigues, P. M.; Roncada, P.; Schrama, D.; Cirkovic-Velickovic, T.; Verhoeckx, K.; Villa, C.; Kuehn, A.; Hoffmann-Sommergruber, K.; Holzhauser, T. Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens? Clinic Rev Allerg Immunol 2022, 62 (1), 37–63. https://doi.org/10.1007/s12016-020-08810-9." in Clinical Reviews in Allergy & Immunology (2022),
https://hdl.handle.net/21.15107/rcub_cherry_4982 .

TY  - JOUR
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Nagl, Christoph
AU  - Ballmer-Weber, Barbara
AU  - Hoffmann-Sommergruber, Karin
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5653
AB  - Most of the food allergens sensitized via the gastrointestinal tract resist thermal treatments and digestion, particularly digestion by pepsin. Roasted hazelnuts are more commonly consumed than raw ones. Since no studies have characterized gastric digestion protein fragments of raw and roasted hazelnuts nor their IgE binding properties, we compared these aspects of raw and roasted hazelnuts’ gastric digesta obtained by INFOGEST protocol. Their electrophoretically resolved profiles were probed with hazelnut allergic patients’ sera in 1D and 2D immunoblots. Electrophoretic profiles demonstrated pepsin digestion of all hazelnut allergens to varying extents. While 2D immunoblots indicated that roasting slightly reduced allergenicity, IgE ELISA with the pool of sera showed a slight significant (10%) increase in IgE binding in both gastric digesta. Cor a 9 isolated from the raw and roasted hazelnuts, characterized by far and near CD, remained stable after roasting, with preserved IgE reactivity. Its immunoreactivity contribution by inhibitory ELISA was noticeable in raw and roasted hazelnut digesta; its activity was slightly stronger in the roasted preparations. Roasting has a visible impact on proteins; however, it did not affect overall IgE reactivity. Gastric digestion slightly increases the overall IgE reactivity in raw and roasted hazelnuts, and may therefore impact the profiles of allergens and their fragments available to interact with the immune system in the small intestine. © 2022 by the authors.
PB  - MDPI
T2  - Foods
T1  - INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity
VL  - 11
SP  - 2914
DO  - 10.3390/foods11182914
ER  - 

@article{
author = "Prodić, Ivana and Smiljanić, Katarina and Nagl, Christoph and Ballmer-Weber, Barbara and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Most of the food allergens sensitized via the gastrointestinal tract resist thermal treatments and digestion, particularly digestion by pepsin. Roasted hazelnuts are more commonly consumed than raw ones. Since no studies have characterized gastric digestion protein fragments of raw and roasted hazelnuts nor their IgE binding properties, we compared these aspects of raw and roasted hazelnuts’ gastric digesta obtained by INFOGEST protocol. Their electrophoretically resolved profiles were probed with hazelnut allergic patients’ sera in 1D and 2D immunoblots. Electrophoretic profiles demonstrated pepsin digestion of all hazelnut allergens to varying extents. While 2D immunoblots indicated that roasting slightly reduced allergenicity, IgE ELISA with the pool of sera showed a slight significant (10%) increase in IgE binding in both gastric digesta. Cor a 9 isolated from the raw and roasted hazelnuts, characterized by far and near CD, remained stable after roasting, with preserved IgE reactivity. Its immunoreactivity contribution by inhibitory ELISA was noticeable in raw and roasted hazelnut digesta; its activity was slightly stronger in the roasted preparations. Roasting has a visible impact on proteins; however, it did not affect overall IgE reactivity. Gastric digestion slightly increases the overall IgE reactivity in raw and roasted hazelnuts, and may therefore impact the profiles of allergens and their fragments available to interact with the immune system in the small intestine. © 2022 by the authors.",
publisher = "MDPI",
journal = "Foods",
title = "INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity",
volume = "11",
pages = "2914",
doi = "10.3390/foods11182914"
}

Prodić, I., Smiljanić, K., Nagl, C., Ballmer-Weber, B., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2022). INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity. in Foods
MDPI., 11, 2914.
https://doi.org/10.3390/foods11182914

Prodić I, Smiljanić K, Nagl C, Ballmer-Weber B, Hoffmann-Sommergruber K, Ćirković-Veličković T. INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity. in Foods. 2022;11:2914.
doi:10.3390/foods11182914 .

Prodić, Ivana, Smiljanić, Katarina, Nagl, Christoph, Ballmer-Weber, Barbara, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, "INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity" in Foods, 11 (2022):2914,
https://doi.org/10.3390/foods11182914 . .

TY  - DATA
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Nagl, Christoph
AU  - Ballmer-Weber, Barbara
AU  - Hoffmann-Sommergruber, Karin
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - https://doi.org/10.3390/foods11182914
AB  - Most of the food allergens sensitized via the gastrointestinal tract resist thermal treatments and digestion, particularly digestion by pepsin. Roasted hazelnuts are more commonly consumed than raw ones. Since no studies have characterized gastric digestion protein fragments of raw and roasted hazelnuts nor their IgE binding properties, we compared these aspects of raw and roasted hazelnuts’ gastric digesta obtained by INFOGEST protocol. Their electrophoretically resolved profiles were probed with hazelnut allergic patients’ sera in 1D and 2D immunoblots. Electrophoretic profiles demonstrated pepsin digestion of all hazelnut allergens to varying extents. While 2D immunoblots indicated that roasting slightly reduced allergenicity, IgE ELISA with the pool of sera showed a slight significant (10%) increase in IgE binding in both gastric digesta. Cor a 9 isolated from the raw and roasted hazelnuts, characterized by far and near CD, remained stable after roasting, with preserved IgE reactivity. Its immunoreactivity contribution by inhibitory ELISA was noticeable in raw and roasted hazelnut digesta; its activity was slightly stronger in the roasted preparations. Roasting has a visible impact on proteins; however, it did not affect overall IgE reactivity. Gastric digestion slightly increases the overall IgE reactivity in raw and roasted hazelnuts, and may therefore impact the profiles of allergens and their fragments available to interact with the immune system in the small intestine. © 2022 by the authors.
PB  - MDPI
T2  - Foods
T1  - Supplementary material for:Prodić, I., Smiljanić, K., Nagl, C., Ballmer-Weber, B., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2022). INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity. in Foods MDPI., 11, 2914. https://doi.org/10.3390/foods11182914
VL  - 11
SP  - 2914
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5657
ER  - 

@misc{
author = "Prodić, Ivana and Smiljanić, Katarina and Nagl, Christoph and Ballmer-Weber, Barbara and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Most of the food allergens sensitized via the gastrointestinal tract resist thermal treatments and digestion, particularly digestion by pepsin. Roasted hazelnuts are more commonly consumed than raw ones. Since no studies have characterized gastric digestion protein fragments of raw and roasted hazelnuts nor their IgE binding properties, we compared these aspects of raw and roasted hazelnuts’ gastric digesta obtained by INFOGEST protocol. Their electrophoretically resolved profiles were probed with hazelnut allergic patients’ sera in 1D and 2D immunoblots. Electrophoretic profiles demonstrated pepsin digestion of all hazelnut allergens to varying extents. While 2D immunoblots indicated that roasting slightly reduced allergenicity, IgE ELISA with the pool of sera showed a slight significant (10%) increase in IgE binding in both gastric digesta. Cor a 9 isolated from the raw and roasted hazelnuts, characterized by far and near CD, remained stable after roasting, with preserved IgE reactivity. Its immunoreactivity contribution by inhibitory ELISA was noticeable in raw and roasted hazelnut digesta; its activity was slightly stronger in the roasted preparations. Roasting has a visible impact on proteins; however, it did not affect overall IgE reactivity. Gastric digestion slightly increases the overall IgE reactivity in raw and roasted hazelnuts, and may therefore impact the profiles of allergens and their fragments available to interact with the immune system in the small intestine. © 2022 by the authors.",
publisher = "MDPI",
journal = "Foods",
title = "Supplementary material for:Prodić, I., Smiljanić, K., Nagl, C., Ballmer-Weber, B., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2022). INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity. in Foods MDPI., 11, 2914. https://doi.org/10.3390/foods11182914",
volume = "11",
pages = "2914",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5657"
}

Prodić, I., Smiljanić, K., Nagl, C., Ballmer-Weber, B., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2022). Supplementary material for:Prodić, I., Smiljanić, K., Nagl, C., Ballmer-Weber, B., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2022). INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity. in Foods MDPI., 11, 2914. https://doi.org/10.3390/foods11182914. in Foods
MDPI., 11, 2914.
https://hdl.handle.net/21.15107/rcub_cherry_5657

Prodić I, Smiljanić K, Nagl C, Ballmer-Weber B, Hoffmann-Sommergruber K, Ćirković-Veličković T. Supplementary material for:Prodić, I., Smiljanić, K., Nagl, C., Ballmer-Weber, B., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2022). INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity. in Foods MDPI., 11, 2914. https://doi.org/10.3390/foods11182914. in Foods. 2022;11:2914.
https://hdl.handle.net/21.15107/rcub_cherry_5657 .

Prodić, Ivana, Smiljanić, Katarina, Nagl, Christoph, Ballmer-Weber, Barbara, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, "Supplementary material for:Prodić, I., Smiljanić, K., Nagl, C., Ballmer-Weber, B., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2022). INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity. in Foods MDPI., 11, 2914. https://doi.org/10.3390/foods11182914" in Foods, 11 (2022):2914,
https://hdl.handle.net/21.15107/rcub_cherry_5657 .

TY  - JOUR
AU  - Costa, Joana
AU  - Bavaro, Simona Lucia
AU  - Benedé, Sara
AU  - Diaz-Perales, Araceli
AU  - Bueno-Diaz, Cristina
AU  - Gelencser, Eva
AU  - Klueber, Julia
AU  - Larré, Colette
AU  - Lozano-Ojalvo, Daniel
AU  - Lupi, Roberta
AU  - Mafra, Isabel
AU  - Mazzucchelli, Gabriel
AU  - Molina, Elena
AU  - Monaci, Linda
AU  - Martín-Pedraza, Laura
AU  - Piras, Cristian
AU  - Rodrigues, Pedro M.
AU  - Roncada, Paola
AU  - Schrama, Denise
AU  - Ćirković-Veličković, Tanja
AU  - Verhoeckx, Kitty
AU  - Villa, Caterina
AU  - Kuehn, Annette
AU  - Hoffmann-Sommergruber, Karin
AU  - Holzhauser, Thomas
PY  - 2022
UR  - https://doi.org/10.1007/s12016-020-08810-9
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4981
AB  - This review searched for published evidence that could explain how different physicochemical properties impact on the allergenicity of food proteins and if their effects would follow specific patterns among distinct protein families. Owing to the amount and complexity of the collected information, this literature overview was divided in two articles, the current one dedicated to protein families of plant allergens and a second one focused on animal allergens. Our extensive analysis of the available literature revealed that physicochemical characteristics had consistent effects on protein allergenicity for allergens belonging to the same protein family. For example, protein aggregation contributes to increased allergenicity of 2S albumins, while for legumins and cereal prolamins, the same phenomenon leads to a reduction. Molecular stability, related to structural resistance to heat and proteolysis, was identified as the most common feature promoting plant protein allergenicity, although it fails to explain the potency of some unstable allergens (e.g. pollen-related food allergens). Furthermore, data on physicochemical characteristics translating into clinical effects are limited, mainly because most studies are focused on in vitro IgE binding. Clinical data assessing how these parameters affect the development and clinical manifestation of allergies is minimal, with only few reports evaluating the sensitising capacity of modified proteins (addressing different physicochemical properties) in murine allergy models. In vivo testing of modified pure proteins by SPT or DBPCFC is scarce. At this stage, a systematic approach to link the physicochemical properties with clinical plant allergenicity in real-life scenarios is still missing.
PB  - Springer
T2  - Clinical Reviews in Allergy & Immunology
T1  - Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?
VL  - 62
IS  - 1
SP  - 37
EP  - 63
DO  - 10.1007/s12016-020-08810-9
ER  - 

@article{
author = "Costa, Joana and Bavaro, Simona Lucia and Benedé, Sara and Diaz-Perales, Araceli and Bueno-Diaz, Cristina and Gelencser, Eva and Klueber, Julia and Larré, Colette and Lozano-Ojalvo, Daniel and Lupi, Roberta and Mafra, Isabel and Mazzucchelli, Gabriel and Molina, Elena and Monaci, Linda and Martín-Pedraza, Laura and Piras, Cristian and Rodrigues, Pedro M. and Roncada, Paola and Schrama, Denise and Ćirković-Veličković, Tanja and Verhoeckx, Kitty and Villa, Caterina and Kuehn, Annette and Hoffmann-Sommergruber, Karin and Holzhauser, Thomas",
year = "2022",
abstract = "This review searched for published evidence that could explain how different physicochemical properties impact on the allergenicity of food proteins and if their effects would follow specific patterns among distinct protein families. Owing to the amount and complexity of the collected information, this literature overview was divided in two articles, the current one dedicated to protein families of plant allergens and a second one focused on animal allergens. Our extensive analysis of the available literature revealed that physicochemical characteristics had consistent effects on protein allergenicity for allergens belonging to the same protein family. For example, protein aggregation contributes to increased allergenicity of 2S albumins, while for legumins and cereal prolamins, the same phenomenon leads to a reduction. Molecular stability, related to structural resistance to heat and proteolysis, was identified as the most common feature promoting plant protein allergenicity, although it fails to explain the potency of some unstable allergens (e.g. pollen-related food allergens). Furthermore, data on physicochemical characteristics translating into clinical effects are limited, mainly because most studies are focused on in vitro IgE binding. Clinical data assessing how these parameters affect the development and clinical manifestation of allergies is minimal, with only few reports evaluating the sensitising capacity of modified proteins (addressing different physicochemical properties) in murine allergy models. In vivo testing of modified pure proteins by SPT or DBPCFC is scarce. At this stage, a systematic approach to link the physicochemical properties with clinical plant allergenicity in real-life scenarios is still missing.",
publisher = "Springer",
journal = "Clinical Reviews in Allergy & Immunology",
title = "Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?",
volume = "62",
number = "1",
pages = "37-63",
doi = "10.1007/s12016-020-08810-9"
}

Costa, J., Bavaro, S. L., Benedé, S., Diaz-Perales, A., Bueno-Diaz, C., Gelencser, E., Klueber, J., Larré, C., Lozano-Ojalvo, D., Lupi, R., Mafra, I., Mazzucchelli, G., Molina, E., Monaci, L., Martín-Pedraza, L., Piras, C., Rodrigues, P. M., Roncada, P., Schrama, D., Ćirković-Veličković, T., Verhoeckx, K., Villa, C., Kuehn, A., Hoffmann-Sommergruber, K.,& Holzhauser, T.. (2022). Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?. in Clinical Reviews in Allergy & Immunology
Springer., 62(1), 37-63.
https://doi.org/10.1007/s12016-020-08810-9

Costa J, Bavaro SL, Benedé S, Diaz-Perales A, Bueno-Diaz C, Gelencser E, Klueber J, Larré C, Lozano-Ojalvo D, Lupi R, Mafra I, Mazzucchelli G, Molina E, Monaci L, Martín-Pedraza L, Piras C, Rodrigues PM, Roncada P, Schrama D, Ćirković-Veličković T, Verhoeckx K, Villa C, Kuehn A, Hoffmann-Sommergruber K, Holzhauser T. Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?. in Clinical Reviews in Allergy & Immunology. 2022;62(1):37-63.
doi:10.1007/s12016-020-08810-9 .

Costa, Joana, Bavaro, Simona Lucia, Benedé, Sara, Diaz-Perales, Araceli, Bueno-Diaz, Cristina, Gelencser, Eva, Klueber, Julia, Larré, Colette, Lozano-Ojalvo, Daniel, Lupi, Roberta, Mafra, Isabel, Mazzucchelli, Gabriel, Molina, Elena, Monaci, Linda, Martín-Pedraza, Laura, Piras, Cristian, Rodrigues, Pedro M., Roncada, Paola, Schrama, Denise, Ćirković-Veličković, Tanja, Verhoeckx, Kitty, Villa, Caterina, Kuehn, Annette, Hoffmann-Sommergruber, Karin, Holzhauser, Thomas, "Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?" in Clinical Reviews in Allergy & Immunology, 62, no. 1 (2022):37-63,
https://doi.org/10.1007/s12016-020-08810-9 . .

TY  - JOUR
AU  - Mazzucchelli, Gabriel
AU  - Holzhauser, Thomas
AU  - Ćirković-Veličković, Tanja
AU  - Diaz-Perales, Araceli
AU  - Molina, Elena
AU  - Roncada, Paola
AU  - Rodrigues, Pedro
AU  - Verhoeckx, Kitty
AU  - Hoffmann-Sommergruber, Karin
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2067
AB  - Food allergies are recognized as a global health concern. In order to protect allergic consumers from severe symptoms, allergenic risk assessment for well-known foods and foods containing genetically modified ingredients is installed. However, population is steadily growing and there is a rising need to provide adequate protein-based foods, including novel sources, not yet used for human consumption. In this context safety issues such as a potential increased allergenic risk need to be assessed before marketing novel food sources. Therefore, the established allergenic risk assessment for genetically modified organisms needs to be re-evaluated for its applicability for risk assessment of novel food proteins. Two different scenarios of allergic sensitization have to be assessed. The first scenario is the presence of already known allergenic structures in novel foods. For this, a comparative assessment can be performed and the range of cross-reactivity can be explored, while in the second scenario allergic reactions are observed toward so far novel allergenic structures and no reference material is available. This review summarizes the current analytical methods for allergenic risk assessment, highlighting the strengths and limitations of each method and discussing the gaps in this assessment that need to be addressed in the near future.
PB  - Wiley, Hoboken
T2  - Molecular Nutrition and Food Research
T1  - Current (Food) Allergenic Risk Assessment: Is It Fit for Novel Foods? Status Quo and Identification of Gaps
VL  - 62
IS  - 1
DO  - 10.1002/mnfr.201700278
ER  - 

@article{
author = "Mazzucchelli, Gabriel and Holzhauser, Thomas and Ćirković-Veličković, Tanja and Diaz-Perales, Araceli and Molina, Elena and Roncada, Paola and Rodrigues, Pedro and Verhoeckx, Kitty and Hoffmann-Sommergruber, Karin",
year = "2018",
abstract = "Food allergies are recognized as a global health concern. In order to protect allergic consumers from severe symptoms, allergenic risk assessment for well-known foods and foods containing genetically modified ingredients is installed. However, population is steadily growing and there is a rising need to provide adequate protein-based foods, including novel sources, not yet used for human consumption. In this context safety issues such as a potential increased allergenic risk need to be assessed before marketing novel food sources. Therefore, the established allergenic risk assessment for genetically modified organisms needs to be re-evaluated for its applicability for risk assessment of novel food proteins. Two different scenarios of allergic sensitization have to be assessed. The first scenario is the presence of already known allergenic structures in novel foods. For this, a comparative assessment can be performed and the range of cross-reactivity can be explored, while in the second scenario allergic reactions are observed toward so far novel allergenic structures and no reference material is available. This review summarizes the current analytical methods for allergenic risk assessment, highlighting the strengths and limitations of each method and discussing the gaps in this assessment that need to be addressed in the near future.",
publisher = "Wiley, Hoboken",
journal = "Molecular Nutrition and Food Research",
title = "Current (Food) Allergenic Risk Assessment: Is It Fit for Novel Foods? Status Quo and Identification of Gaps",
volume = "62",
number = "1",
doi = "10.1002/mnfr.201700278"
}

Mazzucchelli, G., Holzhauser, T., Ćirković-Veličković, T., Diaz-Perales, A., Molina, E., Roncada, P., Rodrigues, P., Verhoeckx, K.,& Hoffmann-Sommergruber, K.. (2018). Current (Food) Allergenic Risk Assessment: Is It Fit for Novel Foods? Status Quo and Identification of Gaps. in Molecular Nutrition and Food Research
Wiley, Hoboken., 62(1).
https://doi.org/10.1002/mnfr.201700278

Mazzucchelli G, Holzhauser T, Ćirković-Veličković T, Diaz-Perales A, Molina E, Roncada P, Rodrigues P, Verhoeckx K, Hoffmann-Sommergruber K. Current (Food) Allergenic Risk Assessment: Is It Fit for Novel Foods? Status Quo and Identification of Gaps. in Molecular Nutrition and Food Research. 2018;62(1).
doi:10.1002/mnfr.201700278 .

Mazzucchelli, Gabriel, Holzhauser, Thomas, Ćirković-Veličković, Tanja, Diaz-Perales, Araceli, Molina, Elena, Roncada, Paola, Rodrigues, Pedro, Verhoeckx, Kitty, Hoffmann-Sommergruber, Karin, "Current (Food) Allergenic Risk Assessment: Is It Fit for Novel Foods? Status Quo and Identification of Gaps" in Molecular Nutrition and Food Research, 62, no. 1 (2018),
https://doi.org/10.1002/mnfr.201700278 . .

TY  - JOUR
AU  - Popović, Milica M.
AU  - Milovanovic, Mina
AU  - Burazer, Lidija M.
AU  - Vučković, Olga
AU  - Hoffmann-Sommergruber, Karin
AU  - Knulst, Andre C.
AU  - Lindner, Buko
AU  - Petersen, Arnd
AU  - Jankov, Ratko M.
AU  - Gavrović-Jankulović, Marija
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1068
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-V C H Verlag Gmbh, Weinheim
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
VL  - 54
IS  - 3
SP  - 373
EP  - 380
DO  - 10.1002/mnfr.200900035
ER  - 

@article{
author = "Popović, Milica M. and Milovanovic, Mina and Burazer, Lidija M. and Vučković, Olga and Hoffmann-Sommergruber, Karin and Knulst, Andre C. and Lindner, Buko and Petersen, Arnd and Jankov, Ratko M. 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-V C H Verlag Gmbh, Weinheim",
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",
volume = "54",
number = "3",
pages = "373-380",
doi = "10.1002/mnfr.200900035"
}

Popović, M. M., Milovanovic, M., Burazer, L. M., Vučković, O., Hoffmann-Sommergruber, K., Knulst, A. C., Lindner, B., Petersen, A., Jankov, R. M.,& 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-V C H Verlag Gmbh, Weinheim., 54(3), 373-380.
https://doi.org/10.1002/mnfr.200900035

Popović MM, Milovanovic M, Burazer LM, Vučković O, Hoffmann-Sommergruber K, Knulst AC, Lindner B, Petersen A, Jankov RM, 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 M., Milovanovic, Mina, Burazer, Lidija M., Vučković, Olga, Hoffmann-Sommergruber, Karin, Knulst, Andre C., Lindner, Buko, Petersen, Arnd, Jankov, Ratko M., 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 . .