Pieters, Raymond

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  • Pieters, Raymond (10)
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Author's Bibliography

Applying the adverse outcome pathway (AOP) for food sensitization to support in vitro testing strategies

Lozano-Ojalvo, Daniel; Benedé, Sara; Antunes, Celia M.; Bavaro, Simona L.; Bouchaud, Grégory; Costa, Ana; Denery-Papini, Sandra; Díaz-Perales, Araceli; Garrido-Arandia, María; Gavrović-Jankulović, Marija; Hayen, Simone; Martínez-Blanco, Mónica; Molina, Elena; Monaci, Linda; Pieters, Raymond; Villemin, Clelia; Wichers, Harry J.; Wróblewska, Barbara; Willemsen, Linette E.M.; Roggen, Erwin L.; van Bilsen, Jolanda H.M.

(Elsevier, 2019)

TY  - JOUR
AU  - Lozano-Ojalvo, Daniel
AU  - Benedé, Sara
AU  - Antunes, Celia M.
AU  - Bavaro, Simona L.
AU  - Bouchaud, Grégory
AU  - Costa, Ana
AU  - Denery-Papini, Sandra
AU  - Díaz-Perales, Araceli
AU  - Garrido-Arandia, María
AU  - Gavrović-Jankulović, Marija
AU  - Hayen, Simone
AU  - Martínez-Blanco, Mónica
AU  - Molina, Elena
AU  - Monaci, Linda
AU  - Pieters, Raymond
AU  - Villemin, Clelia
AU  - Wichers, Harry J.
AU  - Wróblewska, Barbara
AU  - Willemsen, Linette E.M.
AU  - Roggen, Erwin L.
AU  - van Bilsen, Jolanda H.M.
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2864
AB  - Background: Before introducing proteins from new or alternative dietary sources into the market, a compressive risk assessment including food allergic sensitization should be carried out in order to ensure their safety. We have recently proposed the adverse outcome pathway (AOP) concept to structure the current mechanistic understanding of the molecular and cellular pathways evidenced to drive IgE-mediated food allergies. This AOP framework offers the biological context to collect and structure existing in vitro methods and to identify missing assays to evaluate sensitizing potential of food proteins. Scope and approach: In this review, we provide a state-of-the-art overview of available in vitro approaches for assessing the sensitizing potential of food proteins, including their strengths and limitations. These approaches are structured by their potential to evaluate the molecular initiating and key events driving food sensitization. Key findings and conclusions: The application of the AOP framework offers the opportunity to anchor existing testing methods to specific building blocks of the AOP for food sensitization. In general, in vitro methods evaluating mechanisms involved in the innate immune response are easier to address than assays addressing the adaptive immune response due to the low precursor frequency of allergen-specific T and B cells. Novel ex vivo culture strategies may have the potential to become useful tools for investigating the sensitizing potential of food proteins. When applied in the context of an integrated testing strategy, the described approaches may reduce, if not replace, current animal testing approaches.
PB  - Elsevier
T2  - Trends in Food Science and Technology
T1  - Applying the adverse outcome pathway (AOP) for food sensitization to support in vitro testing strategies
VL  - 85
SP  - 307
EP  - 319
DO  - 10.1016/j.tifs.2019.01.014
ER  - 
@article{
author = "Lozano-Ojalvo, Daniel and Benedé, Sara and Antunes, Celia M. and Bavaro, Simona L. and Bouchaud, Grégory and Costa, Ana and Denery-Papini, Sandra and Díaz-Perales, Araceli and Garrido-Arandia, María and Gavrović-Jankulović, Marija and Hayen, Simone and Martínez-Blanco, Mónica and Molina, Elena and Monaci, Linda and Pieters, Raymond and Villemin, Clelia and Wichers, Harry J. and Wróblewska, Barbara and Willemsen, Linette E.M. and Roggen, Erwin L. and van Bilsen, Jolanda H.M.",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2864",
abstract = "Background: Before introducing proteins from new or alternative dietary sources into the market, a compressive risk assessment including food allergic sensitization should be carried out in order to ensure their safety. We have recently proposed the adverse outcome pathway (AOP) concept to structure the current mechanistic understanding of the molecular and cellular pathways evidenced to drive IgE-mediated food allergies. This AOP framework offers the biological context to collect and structure existing in vitro methods and to identify missing assays to evaluate sensitizing potential of food proteins. Scope and approach: In this review, we provide a state-of-the-art overview of available in vitro approaches for assessing the sensitizing potential of food proteins, including their strengths and limitations. These approaches are structured by their potential to evaluate the molecular initiating and key events driving food sensitization. Key findings and conclusions: The application of the AOP framework offers the opportunity to anchor existing testing methods to specific building blocks of the AOP for food sensitization. In general, in vitro methods evaluating mechanisms involved in the innate immune response are easier to address than assays addressing the adaptive immune response due to the low precursor frequency of allergen-specific T and B cells. Novel ex vivo culture strategies may have the potential to become useful tools for investigating the sensitizing potential of food proteins. When applied in the context of an integrated testing strategy, the described approaches may reduce, if not replace, current animal testing approaches.",
publisher = "Elsevier",
journal = "Trends in Food Science and Technology",
title = "Applying the adverse outcome pathway (AOP) for food sensitization to support in vitro testing strategies",
volume = "85",
pages = "307-319",
doi = "10.1016/j.tifs.2019.01.014"
}
Lozano-Ojalvo, D., Benedé, S., Antunes, C. M., Bavaro, S. L., Bouchaud, G., Costa, A., Denery-Papini, S., Díaz-Perales, A., Garrido-Arandia, M., Gavrović-Jankulović, M., Hayen, S., Martínez-Blanco, M., Molina, E., Monaci, L., Pieters, R., Villemin, C., Wichers, H. J., Wróblewska, B., Willemsen, L. E.M., Roggen, E. L.,& van Bilsen, J. H.M. (2019). Applying the adverse outcome pathway (AOP) for food sensitization to support in vitro testing strategies.
Trends in Food Science and Technology
Elsevier., 85, 307-319.
https://doi.org/10.1016/j.tifs.2019.01.014
Lozano-Ojalvo D, Benedé S, Antunes CM, Bavaro SL, Bouchaud G, Costa A, Denery-Papini S, Díaz-Perales A, Garrido-Arandia M, Gavrović-Jankulović M, Hayen S, Martínez-Blanco M, Molina E, Monaci L, Pieters R, Villemin C, Wichers HJ, Wróblewska B, Willemsen LE, Roggen EL, van Bilsen JH. Applying the adverse outcome pathway (AOP) for food sensitization to support in vitro testing strategies. Trends in Food Science and Technology. 2019;85:307-319
Lozano-Ojalvo Daniel, Benedé Sara, Antunes Celia M., Bavaro Simona L., Bouchaud Grégory, Costa Ana, Denery-Papini Sandra, Díaz-Perales Araceli, Garrido-Arandia María, Gavrović-Jankulović Marija, Hayen Simone, Martínez-Blanco Mónica, Molina Elena, Monaci Linda, Pieters Raymond, Villemin Clelia, Wichers Harry J., Wróblewska Barbara, Willemsen Linette E.M., Roggen Erwin L., van Bilsen Jolanda H.M., "Applying the adverse outcome pathway (AOP) for food sensitization to support in vitro testing strategies" Trends in Food Science and Technology, 85 (2019):307-319,
https://doi.org/10.1016/j.tifs.2019.01.014 .
4
2
3

Activation of epithelial cells by the major kiwifruit allergen Act d 1 in human and mouse-derived intestinal model

Nešić, Andrijana; Stam, Annemarie; Čavić, Milena; Ten Klooster, Jean Paul; Pieters, Raymond; Smit, Joost; Gavrović-Jankulović, Marija

(2019)

TY  - JOUR
AU  - Nešić, Andrijana
AU  - Stam, Annemarie
AU  - Čavić, Milena
AU  - Ten Klooster, Jean Paul
AU  - Pieters, Raymond
AU  - Smit, Joost
AU  - Gavrović-Jankulović, Marija
PY  - 2019
UR  - https://www.scopus.com/inward/record.uri?eid=2-s2.0-85071845404&doi=10.1016%2fj.jff.2019.103556&partnerID=40&md5=c210fd8346babe18cc93e9b0994c4a1e
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3485
AB  - In this study, two intestinal models were employed to assess the modulatory potential of a major kiwifruit allergen on the innate immunity of epithelial cells. Effects of Act d 1 were analyzed in terms of gene expression and structural changes of tight junction (TJ) proteins, as well as up-regulation of pro-inflammatory cytokines in Caco-2 cells and, for the first time, in mouse-derived intestinal 2-dimensional (2D) organoids.

Biologically active Act d 1 induced up-regulation of TJ genes for CLDN-2, CLDN-3, CLDN-4, ZO-1, and on the protein level induced release of pro-inflammatory cytokines IL-1β, TNFα and IL-33 in both employed model systems. In 2D-organoids, active Act d 1 impaired the TJ protein networks of E-cadherin, claudin-3, and ZO-1.

2D-organoids generated from mouse intestine are a promising new model system for the assessment of allergen-induced intestinal cell responses and a useful tool for mitigation of risks associated with novel food proteins.
T2  - Journal of Functional Foods
T1  - Activation of epithelial cells by the major kiwifruit allergen Act d 1 in human and mouse-derived intestinal model
VL  - 62
DO  - 10.1016/j.jff.2019.103556
ER  - 
@article{
author = "Nešić, Andrijana and Stam, Annemarie and Čavić, Milena and Ten Klooster, Jean Paul and Pieters, Raymond and Smit, Joost and Gavrović-Jankulović, Marija",
year = "2019",
url = "https://www.scopus.com/inward/record.uri?eid=2-s2.0-85071845404&doi=10.1016%2fj.jff.2019.103556&partnerID=40&md5=c210fd8346babe18cc93e9b0994c4a1e, http://cherry.chem.bg.ac.rs/handle/123456789/3485",
abstract = "In this study, two intestinal models were employed to assess the modulatory potential of a major kiwifruit allergen on the innate immunity of epithelial cells. Effects of Act d 1 were analyzed in terms of gene expression and structural changes of tight junction (TJ) proteins, as well as up-regulation of pro-inflammatory cytokines in Caco-2 cells and, for the first time, in mouse-derived intestinal 2-dimensional (2D) organoids.

Biologically active Act d 1 induced up-regulation of TJ genes for CLDN-2, CLDN-3, CLDN-4, ZO-1, and on the protein level induced release of pro-inflammatory cytokines IL-1β, TNFα and IL-33 in both employed model systems. In 2D-organoids, active Act d 1 impaired the TJ protein networks of E-cadherin, claudin-3, and ZO-1.

2D-organoids generated from mouse intestine are a promising new model system for the assessment of allergen-induced intestinal cell responses and a useful tool for mitigation of risks associated with novel food proteins.",
journal = "Journal of Functional Foods",
title = "Activation of epithelial cells by the major kiwifruit allergen Act d 1 in human and mouse-derived intestinal model",
volume = "62",
doi = "10.1016/j.jff.2019.103556"
}
Nešić, A., Stam, A., Čavić, M., Ten Klooster, J. P., Pieters, R., Smit, J.,& Gavrović-Jankulović, M. (2019). Activation of epithelial cells by the major kiwifruit allergen Act d 1 in human and mouse-derived intestinal model.
Journal of Functional Foods, 62.
https://doi.org/10.1016/j.jff.2019.103556
Nešić A, Stam A, Čavić M, Ten Klooster JP, Pieters R, Smit J, Gavrović-Jankulović M. Activation of epithelial cells by the major kiwifruit allergen Act d 1 in human and mouse-derived intestinal model. Journal of Functional Foods. 2019;62
Nešić Andrijana, Stam Annemarie, Čavić Milena, Ten Klooster Jean Paul, Pieters Raymond, Smit Joost, Gavrović-Jankulović Marija, "Activation of epithelial cells by the major kiwifruit allergen Act d 1 in human and mouse-derived intestinal model" Journal of Functional Foods, 62 (2019),
https://doi.org/10.1016/j.jff.2019.103556 .
2
1
1

The kiwifruit allergen act d 1 activates NF-κB signaling and affects mRNA expression of TJ proteins and innate pro-allergenic cytokines

Nešić, Andrijana N.; Čavić, Milena; Popović, Milica; Zlatanova, Milena; Pieters, Raymond; Smit, Joost; Gavrović-Jankulović, Marija

(MDPI, 2019)

TY  - JOUR
AU  - Nešić, Andrijana N.
AU  - Čavić, Milena
AU  - Popović, Milica
AU  - Zlatanova, Milena
AU  - Pieters, Raymond
AU  - Smit, Joost
AU  - Gavrović-Jankulović, Marija
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3799
AB  - Impairment of the intestinal barrier is one of the key events in the initiation of the sensitization process in food allergy. The aim of this study was to explore the effects of kiwifruit allergen Act d 1 on intestinal permeability and tight junction protein (TJP) gene expression in vivo and to explore its potential to activate the NF-ĸB signaling pathway and to regulate expression of epithelial pro-allergenic cytokines. Influences of Act d 1 on TJP gene expression and pro-allergenic cytokines in the mouse intestine was analyzed by qPCR upon allergen administration by oral gavage. The effect on the in vivo intestinal permeability was assessed in ELISA by measuring the translocation of β-lactoglobulin (BLG) into circulation. The capacity of Act d 1 to activate the NF-ĸB pathway was tested in HEK293 cells by fluorescent microscopy and flow cytometry. Administration of Actinidin (Act d 1) increased intestinal permeability to the BLG. This was accompanied by changes in gene expression of TJP mRNA and pro-allergenic cytokines IL-25, IL-33, and thymic stromal lymphopoietin (TSLP) compared to the control. Act d 1 reduced TEER of the HEK293 monolayer, was positive in an NF-ĸB-reporter HEK293 cell assay, and induced secretion of TSLP. These findings shed more light on the molecular events in the sensitization process of kiwifruit but possibly also of other protease food allergens.
PB  - MDPI
T2  - Biomolecules
T1  - The kiwifruit allergen act d 1 activates NF-κB signaling and affects mRNA expression of TJ proteins and innate pro-allergenic cytokines
VL  - 9
IS  - 12
SP  - 816
DO  - 10.3390/biom9120816
ER  - 
@article{
author = "Nešić, Andrijana N. and Čavić, Milena and Popović, Milica and Zlatanova, Milena and Pieters, Raymond and Smit, Joost and Gavrović-Jankulović, Marija",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3799",
abstract = "Impairment of the intestinal barrier is one of the key events in the initiation of the sensitization process in food allergy. The aim of this study was to explore the effects of kiwifruit allergen Act d 1 on intestinal permeability and tight junction protein (TJP) gene expression in vivo and to explore its potential to activate the NF-ĸB signaling pathway and to regulate expression of epithelial pro-allergenic cytokines. Influences of Act d 1 on TJP gene expression and pro-allergenic cytokines in the mouse intestine was analyzed by qPCR upon allergen administration by oral gavage. The effect on the in vivo intestinal permeability was assessed in ELISA by measuring the translocation of β-lactoglobulin (BLG) into circulation. The capacity of Act d 1 to activate the NF-ĸB pathway was tested in HEK293 cells by fluorescent microscopy and flow cytometry. Administration of Actinidin (Act d 1) increased intestinal permeability to the BLG. This was accompanied by changes in gene expression of TJP mRNA and pro-allergenic cytokines IL-25, IL-33, and thymic stromal lymphopoietin (TSLP) compared to the control. Act d 1 reduced TEER of the HEK293 monolayer, was positive in an NF-ĸB-reporter HEK293 cell assay, and induced secretion of TSLP. These findings shed more light on the molecular events in the sensitization process of kiwifruit but possibly also of other protease food allergens.",
publisher = "MDPI",
journal = "Biomolecules",
title = "The kiwifruit allergen act d 1 activates NF-κB signaling and affects mRNA expression of TJ proteins and innate pro-allergenic cytokines",
volume = "9",
number = "12",
pages = "816",
doi = "10.3390/biom9120816"
}
Nešić, A. N., Čavić, M., Popović, M., Zlatanova, M., Pieters, R., Smit, J.,& Gavrović-Jankulović, M. (2019). The kiwifruit allergen act d 1 activates NF-κB signaling and affects mRNA expression of TJ proteins and innate pro-allergenic cytokines.
Biomolecules
MDPI., 9(12), 816.
https://doi.org/10.3390/biom9120816
Nešić AN, Čavić M, Popović M, Zlatanova M, Pieters R, Smit J, Gavrović-Jankulović M. The kiwifruit allergen act d 1 activates NF-κB signaling and affects mRNA expression of TJ proteins and innate pro-allergenic cytokines. Biomolecules. 2019;9(12):816
Nešić Andrijana N., Čavić Milena, Popović Milica, Zlatanova Milena, Pieters Raymond, Smit Joost, Gavrović-Jankulović Marija, "The kiwifruit allergen act d 1 activates NF-κB signaling and affects mRNA expression of TJ proteins and innate pro-allergenic cytokines" Biomolecules, 9, no. 12 (2019):816,
https://doi.org/10.3390/biom9120816 .
1
3
2

Applying the adverse outcome pathway (AOP) for food sensitization to support in vitro testing strategies

Lozano-Ojalvo, Daniel; Benedé, Sara; Antunes, Celia M.; Bavaro, Simona L.; Bouchaud, Grégory; Costa, Ana; Denery-Papini, Sandra; Díaz-Perales, Araceli; Garrido-Arandia, María; Gavrović-Jankulović, Marija; Hayen, Simone; Martínez-Blanco, Mónica; Molina, Elena; Monaci, Linda; Pieters, Raymond; Villemin, Clelia; Wichers, Harry J.; Wróblewska, Barbara; Willemsen, Linette E.M.; Roggen, Erwin L.; van Bilsen, Jolanda H.M.

(Elsevier, 2019)

TY  - JOUR
AU  - Lozano-Ojalvo, Daniel
AU  - Benedé, Sara
AU  - Antunes, Celia M.
AU  - Bavaro, Simona L.
AU  - Bouchaud, Grégory
AU  - Costa, Ana
AU  - Denery-Papini, Sandra
AU  - Díaz-Perales, Araceli
AU  - Garrido-Arandia, María
AU  - Gavrović-Jankulović, Marija
AU  - Hayen, Simone
AU  - Martínez-Blanco, Mónica
AU  - Molina, Elena
AU  - Monaci, Linda
AU  - Pieters, Raymond
AU  - Villemin, Clelia
AU  - Wichers, Harry J.
AU  - Wróblewska, Barbara
AU  - Willemsen, Linette E.M.
AU  - Roggen, Erwin L.
AU  - van Bilsen, Jolanda H.M.
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2852
AB  - Background: Before introducing proteins from new or alternative dietary sources into the market, a compressive risk assessment including food allergic sensitization should be carried out in order to ensure their safety. We have recently proposed the adverse outcome pathway (AOP) concept to structure the current mechanistic understanding of the molecular and cellular pathways evidenced to drive IgE-mediated food allergies. This AOP framework offers the biological context to collect and structure existing in vitro methods and to identify missing assays to evaluate sensitizing potential of food proteins. Scope and approach: In this review, we provide a state-of-the-art overview of available in vitro approaches for assessing the sensitizing potential of food proteins, including their strengths and limitations. These approaches are structured by their potential to evaluate the molecular initiating and key events driving food sensitization. Key findings and conclusions: The application of the AOP framework offers the opportunity to anchor existing testing methods to specific building blocks of the AOP for food sensitization. In general, in vitro methods evaluating mechanisms involved in the innate immune response are easier to address than assays addressing the adaptive immune response due to the low precursor frequency of allergen-specific T and B cells. Novel ex vivo culture strategies may have the potential to become useful tools for investigating the sensitizing potential of food proteins. When applied in the context of an integrated testing strategy, the described approaches may reduce, if not replace, current animal testing approaches.
PB  - Elsevier
T2  - Trends in Food Science and Technology
T1  - Applying the adverse outcome pathway (AOP) for food sensitization to support in vitro testing strategies
VL  - 85
SP  - 307
EP  - 319
DO  - 10.1016/j.tifs.2019.01.014
ER  - 
@article{
author = "Lozano-Ojalvo, Daniel and Benedé, Sara and Antunes, Celia M. and Bavaro, Simona L. and Bouchaud, Grégory and Costa, Ana and Denery-Papini, Sandra and Díaz-Perales, Araceli and Garrido-Arandia, María and Gavrović-Jankulović, Marija and Hayen, Simone and Martínez-Blanco, Mónica and Molina, Elena and Monaci, Linda and Pieters, Raymond and Villemin, Clelia and Wichers, Harry J. and Wróblewska, Barbara and Willemsen, Linette E.M. and Roggen, Erwin L. and van Bilsen, Jolanda H.M.",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2852",
abstract = "Background: Before introducing proteins from new or alternative dietary sources into the market, a compressive risk assessment including food allergic sensitization should be carried out in order to ensure their safety. We have recently proposed the adverse outcome pathway (AOP) concept to structure the current mechanistic understanding of the molecular and cellular pathways evidenced to drive IgE-mediated food allergies. This AOP framework offers the biological context to collect and structure existing in vitro methods and to identify missing assays to evaluate sensitizing potential of food proteins. Scope and approach: In this review, we provide a state-of-the-art overview of available in vitro approaches for assessing the sensitizing potential of food proteins, including their strengths and limitations. These approaches are structured by their potential to evaluate the molecular initiating and key events driving food sensitization. Key findings and conclusions: The application of the AOP framework offers the opportunity to anchor existing testing methods to specific building blocks of the AOP for food sensitization. In general, in vitro methods evaluating mechanisms involved in the innate immune response are easier to address than assays addressing the adaptive immune response due to the low precursor frequency of allergen-specific T and B cells. Novel ex vivo culture strategies may have the potential to become useful tools for investigating the sensitizing potential of food proteins. When applied in the context of an integrated testing strategy, the described approaches may reduce, if not replace, current animal testing approaches.",
publisher = "Elsevier",
journal = "Trends in Food Science and Technology",
title = "Applying the adverse outcome pathway (AOP) for food sensitization to support in vitro testing strategies",
volume = "85",
pages = "307-319",
doi = "10.1016/j.tifs.2019.01.014"
}
Lozano-Ojalvo, D., Benedé, S., Antunes, C. M., Bavaro, S. L., Bouchaud, G., Costa, A., Denery-Papini, S., Díaz-Perales, A., Garrido-Arandia, M., Gavrović-Jankulović, M., Hayen, S., Martínez-Blanco, M., Molina, E., Monaci, L., Pieters, R., Villemin, C., Wichers, H. J., Wróblewska, B., Willemsen, L. E.M., Roggen, E. L.,& van Bilsen, J. H.M. (2019). Applying the adverse outcome pathway (AOP) for food sensitization to support in vitro testing strategies.
Trends in Food Science and Technology
Elsevier., 85, 307-319.
https://doi.org/10.1016/j.tifs.2019.01.014
Lozano-Ojalvo D, Benedé S, Antunes CM, Bavaro SL, Bouchaud G, Costa A, Denery-Papini S, Díaz-Perales A, Garrido-Arandia M, Gavrović-Jankulović M, Hayen S, Martínez-Blanco M, Molina E, Monaci L, Pieters R, Villemin C, Wichers HJ, Wróblewska B, Willemsen LE, Roggen EL, van Bilsen JH. Applying the adverse outcome pathway (AOP) for food sensitization to support in vitro testing strategies. Trends in Food Science and Technology. 2019;85:307-319
Lozano-Ojalvo Daniel, Benedé Sara, Antunes Celia M., Bavaro Simona L., Bouchaud Grégory, Costa Ana, Denery-Papini Sandra, Díaz-Perales Araceli, Garrido-Arandia María, Gavrović-Jankulović Marija, Hayen Simone, Martínez-Blanco Mónica, Molina Elena, Monaci Linda, Pieters Raymond, Villemin Clelia, Wichers Harry J., Wróblewska Barbara, Willemsen Linette E.M., Roggen Erwin L., van Bilsen Jolanda H.M., "Applying the adverse outcome pathway (AOP) for food sensitization to support in vitro testing strategies" Trends in Food Science and Technology, 85 (2019):307-319,
https://doi.org/10.1016/j.tifs.2019.01.014 .
4
2
3

Supplementary material for the article: Perusko, M.; van Roest, M.; Stanic-Vucinic, D.; Simons, P. J.; Pieters, R. H. H.; Cirkovic Velickovic, T.; Smit, J. J. Glycation of the Major Milk Allergen β-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation. Molecular Nutrition and Food Research 2018, 62 (17). https://doi.org/10.1002/mnfr.201800341

Peruško, Marija; van Roest, Manon; Stanić-Vučinić, Dragana; Simons, Peter J.; Pieters, Raymond; Ćirković-Veličković, Tanja; Smit, Joost

(Wiley, Hoboken, 2018)

TY  - BOOK
AU  - Peruško, Marija
AU  - van Roest, Manon
AU  - Stanić-Vučinić, Dragana
AU  - Simons, Peter J.
AU  - Pieters, Raymond
AU  - Ćirković-Veličković, Tanja
AU  - Smit, Joost
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3205
PB  - Wiley, Hoboken
T2  - Molecular Nutrition and Food Research
T1  - Supplementary material for the article: Perusko, M.; van Roest, M.; Stanic-Vucinic, D.; Simons, P. J.; Pieters, R. H. H.; Cirkovic Velickovic, T.; Smit, J. J. Glycation of the Major Milk Allergen β-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation. Molecular Nutrition and Food Research 2018, 62 (17). https://doi.org/10.1002/mnfr.201800341
ER  - 
@book{
author = "Peruško, Marija and van Roest, Manon and Stanić-Vučinić, Dragana and Simons, Peter J. and Pieters, Raymond and Ćirković-Veličković, Tanja and Smit, Joost",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3205",
publisher = "Wiley, Hoboken",
journal = "Molecular Nutrition and Food Research",
title = "Supplementary material for the article: Perusko, M.; van Roest, M.; Stanic-Vucinic, D.; Simons, P. J.; Pieters, R. H. H.; Cirkovic Velickovic, T.; Smit, J. J. Glycation of the Major Milk Allergen β-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation. Molecular Nutrition and Food Research 2018, 62 (17). https://doi.org/10.1002/mnfr.201800341"
}
Peruško, M., van Roest, M., Stanić-Vučinić, D., Simons, P. J., Pieters, R., Ćirković-Veličković, T.,& Smit, J. (2018). Supplementary material for the article: Perusko, M.; van Roest, M.; Stanic-Vucinic, D.; Simons, P. J.; Pieters, R. H. H.; Cirkovic Velickovic, T.; Smit, J. J. Glycation of the Major Milk Allergen β-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation. Molecular Nutrition and Food Research 2018, 62 (17). https://doi.org/10.1002/mnfr.201800341.
Molecular Nutrition and Food Research
Wiley, Hoboken..
Peruško M, van Roest M, Stanić-Vučinić D, Simons PJ, Pieters R, Ćirković-Veličković T, Smit J. Supplementary material for the article: Perusko, M.; van Roest, M.; Stanic-Vucinic, D.; Simons, P. J.; Pieters, R. H. H.; Cirkovic Velickovic, T.; Smit, J. J. Glycation of the Major Milk Allergen β-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation. Molecular Nutrition and Food Research 2018, 62 (17). https://doi.org/10.1002/mnfr.201800341. Molecular Nutrition and Food Research. 2018;
Peruško Marija, van Roest Manon, Stanić-Vučinić Dragana, Simons Peter J., Pieters Raymond, Ćirković-Veličković Tanja, Smit Joost, "Supplementary material for the article: Perusko, M.; van Roest, M.; Stanic-Vucinic, D.; Simons, P. J.; Pieters, R. H. H.; Cirkovic Velickovic, T.; Smit, J. J. Glycation of the Major Milk Allergen β-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation. Molecular Nutrition and Food Research 2018, 62 (17). https://doi.org/10.1002/mnfr.201800341" Molecular Nutrition and Food Research (2018)

Glycation of the Major Milk Allergen beta-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation

Peruško, Marija; van Roest, Manon; Stanić-Vučinić, Dragana; Simons, Peter J.; Pieters, Raymond; Ćirković-Veličković, Tanja; Smit, Joost

(Wiley, Hoboken, 2018)

TY  - JOUR
AU  - Peruško, Marija
AU  - van Roest, Manon
AU  - Stanić-Vučinić, Dragana
AU  - Simons, Peter J.
AU  - Pieters, Raymond
AU  - Ćirković-Veličković, Tanja
AU  - Smit, Joost
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2212
AB  - Scope: During food processing, the Maillard reaction (MR) may occur, resulting in the formation of glycated proteins. Glycated proteins are of particular importance in food allergies because glycation may influence interactions with the immune system. This study compared native and extensively glycated milk allergen beta-lactoglobulin (BLG), in their interactions with cells crucially involved in allergy. Methods and results: BLG was glycated in MR and characterized. Native and glycated BLG were tested in experiments of epithelial transport, uptake and degradation by DCs, T-cell cytokine responses, and basophil cell degranulation using ELISA and flow cytometry. Glycation of BLG induced partial unfolding and reduced its intestinal epithelial transfer over a Caco-2 monolayer. Uptake of glycated BLG by bone marrow-derived dendritic cells (BMDC) was increased, although both BLG forms entered BMDC via the same mechanism, receptor-mediated endocytosis. Once inside the BMDC, glycated BLG was degraded faster, which might have led to observed lower cytokine production in BMDC/CD4(+) T-cells coculture. Finally, glycated BLG was less efficient in induction of degranulation of BLG-specific IgE sensitized basophil cells. Conclusions: This study suggests that glycation of BLG by MR significantly alters its fate in processes involved in immunogenicity and allergenicity, pointing out the importance of food processing in food allergy.
PB  - Wiley, Hoboken
T2  - Molecular Nutrition and Food Research
T1  - Glycation of the Major Milk Allergen beta-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation
VL  - 62
IS  - 17
DO  - 10.1002/mnfr.201800341
ER  - 
@article{
author = "Peruško, Marija and van Roest, Manon and Stanić-Vučinić, Dragana and Simons, Peter J. and Pieters, Raymond and Ćirković-Veličković, Tanja and Smit, Joost",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2212",
abstract = "Scope: During food processing, the Maillard reaction (MR) may occur, resulting in the formation of glycated proteins. Glycated proteins are of particular importance in food allergies because glycation may influence interactions with the immune system. This study compared native and extensively glycated milk allergen beta-lactoglobulin (BLG), in their interactions with cells crucially involved in allergy. Methods and results: BLG was glycated in MR and characterized. Native and glycated BLG were tested in experiments of epithelial transport, uptake and degradation by DCs, T-cell cytokine responses, and basophil cell degranulation using ELISA and flow cytometry. Glycation of BLG induced partial unfolding and reduced its intestinal epithelial transfer over a Caco-2 monolayer. Uptake of glycated BLG by bone marrow-derived dendritic cells (BMDC) was increased, although both BLG forms entered BMDC via the same mechanism, receptor-mediated endocytosis. Once inside the BMDC, glycated BLG was degraded faster, which might have led to observed lower cytokine production in BMDC/CD4(+) T-cells coculture. Finally, glycated BLG was less efficient in induction of degranulation of BLG-specific IgE sensitized basophil cells. Conclusions: This study suggests that glycation of BLG by MR significantly alters its fate in processes involved in immunogenicity and allergenicity, pointing out the importance of food processing in food allergy.",
publisher = "Wiley, Hoboken",
journal = "Molecular Nutrition and Food Research",
title = "Glycation of the Major Milk Allergen beta-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation",
volume = "62",
number = "17",
doi = "10.1002/mnfr.201800341"
}
Peruško, M., van Roest, M., Stanić-Vučinić, D., Simons, P. J., Pieters, R., Ćirković-Veličković, T.,& Smit, J. (2018). Glycation of the Major Milk Allergen beta-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation.
Molecular Nutrition and Food Research
Wiley, Hoboken., 62(17).
https://doi.org/10.1002/mnfr.201800341
Peruško M, van Roest M, Stanić-Vučinić D, Simons PJ, Pieters R, Ćirković-Veličković T, Smit J. Glycation of the Major Milk Allergen beta-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation. Molecular Nutrition and Food Research. 2018;62(17)
Peruško Marija, van Roest Manon, Stanić-Vučinić Dragana, Simons Peter J., Pieters Raymond, Ćirković-Veličković Tanja, Smit Joost, "Glycation of the Major Milk Allergen beta-Lactoglobulin Changes Its Allergenicity by Alterations in Cellular Uptake and Degradation" Molecular Nutrition and Food Research, 62, no. 17 (2018),
https://doi.org/10.1002/mnfr.201800341 .
2
14
11
12

Assessing immunogenicity of enzymatically cross-linked beta-lactoglobulin using dendritic-cell derived endolysosomal degradome

Stojadinović, Marija M.; Pieters, Raymond; Smit, Joost; Ćirković-Veličković, Tanja

(Wiley-Blackwell, Hoboken, 2014)

TY  - CONF
AU  - Stojadinović, Marija M.
AU  - Pieters, Raymond
AU  - Smit, Joost
AU  - Ćirković-Veličković, Tanja
PY  - 2014
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1755
PB  - Wiley-Blackwell, Hoboken
C3  - FEBS Journal / Federation of European of Biochemical Societies
T1  - Assessing immunogenicity of enzymatically cross-linked beta-lactoglobulin using dendritic-cell derived endolysosomal degradome
VL  - 281
SP  - 98
EP  - 98
ER  - 
@conference{
author = "Stojadinović, Marija M. and Pieters, Raymond and Smit, Joost and Ćirković-Veličković, Tanja",
year = "2014",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1755",
publisher = "Wiley-Blackwell, Hoboken",
journal = "FEBS Journal / Federation of European of Biochemical Societies",
title = "Assessing immunogenicity of enzymatically cross-linked beta-lactoglobulin using dendritic-cell derived endolysosomal degradome",
volume = "281",
pages = "98-98"
}
Stojadinović, M. M., Pieters, R., Smit, J.,& Ćirković-Veličković, T. (2014). Assessing immunogenicity of enzymatically cross-linked beta-lactoglobulin using dendritic-cell derived endolysosomal degradome.
FEBS Journal / Federation of European of Biochemical Societies
Wiley-Blackwell, Hoboken., 281, 98-98.
Stojadinović MM, Pieters R, Smit J, Ćirković-Veličković T. Assessing immunogenicity of enzymatically cross-linked beta-lactoglobulin using dendritic-cell derived endolysosomal degradome. FEBS Journal / Federation of European of Biochemical Societies. 2014;281:98-98
Stojadinović Marija M., Pieters Raymond, Smit Joost, Ćirković-Veličković Tanja, "Assessing immunogenicity of enzymatically cross-linked beta-lactoglobulin using dendritic-cell derived endolysosomal degradome" FEBS Journal / Federation of European of Biochemical Societies, 281 (2014):98-98

Cross-Linking of beta-Lactoglobulin Enhances Allergic Sensitization Through Changes in Cellular Uptake and Processing

Stojadinović, Marija M.; Pieters, Raymond; Smit, Joost; Ćirković-Veličković, Tanja

(Oxford Univ Press, Oxford, 2014)

TY  - JOUR
AU  - Stojadinović, Marija M.
AU  - Pieters, Raymond
AU  - Smit, Joost
AU  - Ćirković-Veličković, Tanja
PY  - 2014
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1823
AB  - Cross-linking of proteins has been exploited by the food industry to change food texture and functionality but the effects of these manipulations on food allergenicity still remain unclear. To model the safety assessment of these food biopolymers, we created cross-linked bovine beta-lactoglobulin (CL-BLG) by laccase treatment. The purpose of the present study was to compare the immunogenicity and allergenicity of CL-BLG with native BLG in a mouse model of food allergy. First, BALB/c mice were intragastrically sensitized and orally challenged with BLG or CL-BLG and BLG-specific serum antibodies and splenic leukocyte cytokine production and cell proliferation were measured. Hereafter, epithelial protein uptake was monitored in vitro and in vivo and the effects of BLG cross-linking on interactions with dendritic cells were analyzed in vitro. Sensitization of mice with CL-BLG resulted in higher levels of IgE, IgG1, and IgG2a. In contrast, a subsequent oral challenge with CL-BLG resulted in lower mast cell degranulation. Cross-linking of BLG reduced its epithelial uptake but promoted sampling through Peyer's patches. Differences in endocytosis by dendritic cells (DCs) and in vitro endolysosomal processing were observed between BLG and CL-BLG. CL-BLG primed DCs induced higher Th2 response in vitro. Cross-linking of BLG increased its sensitizing capacity, implying that the assessment of highly polymerized food proteins is of clinical importance in food allergy. Moreover, manufacturers of foods or therapeutic proteins should pay considerate attention to the health risk of protein aggregation.
PB  - Oxford Univ Press, Oxford
T2  - Toxicological Sciences
T1  - Cross-Linking of beta-Lactoglobulin Enhances Allergic Sensitization Through Changes in Cellular Uptake and Processing
VL  - 140
IS  - 1
SP  - 224
EP  - 235
DO  - 10.1093/toxsci/kfu062
ER  - 
@article{
author = "Stojadinović, Marija M. and Pieters, Raymond and Smit, Joost and Ćirković-Veličković, Tanja",
year = "2014",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1823",
abstract = "Cross-linking of proteins has been exploited by the food industry to change food texture and functionality but the effects of these manipulations on food allergenicity still remain unclear. To model the safety assessment of these food biopolymers, we created cross-linked bovine beta-lactoglobulin (CL-BLG) by laccase treatment. The purpose of the present study was to compare the immunogenicity and allergenicity of CL-BLG with native BLG in a mouse model of food allergy. First, BALB/c mice were intragastrically sensitized and orally challenged with BLG or CL-BLG and BLG-specific serum antibodies and splenic leukocyte cytokine production and cell proliferation were measured. Hereafter, epithelial protein uptake was monitored in vitro and in vivo and the effects of BLG cross-linking on interactions with dendritic cells were analyzed in vitro. Sensitization of mice with CL-BLG resulted in higher levels of IgE, IgG1, and IgG2a. In contrast, a subsequent oral challenge with CL-BLG resulted in lower mast cell degranulation. Cross-linking of BLG reduced its epithelial uptake but promoted sampling through Peyer's patches. Differences in endocytosis by dendritic cells (DCs) and in vitro endolysosomal processing were observed between BLG and CL-BLG. CL-BLG primed DCs induced higher Th2 response in vitro. Cross-linking of BLG increased its sensitizing capacity, implying that the assessment of highly polymerized food proteins is of clinical importance in food allergy. Moreover, manufacturers of foods or therapeutic proteins should pay considerate attention to the health risk of protein aggregation.",
publisher = "Oxford Univ Press, Oxford",
journal = "Toxicological Sciences",
title = "Cross-Linking of beta-Lactoglobulin Enhances Allergic Sensitization Through Changes in Cellular Uptake and Processing",
volume = "140",
number = "1",
pages = "224-235",
doi = "10.1093/toxsci/kfu062"
}
Stojadinović, M. M., Pieters, R., Smit, J.,& Ćirković-Veličković, T. (2014). Cross-Linking of beta-Lactoglobulin Enhances Allergic Sensitization Through Changes in Cellular Uptake and Processing.
Toxicological Sciences
Oxford Univ Press, Oxford., 140(1), 224-235.
https://doi.org/10.1093/toxsci/kfu062
Stojadinović MM, Pieters R, Smit J, Ćirković-Veličković T. Cross-Linking of beta-Lactoglobulin Enhances Allergic Sensitization Through Changes in Cellular Uptake and Processing. Toxicological Sciences. 2014;140(1):224-235
Stojadinović Marija M., Pieters Raymond, Smit Joost, Ćirković-Veličković Tanja, "Cross-Linking of beta-Lactoglobulin Enhances Allergic Sensitization Through Changes in Cellular Uptake and Processing" Toxicological Sciences, 140, no. 1 (2014):224-235,
https://doi.org/10.1093/toxsci/kfu062 .
2
39
33
38

Effect of enzymatic cross-linking on allergenic properties of bovine beta-lactoglobulin

Stojadinović, Marija M.; Ćirković-Veličković, Tanja; Pieters, Raymond; Smit, Joost

(Wiley-Blackwell, Hoboken, 2013)

TY  - CONF
AU  - Stojadinović, Marija M.
AU  - Ćirković-Veličković, Tanja
AU  - Pieters, Raymond
AU  - Smit, Joost
PY  - 2013
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1417
PB  - Wiley-Blackwell, Hoboken
C3  - FEBS Journal / Federation of European of Biochemical Societies
T1  - Effect of enzymatic cross-linking on allergenic properties of bovine beta-lactoglobulin
VL  - 280
SP  - 467
EP  - 467
ER  - 
@conference{
author = "Stojadinović, Marija M. and Ćirković-Veličković, Tanja and Pieters, Raymond and Smit, Joost",
year = "2013",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1417",
publisher = "Wiley-Blackwell, Hoboken",
journal = "FEBS Journal / Federation of European of Biochemical Societies",
title = "Effect of enzymatic cross-linking on allergenic properties of bovine beta-lactoglobulin",
volume = "280",
pages = "467-467"
}
Stojadinović, M. M., Ćirković-Veličković, T., Pieters, R.,& Smit, J. (2013). Effect of enzymatic cross-linking on allergenic properties of bovine beta-lactoglobulin.
FEBS Journal / Federation of European of Biochemical Societies
Wiley-Blackwell, Hoboken., 280, 467-467.
Stojadinović MM, Ćirković-Veličković T, Pieters R, Smit J. Effect of enzymatic cross-linking on allergenic properties of bovine beta-lactoglobulin. FEBS Journal / Federation of European of Biochemical Societies. 2013;280:467-467
Stojadinović Marija M., Ćirković-Veličković Tanja, Pieters Raymond, Smit Joost, "Effect of enzymatic cross-linking on allergenic properties of bovine beta-lactoglobulin" FEBS Journal / Federation of European of Biochemical Societies, 280 (2013):467-467

Allergenic potential of cross-linked peanut proteins

Radosavljević, Jelena; Luka, M.; Karina, W.; Emilia, S.; Johanna, B.; Pieters, Raymond; Smit, Joost; Ćirković-Veličković, Tanja

(Wiley-Blackwell, Hoboken, 2010)

TY  - CONF
AU  - Radosavljević, Jelena
AU  - Luka, M.
AU  - Karina, W.
AU  - Emilia, S.
AU  - Johanna, B.
AU  - Pieters, Raymond
AU  - Smit, Joost
AU  - Ćirković-Veličković, Tanja
PY  - 2010
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1470
PB  - Wiley-Blackwell, Hoboken
C3  - Allergy
T1  - Allergenic potential of cross-linked peanut proteins
VL  - 65
SP  - 403
EP  - 403
ER  - 
@conference{
author = "Radosavljević, Jelena and Luka, M. and Karina, W. and Emilia, S. and Johanna, B. and Pieters, Raymond and Smit, Joost and Ćirković-Veličković, Tanja",
year = "2010",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1470",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "Allergenic potential of cross-linked peanut proteins",
volume = "65",
pages = "403-403"
}
Radosavljević, J., Luka, M., Karina, W., Emilia, S., Johanna, B., Pieters, R., Smit, J.,& Ćirković-Veličković, T. (2010). Allergenic potential of cross-linked peanut proteins.
Allergy
Wiley-Blackwell, Hoboken., 65, 403-403.
Radosavljević J, Luka M, Karina W, Emilia S, Johanna B, Pieters R, Smit J, Ćirković-Veličković T. Allergenic potential of cross-linked peanut proteins. Allergy. 2010;65:403-403
Radosavljević Jelena, Luka M., Karina W., Emilia S., Johanna B., Pieters Raymond, Smit Joost, Ćirković-Veličković Tanja, "Allergenic potential of cross-linked peanut proteins" Allergy, 65 (2010):403-403