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Impact of oligomerization on the allergenicity of allergens
Type I hypersensitivity (allergic reaction) is an unsuitable or overreactive immune response to an allergen due to cross-link immunoglobulin E (IgE) antibodies bound to its high-affinity IgE receptors (FcεRIs) on effector cells. It is needless to say that at least two epitopes on allergens are requi...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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BioMed Central
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9052586/ https://www.ncbi.nlm.nih.gov/pubmed/35488339 http://dx.doi.org/10.1186/s12948-022-00172-1 |
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author | Hasan-Abad, Amin Moradi Mohammadi, Mohsen Mirzaei, Hamed Mehrabi, Mohsen Motedayyen, Hossein Arefnezhad, Reza |
author_facet | Hasan-Abad, Amin Moradi Mohammadi, Mohsen Mirzaei, Hamed Mehrabi, Mohsen Motedayyen, Hossein Arefnezhad, Reza |
author_sort | Hasan-Abad, Amin Moradi |
collection | PubMed |
description | Type I hypersensitivity (allergic reaction) is an unsuitable or overreactive immune response to an allergen due to cross-link immunoglobulin E (IgE) antibodies bound to its high-affinity IgE receptors (FcεRIs) on effector cells. It is needless to say that at least two epitopes on allergens are required to the successful and effective cross-linking. There are some reports pointing to small proteins with only one IgE epitope could cross-link FcεRI-bound IgE through homo-oligomerization which provides two same IgE epitopes. Therefore, oligomerization of allergens plays an indisputable role in the allergenic feature and stability of allergens. In this regard, we review the signaling capacity of the B cell receptor (BCR) complex and cross-linking of FcεRI which results in the synthesis of allergen-specific IgE. This review also discusses the protein-protein interactions involved in the oligomerization of allergens and provide some explanations about the oligomerization of some well-known allergens, such as calcium-binding allergens, Alt a 1, Bet v 1, Der p 1, Per a3, and Fel d 1, along with the effects of their concentrations on dimerization. |
format | Online Article Text |
id | pubmed-9052586 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-90525862022-04-30 Impact of oligomerization on the allergenicity of allergens Hasan-Abad, Amin Moradi Mohammadi, Mohsen Mirzaei, Hamed Mehrabi, Mohsen Motedayyen, Hossein Arefnezhad, Reza Clin Mol Allergy Review Type I hypersensitivity (allergic reaction) is an unsuitable or overreactive immune response to an allergen due to cross-link immunoglobulin E (IgE) antibodies bound to its high-affinity IgE receptors (FcεRIs) on effector cells. It is needless to say that at least two epitopes on allergens are required to the successful and effective cross-linking. There are some reports pointing to small proteins with only one IgE epitope could cross-link FcεRI-bound IgE through homo-oligomerization which provides two same IgE epitopes. Therefore, oligomerization of allergens plays an indisputable role in the allergenic feature and stability of allergens. In this regard, we review the signaling capacity of the B cell receptor (BCR) complex and cross-linking of FcεRI which results in the synthesis of allergen-specific IgE. This review also discusses the protein-protein interactions involved in the oligomerization of allergens and provide some explanations about the oligomerization of some well-known allergens, such as calcium-binding allergens, Alt a 1, Bet v 1, Der p 1, Per a3, and Fel d 1, along with the effects of their concentrations on dimerization. BioMed Central 2022-04-29 /pmc/articles/PMC9052586/ /pubmed/35488339 http://dx.doi.org/10.1186/s12948-022-00172-1 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visithttp://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/ (https://creativecommons.org/publicdomain/zero/1.0/) ) applies to the data made available in this article, unless otherwise stated in a credit line to the data. |
spellingShingle | Review Hasan-Abad, Amin Moradi Mohammadi, Mohsen Mirzaei, Hamed Mehrabi, Mohsen Motedayyen, Hossein Arefnezhad, Reza Impact of oligomerization on the allergenicity of allergens |
title | Impact of oligomerization on the allergenicity of allergens |
title_full | Impact of oligomerization on the allergenicity of allergens |
title_fullStr | Impact of oligomerization on the allergenicity of allergens |
title_full_unstemmed | Impact of oligomerization on the allergenicity of allergens |
title_short | Impact of oligomerization on the allergenicity of allergens |
title_sort | impact of oligomerization on the allergenicity of allergens |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9052586/ https://www.ncbi.nlm.nih.gov/pubmed/35488339 http://dx.doi.org/10.1186/s12948-022-00172-1 |
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