Academic Journal
Are dietary lectins relevant allergens in plant food allergy?
| العنوان: | Are dietary lectins relevant allergens in plant food allergy? |
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| المؤلفون: | Barre, Annick, Van Damme, Els, Simplicien, Mathias, Benoist, Hervé, Rougé, Pierre |
| المصدر: | FOODS ; ISSN: 2304-8158 |
| سنة النشر: | 2020 |
| المجموعة: | Ghent University Academic Bibliography |
| مصطلحات موضوعية: | Biology and Life Sciences, lectin, agglutinin, Ara h agglutinin, legume lectins, soybean lectin, garlic lectin, phytohemagglutinin, chitinase, allergen, IgE-binding epitope, allergenicity, food allergy, RIBOSOME-INACTIVATING PROTEINS, ELDERBERRY SAMBUCUS-NIGRA, LIPID-TRANSFER PROTEIN, CLASS-I CHITINASES, HEV B 6.02, MOLECULAR CHARACTERIZATION, LEGUME LECTIN, PROTEOMIC ANALYSIS, CRYSTAL-STRUCTURE, CROSS-REACTIVITY |
| الوصف: | Lectins or carbohydrate-binding proteins are widely distributed in seeds and vegetative parts of edible plant species. A few lectins from different fruits and vegetables have been identified as potential food allergens, including wheat agglutinin, hevein (Hev b 6.02) from the rubber tree and chitinases containing a hevein domain from different fruits and vegetables. However, other well-known lectins from legumes have been demonstrated to behave as potential food allergens taking into account their ability to specifically bind IgE from allergic patients, trigger the degranulation of sensitized basophils, and to elicit interleukin secretion in sensitized people. These allergens include members from the different families of higher plant lectins, including legume lectins, type II ribosome-inactivating proteins (RIP-II), wheat germ agglutinin (WGA), jacalin-related lectins, GNA (Galanthus nivalis agglutinin)-like lectins, and Nictaba-related lectins. Most of these potentially active lectin allergens belong to the group of seed storage proteins (legume lectins), pathogenesis-related protein family PR-3 comprising hevein and class I, II, IV, V, VI, and VII chitinases containing a hevein domain, and type II ribosome-inactivating proteins containing a ricin B-chain domain (RIP-II). In the present review, we present an exhaustive survey of both the structural organization and structural features responsible for the allergenic potency of lectins, with special reference to lectins from dietary plant species/tissues consumed in Western countries. |
| نوع الوثيقة: | article in journal/newspaper |
| وصف الملف: | application/pdf |
| اللغة: | English |
| Relation: | https://biblio.ugent.be/publication/8696024; http://hdl.handle.net/1854/LU-8696024; http://dx.doi.org/10.3390/foods9121724; https://biblio.ugent.be/publication/8696024/file/8696025 |
| DOI: | 10.3390/foods9121724 |
| الاتاحة: | https://biblio.ugent.be/publication/8696024 http://hdl.handle.net/1854/LU-8696024 https://doi.org/10.3390/foods9121724 https://biblio.ugent.be/publication/8696024/file/8696025 |
| Rights: | Creative Commons Attribution 4.0 International Public License (CC-BY 4.0) ; info:eu-repo/semantics/openAccess |
| رقم الانضمام: | edsbas.A8F0666C |
| قاعدة البيانات: | BASE |
| DOI: | 10.3390/foods9121724 |
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