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Are dietary lectins relevant allergens in plant food allergy?

(2020) FOODS. 9(12).
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Abstract
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.
Keywords
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

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Citation

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MLA
Barre, Annick, et al. “Are Dietary Lectins Relevant Allergens in Plant Food Allergy?” FOODS, vol. 9, no. 12, 2020, doi:10.3390/foods9121724.
APA
Barre, A., Van Damme, E., Simplicien, M., Benoist, H., & Rougé, P. (2020). Are dietary lectins relevant allergens in plant food allergy? FOODS, 9(12). https://doi.org/10.3390/foods9121724
Chicago author-date
Barre, Annick, Els Van Damme, Mathias Simplicien, Hervé Benoist, and Pierre Rougé. 2020. “Are Dietary Lectins Relevant Allergens in Plant Food Allergy?” FOODS 9 (12). https://doi.org/10.3390/foods9121724.
Chicago author-date (all authors)
Barre, Annick, Els Van Damme, Mathias Simplicien, Hervé Benoist, and Pierre Rougé. 2020. “Are Dietary Lectins Relevant Allergens in Plant Food Allergy?” FOODS 9 (12). doi:10.3390/foods9121724.
Vancouver
1.
Barre A, Van Damme E, Simplicien M, Benoist H, Rougé P. Are dietary lectins relevant allergens in plant food allergy? FOODS. 2020;9(12).
IEEE
[1]
A. Barre, E. Van Damme, M. Simplicien, H. Benoist, and P. Rougé, “Are dietary lectins relevant allergens in plant food allergy?,” FOODS, vol. 9, no. 12, 2020.
@article{8696024,
  abstract     = {{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.}},
  articleno    = {{1724}},
  author       = {{Barre, Annick and Van Damme, Els and Simplicien, Mathias and Benoist, Hervé and Rougé, Pierre}},
  issn         = {{2304-8158}},
  journal      = {{FOODS}},
  keywords     = {{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}},
  language     = {{eng}},
  number       = {{12}},
  pages        = {{22}},
  title        = {{Are dietary lectins relevant allergens in plant food allergy?}},
  url          = {{http://doi.org/10.3390/foods9121724}},
  volume       = {{9}},
  year         = {{2020}},
}

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