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Characterization of 2S albumin allergenic proteins for anaphylaxis in common buckwheat

2S albumin (2SA) is responsible for anaphylaxis following consumption of buckwheat in allergic individuals. To reduce allergen incidents, characterization of 2SA polypeptides is prerequisite, thus was analyzed in this study. Of the five 2S albumin genes (g03, g11, g13, g14, and g28), g03 was seeming...

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Autores principales: Katsube-Tanaka, Tomoyuki, Monshi, Fakhrul Islam
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9363963/
https://www.ncbi.nlm.nih.gov/pubmed/35968535
http://dx.doi.org/10.1016/j.fochms.2022.100127
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author Katsube-Tanaka, Tomoyuki
Monshi, Fakhrul Islam
author_facet Katsube-Tanaka, Tomoyuki
Monshi, Fakhrul Islam
author_sort Katsube-Tanaka, Tomoyuki
collection PubMed
description 2S albumin (2SA) is responsible for anaphylaxis following consumption of buckwheat in allergic individuals. To reduce allergen incidents, characterization of 2SA polypeptides is prerequisite, thus was analyzed in this study. Of the five 2S albumin genes (g03, g11, g13, g14, and g28), g03 was seemingly non-functional. The g14 content was 3- and 40-fold higher than that of g11/g28 and g13, respectively. The g11/g28 were more processed to a ∼8 kDa band from a 16 kDa band than g14 in seeds, agreeing with that g11/g28 have high similarity with Fag e 8kD. Meanwhile, anti-g13 produced only a single ∼10 kDa band. Modification of g13 and domain exchange between g13 and g14 suggested that the hydrophobicity of the first domain and the nature of some amino acids in g13 contributed, at least in part, to the lower apparent molecular weight of g13 than expected. Thus, g13 might be an unexplored and noteworthy allergen.
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spelling pubmed-93639632022-08-11 Characterization of 2S albumin allergenic proteins for anaphylaxis in common buckwheat Katsube-Tanaka, Tomoyuki Monshi, Fakhrul Islam Food Chem (Oxf) Research Article 2S albumin (2SA) is responsible for anaphylaxis following consumption of buckwheat in allergic individuals. To reduce allergen incidents, characterization of 2SA polypeptides is prerequisite, thus was analyzed in this study. Of the five 2S albumin genes (g03, g11, g13, g14, and g28), g03 was seemingly non-functional. The g14 content was 3- and 40-fold higher than that of g11/g28 and g13, respectively. The g11/g28 were more processed to a ∼8 kDa band from a 16 kDa band than g14 in seeds, agreeing with that g11/g28 have high similarity with Fag e 8kD. Meanwhile, anti-g13 produced only a single ∼10 kDa band. Modification of g13 and domain exchange between g13 and g14 suggested that the hydrophobicity of the first domain and the nature of some amino acids in g13 contributed, at least in part, to the lower apparent molecular weight of g13 than expected. Thus, g13 might be an unexplored and noteworthy allergen. Elsevier 2022-07-26 /pmc/articles/PMC9363963/ /pubmed/35968535 http://dx.doi.org/10.1016/j.fochms.2022.100127 Text en © 2022 The Author(s) https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Research Article
Katsube-Tanaka, Tomoyuki
Monshi, Fakhrul Islam
Characterization of 2S albumin allergenic proteins for anaphylaxis in common buckwheat
title Characterization of 2S albumin allergenic proteins for anaphylaxis in common buckwheat
title_full Characterization of 2S albumin allergenic proteins for anaphylaxis in common buckwheat
title_fullStr Characterization of 2S albumin allergenic proteins for anaphylaxis in common buckwheat
title_full_unstemmed Characterization of 2S albumin allergenic proteins for anaphylaxis in common buckwheat
title_short Characterization of 2S albumin allergenic proteins for anaphylaxis in common buckwheat
title_sort characterization of 2s albumin allergenic proteins for anaphylaxis in common buckwheat
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9363963/
https://www.ncbi.nlm.nih.gov/pubmed/35968535
http://dx.doi.org/10.1016/j.fochms.2022.100127
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