ArticleFrontiers in veterinary science2020
Identification of Allergic Epitopes of Soybean β-Conglycinin in Different Animal Species.
Article in Frontiers in veterinary science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 17 citations in OpenAlex.
- Targeted Reduction of Specific Antinutritional and Allergen-Associated Proteins to Advance Soybean Seed Quality.International journal of molecular sciences · 2026Article
- ImprovingJournal of agricultural and food chemistry · 2026Article
- A Quantity-Dependent Nonlinear Model of Sodium Cromoglycate Suppression on Beta-Conglycinin Transport.International journal of molecular sciences · 2024Article
- Integrated omics profiling of individual variations in intestinal damage to the soybean allergen in piglets.Frontiers in veterinary science · 2024Article
- Advanced applications of sustainable and biological nano-polymers in agricultural production.Frontiers in plant science · 2022Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Soybean can cause allergy in both humans and animals. The herein study aims to identify the antigenic determinants (epitopes) of β-conglycinin that lead to allergy in different animal species (swine, bovine, and rats). The epitopes of β-conglycinin were identified through co-immunoprecipitation and mass spectrometry. The binding abilities of seven identified epitope peptides to allergic sera of three animal species were compared by ELISA and dot-blot techniques. Some epitope peptides could be recognized by the three animal allergic sera, while most epitopes showed some differences in binding abilities to the different animal sera. The strongest reaction using swine sera was detected with peptides α2, β2, and β3, but the biggest sensitive regions for bovine and rats were peptides α2, β1, and β4. Most epitopes of β-conglycinin exhibited different binding abilities to the three animal sera, in which the biggest sensitive regions were peptides α2, β2, and β3 for swine, but peptides α2, β1, and β4 were detected for bovine and rats.
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