Prediction and characterization of the T cell epitopes for the major
soybean protein allergens using bioinformatics approaches
Protein allergens is a health risk for consumption of soybeans. To
understand allerginicity mechanism, T cell epitopes of 7 soybean
allergens were predicted and screened by abilities to induce cytokine
interleukin 4. The relationships among amino acid composition,
properties, allergenicity and pepsin hydrolysis sites were analyzed.
Among the 138 T cell epitopes identified, YIKDVFRVIPSEVLS,
KDVFRVIPSEVLSNS, DVFRVIPSEVLSNSY of Gly m 6.0501 (P04347), and
AKADALFKAIEAYLL, ADALFKAIEAYLLAH of Gly m 4.0101 (P26987) were the most
possible epitope candidates. In T cell epitopes pattern, the frequencies
of amino acids Q, D, E, P and G decreased, while F, I, N, V, K and H
increased. Hydrophobic residues at positions p1 and p2 and positively
charged residues in positions p13 might contribute to allergenicity.
Most of epitopes could be hydrolyzed by pepsin into small polypeptides
within 12 residues length, and the anti-digestive epitope regions
contained I, V, S, N, and Q residues. T cell epitopes EEQRQQEGVIVELSK
from Gly m 5.03 (P25974) showed resistantence to pepsin hydrolysis and
would cause a higher Th2 cell response. This research provides basis for
the development of hypoallergenic soybean products in the soybean
industry as well as for the immunotherapy design for protein allergy.