Abstract: Recently, there has been widespread concern about peanut allergy because of the high sensitization rate to peanut and peanut-induced anaphylaxis. Ara h 1 is a major allergen in peanut that belongs to the Cupin superfamily and can trigger peanut allergies through recognizing and binding to immunoglobulin E (IgE). In this study, bioinformatics was used to analyze the amino acid composition of the linear B cell epitope on peanut allergen Ara h 1 and its correlation with the secondary and tertiary structures of the allergen. The digestion resistant peptides in the Ara h 1 sequence were analyzed by mass spectrometry (MS), and the relationship between the peptides and the predicted linear B cell epitopes was analyzed. The results showed that the linear B cell epitope on Ara h 1 was rich in hydrophilic and charged amino acids. In the secondary structure, the epitope showed no regular distribution pattern but with tuning and folding conformations. In the tertiary structure, it was mainly located in the hydrophobic interaction area between the monomers, partly buried in the trimer conformation. There was a partial overlap between the digestion resistant peptide sequence and the predicted epitope. Detecting peptides from simulated gastrointestinal digestion in vitro by MS combined with bioinformatics analysis can be used as a new method to identify the linear B cell epitope on the Cupin superfamily.

Key words: peanut allergy; Ara h 1; linear B cell epitope; digestion resistant peptide; bioinformatics analysis