Characterization of allergenic epitopes of Ory s1 protein from Oryza sativa and its homologs

Vaccination is the most effective technique suggested now days for allergy treatment. Recombinant-based approaches are mostly focused ongenetic modification of allergens to produce molecules with reduced allergenic activity and conserved antigenicity. The molecules developed forvaccination in allergy possess significantly reduced allergenicity in terms of IgE binding, and therefore will not lead to anaphylactic reactionsupon injection. This approach is probably feasible with every peptide allergen with known amino acid sequence. In this study an in silicoapproach was used to investigate allergenic protein sequences. Motif analysis of these sequences reveals the allergenic epitopes in the amino acidsequences. Physicochemical analysis of protein sequences shows that the homolog allergens of Ory s1 are highly correlated with the aromaticity,GRAVY and cysteine content. Moreover, phylogenetic analysis of Ory s1 with other sequences reveals that Oryza sativa japonica and Zea maysare close homologs, whilst Lolium perenne and Dactylis glomerata are found to be remote homologs. The multiple sequence alignment reveals ofOry s1 with all its homologs in this study reveals the high conservation of residues in DPBB_1 domain (amino acid residue positions 86- 164)and was found distinctly in all the sequences. These findings support the proposal that allergenic epitopes encompass conserved residues. Theconsensus allergenic was found to be mainly composed of hydrophobic residues. The functional sites of allergenic proteins reported in this studyshall be attenuated to develop hypoallergenic vaccine. The sequence comparison strategy adopted in this study would pave way effectiveevolutionary analysis of these allergens.