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Problem statement: Recombinant-based approaches are mostly focused &#13; on genetic modification of allergens to produce molecules with reduced allergenic &#13; activity and conserved antigenicity, such as hypoallergens. Recombinant allergens &#13; represent promising tools for diagnosis and therapy of type I allergy. This approach &#13; was probably feasible with every allergen with known amino acid sequence. Approach: &#13; The primary aim of this study was to determine the consensus epitope &#13; from twenty homologous protein sequences of Ory S1 allergenic protein sequence &#13; from Oryza sativa (indica group) pollen. Molecular modeling calculations had been &#13; used to investigate the allergenic protein models for the epitope. Results: &#13; Oryza sativa (japonica), Phleum pratense, Poa pratensis, Holcus lanatus, &#13; Lolium perenne, Triticum aestivum, Dactylis glomerata and Zea mays were found &#13; more closely related (alignment score 1145-812) among all the homologs and investigated &#13; further. The major binding pocket comprised an area of 604.5 Å2 and 970 &#13; Å3 volume and another key binding pocket had 425.6 Å² area and &#13; 658.8 Å³ volume. The residues found in the key site included ile2, &#13; lys13, cys14, ser15, lys16, pro17, ala25, leu26, ile27, tyr40, his41, phe42, asp43, &#13; leu44, ser45, gly46, leu47, ala48, met49, ala50, asp55, leu58, arg59, ala61, gly62, &#13; ile63, ile64, asp65, gln67, phe68; corresponding to the allergen binding site &#13; and the IgE binding epitope given in the title. Conclusion: These &#13; are the functional sites on the allergenic proteins that can be mutated to develop &#13; hypoallergenic vaccine. These sites can be rationalized on the basis of simple &#13; arguments that lead to vaccine development, by predicting the structure of the &#13; allergenic epitopes and comparative analysis

Target Identification in Ory S1 Pollen Protein Allergen from Oryza sativa in the Course of Construction of Hypoallergenic Vaccines