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Title

 

 

 

 

 

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

 

Authors

 

Ruchi Sharma 1, *, A. K. Singh 1 and V. Umashankar 2

 

Affiliation

 

1Department of Botany, Udaya Pratap College, Varanasi, Uttar Pradesh, India; 2Department of Bioinformatics, School of Biosciences, SRM University, Ramapuram, Chennai, Tamil Nadu, India

 

Email

 

ruchivns@rediffmail.com

Article Type

 

Hypothesis

Date

 

Received March 16, 2009; Revised May 04, 2009; Accepted June 17, 2009; Published August 18, 2009

 

Abstract

Vaccination is the most effective technique suggested now days for allergy treatment. Recombinant-based approaches are mostly focused on genetic modification of allergens to produce molecules with reduced allergenic activity and conserved antigenicity. The molecules developed for vaccination in allergy possess significantly reduced allergenicity in terms of IgE binding, and therefore will not lead to anaphylactic reactions upon injection. This approach is probably feasible with every peptide allergen with known amino acid sequence. In this study an in silico approach was used to investigate allergenic protein sequences. Motif analysis of these sequences reveals the allergenic epitopes in the amino acid sequences. 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 mays are close homologs, whilst Lolium perenne and Dactylis glomerata are found to be remote homologs. The multiple sequence alignment reveals of Ory 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. The consensus allergenic was found to be mainly composed of hydrophobic residues. The functional sites of allergenic proteins reported in this study shall be attenuated to develop hypoallergenic vaccine. The sequence comparison strategy adopted in this study would pave way effective evolutionary analysis of these allergens.

 

Keywords

 

Ory s1, sequence analysis, physicochemical analysis, allergenic epitopes, phylogenetic analysis

Citation

 

Sharma et al, Bioinformation 4(1): 12-18 (2009)

Edited by

 

P. Kangueane

 

ISSN

 

0973-2063

 

Publisher

 

Biomedical Informatics

License

 

 

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.