alexa Identification of Antigenic Determinants, Solvent Accessibility and MHC Binders of Peb1a from Campylobacter jejuni | OMICS International
ISSN: 2155-9597

Journal of Bacteriology & Parasitology
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Research Article

Identification of Antigenic Determinants, Solvent Accessibility and MHC Binders of Peb1a from Campylobacter jejuni

Sherkhane AS1, Waghmare Somnath2 and Gomase VS3*

1The Global Open University, Nagaland, India

2Department of Zoology, Nowrosjee Wadia College of Arts and Science, Pune, India

3Department of Computer Science and IT, Dr. Babasaheb Ambedkar Marathwada University, Aurangabad, India

*Corresponding Author:
Gomase VS
Department of Computer Science and IT
Dr. Babasaheb Ambedkar Marathwada University
Aurangabad, India
Tel: 91- 9987770696
E-mail: [email protected]

Received date: June 2, 2014; Accepted date: July 21, 2014; Published date: July 24, 2014

Citation: Sherkhane AS, Somnath W, Gomase VS (2014) Identification of Antigenic Determinants, Solvent Accessibility and MHC Binders of Peb1a from Campylobacter jejuni. J Bacteriol Parasitol 5:1000193. doi: 10.4172/2155-9597.1000193

Copyright: © 2014 Sherkhane AS, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Abstract

Campylobacter jejuni is a foodborne, highly mutable in response to antibiotic, pathogen causing gastroenteritis in humans. In this study we summarize the potency of Peb1a from Campylobacter jejuni with 259 amino acids. Antigenic peptides of Peb1a from Campylobacter jejuni are most suitable for subunit vaccine development because with single epitope, the immune response can be generated in large population. In this research, we used PSSM and SVM algorithms for the prediction of MHC class I & II binding peptide, antigenicity, Solvent accessibility, polar and nonpolar residue to analyses the regions that are likely exposed on the surface of proteins which are potentially antigenic that allows potential drug targets to identify active sites against infection as well as to design effective drug to treat it.

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