Quantitative Immunoproteomics Approach for the Development of MHC Class I Associated Peptide Antigens of Alpha-Cobra Toxin from Naja kaouthiaSherkhane AS, Changbhale SS and Gomase VS*
The Global Open University, Nagaland, India
- Corresponding Author:
- Virendra S Gomase
The Global Open University
E-mail: [email protected]
Received date: October 30, 2014; Accepted date: November 25, 2014; Published date: December 03, 2014
Citation: Sherkhane AS, Changbhale SS, Gomase VS (2014) Quantitative Immunoproteomics Approach for the Development of MHC Class I Associated Peptide Antigens of Alpha-Cobra Toxin from Naja kaouthia. J Biotechnol Biomater 4:169. doi:10.4172/2155-952X.1000169
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.
Alpha-Cobratoxin from N. kaouthia binds to acetylcholine receptors which are located in neuromuscular junctions, once activated; they cause contract muscles and block their actions thereby bringing on muscle paralysis. Peptide fragments of Alpha-Cobratoxin from N. kaouthia having 71 amino acids, which shows 63 nonamers and are used synthetic peptide vaccine design and to increase the understanding of roles of the immune system against snake bite. For the immune responses against a protein antigen, it is clear that the whole protein is not necessary for raising the immune response, but small segments (15-PNGHVCYTKT-24, 26-CDAFCSIRG-34 and 36-RVDLGCAATCPTVKTGVDIQCCSTD-60) of Alpha-Cobratoxin protein from N. kaouthia called the antigenic determinants or the epitopes are sufficient for eliciting the desired immune response. The identification of specific peptides that binds to MHC class I molecules is important to recognize T-cell epitopes. In this research work, we predict antigenicity, Solvent accessibility to identify the membrane-spanning regions (hydrophobic) or regions that are likely exposed on the surface of proteins (hydrophilic domains) which are potentially antigenic that are used to design synthetic peptide vaccine.