Identification of MHC Class, Transports Antigenic Peptides from Naja melanoleuca Long Neurotoxin 1

Sherkhane As Changbhale Ss

doi:10.4172/2157-7609.1000169

Abstract

Long neurotoxin 1 is a dangerous protein occurs in N. melanoleuca. It is highly dangerous snake due to the quantity of venom inject in a single bite. Peptide fragments of N. Melanoleuca Long neurotoxin 1 antigen protein having 71 amino acids, which shows 63 nanomers can be used to select nanomers for use in synthetic peptide vaccine design and to increase the understanding of roles of the immune system against snake bite. We use to apply computational intelligence algorithm PSSM (Position Specific Scoring Matrices) for the Prediction of MHC class-I binding peptides, we also predict antigenicity, Solvent accessibility, polar and nonpolar residue to analyses the membrane-spanning regions (hydrophobic) or regions that are likely exposed on the surface of proteins (hydrophilic domains) that are potentially antigenic that allows potential drug targets to identify active sites, for protection of host form Snake bites and to design synthetic peptide vaccine.

Highlights

Naja melanoleuca is the largest in all the true cobra (Naja) species in the world [1,2]
The Hopp-Woods scale Hydrophilicity Prediction Result Data was found to be high in position 4-5,8(1.014),910,16-18 in a protein, assuming that the antigenic determinants would be exposed on the surface of the protein and would be located in hydrophilic regions (Figure 1)
The hydrophobicity and hydrophilic characteristics of amino acids is determined by using different scales that are rich in charged and polar residues i.e. Sweet et al [32] hydrophobicity prediction Result Data found high in position 23-24,39-41(0.367), Kyte

Summary

Introduction

Naja melanoleuca (forest cobra, black cobra) is the largest in all the true cobra (Naja) species in the world [1,2]. N. melanoleuca Long neurotoxin 1 antigenic peptides are most suitable for antigenic peptide vaccine development because an ample immune response can be generated even with single epitope. MHC class I molecules present peptides from intracellular proteins, which are targeted by proteasome, cleaved them into short peptides of 8-11 amino acids in length. The second and the C-terminal position of the peptide are the most important for binding [10,11] These amino acids at each position contribute a certain binding energy [12]. These predicted MHC-binding peptides and T-cell epitopes helps improve our understanding of specificity of immune responses [13,14,15]

Methods

Results

Discussion

Conclusion