Abstract

Naja naja is a highly poisonous snake species of cobra in Elapidae family and is commonly found in middle Asia. Long neurotoxin 3 from Naja naja binds to the nicotinic acetylcholine receptors in the postsynaptic membrane, preventing the binding of acetylcholine and blocks excitation of muscles. Antigenic peptides are complex biomolecules that have unique chemical and physical properties resulting of their amino acid composition. In this study, we have predicted the binding affinity of Long neurotoxin 3 from Naja naja having 71 amino acids, which shows 63 nonamers. Peptide fragments of the neurotoxin can be used to select nonamers for use in synthetic peptide vaccine design and to increase the understanding of roles of the immune system in neurotoxin studies. Antigenic peptides of Long neurotoxin 3 from Naja naja are most suitable for synthetic peptide vaccine development because with Small segment' 15-PNGHVCYTKT-24, 26-CDAFCSIRG-34, 36- RVDLGCAATCPTVKTGVDIQCCSTD-60 called the antigenic epitopes is sufficient for eliciting the desired immune response. In this research, we predict of MHC class I and II binding peptide because MHC molecules are cell surface proteins which take active part in immune response, antigenicity, Solvent accessibility, polar and nonpolar residue that are likely exposed on the surface of proteins that are potentially antigenic that allows to design synthetic peptide vaccine.

Highlights

  • Naja naja is one of the most venomous snake species occurs in wild forest and in cultivated areas [1,2]

  • Long neurotoxin 3 from Naja naja contain a long residue with 71 amino acids

  • Prediction of antigenic peptides In this study, we found the antigenic determinants by finding the area of greatest local hydrophilicity

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Summary

Introduction

Naja naja is one of the most venomous snake species occurs in wild forest and in cultivated areas [1,2]. Naja naja’s venom mainly contains a powerful postsynaptic neurotoxin [5]. Major histocompatibility complex (MHC) molecules are cell surface proteins that binds to the peptides derived from host or antigenic proteins and present them at the cell surface for recognition by T-cells [9,10]. MHC class I molecules present peptides from intracellular proteins that are targeted by proteasome, cleaved them into short peptides of 8-11 amino acids in length. These peptides are bound by the transmembrane peptide transporter (TAP) and translocate them from cytoplasm to endoplasmic reticulum, where they are bound by MHC molecule. MHC class II molecule present peptides derived from endocytosed extracellular proteins.

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