IN SILICO PEPTIDE BASED VACCINE DESIGN AGAINST NON-STRUCTURAL PROTEIN 5 OF HEPATITIS C VIRUS
Objective: Hepatitis C virus (HCV) is the cause of hepatitis C in human. A hepatitis C infection does not show any noticeable symptoms in the very early stages of the infection, but a chronic infection can ultimately lead to cirrhosis. The chronic condition results in liver failure or cancer. Protein-Protein interactions play a vital role in the pathogenesis of any pathogen. Protein-Protein interactions maps designed and created in this research provide accurate and valuable resource for better understanding of the pathogenicity pathways of Hepatitis C Virus. The objective of the study was to predict the epitope against non-structural protein NS (5a) of Hepatitis C Virus which could be used as suitable vaccine candidate against Hepatitis C virus infections.
Methods: A specific protein-protein interaction is selected on the basis of its significance in the pathway leading to replication of Hepatitis C genome i. e. Interaction between Hepatitis C Nonstructural protein 5A (NS5A) with sh3 domain of Fyn tyrosine protein kinase. Epitopes was predicted and screened by using various bioinformatics tools. Each of the predicted structure was docked with MHC Class I and class II molecules using PatchDock and FireDock.
Results: The MVGLNSYRI epitope was selected on the basis of half life of dissociation and binding score. The average score of half-life of disassociation (t1/2) for MVGLNSYRI was 20 hrs, which is the greater than the other epitopes. Structure based modeling of epitopes was done and further the energy was optimized. Then after that the binding score was calculated, which was again best in case of MVGLNSYRI.
Conclusion: These findings conclude that the designed protein-protein interaction maps and predicted epitopes can be of great use in the wet laboratory formulations of vaccines against Hepatitis C Virus.
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