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Protein Sequence Analysis of E1 Surface Glycoprotein in Hepatitis C Virus
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Raziyeh Zareh-Khoshchehreh   , Taravat Bamdad *  , Seyed Shahriar Arab , Mahdi Behdani , Mahmoud Biglar |
| Department of Virology, Faculty of Medical Sciences, Tarbiat Modares University, Tehran, Iran. |
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Abstract: (1477 Views) |
Background and Aims: Hepatitis C Virus infects more than 170 million people globally despite highly effective direct acting antiviral drugs that greatly improved treatment. The Hepatitis C virus envelope glycoproteins E1 and E2 are the major target to induce immune responses. Since, the different aspects of E1 such as its function and structure are still discussed and require further study, in current study critical regions of E1 were evaluated.
Materials and Methods: Mutation diversity in these areas was determined using strains that were available in online databanks and authentic software. Furthermore, RT-PCR for E1 was done on HCV-1a positive samples and the sequences were analyzed. The percentage of substitutions, desired and stable residues for mutation in each position were indicated.
Results: The integrated results exhibited bNAb epitope (residues 313-328) which is the most conserved epitope in E1 glycoprotein sequence among all genotypes of HCV.
Conclusion: These kinds of studies may shed light on identification more binding sites of virus and broadly cross-neutralization of antibodies. Moreover, it may facilitate the modeling of peptides to new antiviral design or boosting the immune response in multi-epitope vaccine studies. |
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| Keywords: E1 envelope glycoprotein, Mutation, Epitope, Neutralization, Vaccine design |
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Full-Text [PDF 512 kb]
(480 Downloads)
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Type of Study: Original article |
Subject:
Special
Received: 2021/11/12 | Accepted: 2022/01/11 | Published: 2022/06/20
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