en تخصصي Special پژوهشي Original article <div style="border-bottom:solid windowtext 1.0pt; border-top:solid windowtext 1.0pt; border-left:none; border-right:none; padding:1.0pt 0in 1.0pt 0in"><span style="font-size:12pt"><span style="unicode-bidi:embed"><span new="" roman="" style="font-family:" times=""><b><span style="font-size:11.0pt">Background and Aims: </span></b><span style="font-size:11.0pt">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.</span></span></span></span><br> <span style="font-size:12pt"><span style="unicode-bidi:embed"><span new="" roman="" style="font-family:" times=""><b><span style="font-size:11.0pt">Materials and Methods: </span></b><span style="font-size:11.0pt">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.&nbsp; The percentage of substitutions, desired and stable residues for mutation in each position were indicated.</span></span></span></span><br> <span style="font-size:12pt"><span style="unicode-bidi:embed"><span new="" roman="" style="font-family:" times=""><b><span style="font-size:11.0pt">Results:</span></b><span style="font-size:11.0pt"> The integrated results exhibited bNAb epitope (residues 313-328) which is the most conserved epitope in E1 glycoprotein sequence among all genotypes of HCV.</span></span></span></span><br> <span style="font-size:12pt"><span style="unicode-bidi:embed"><span new="" roman="" style="font-family:" times=""><b><span style="font-size:11.0pt">Conclusion: </span></b><span style="font-size:11.0pt">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</span><span style="font-size:11.0pt">.</span></span></span></span></div> E1 envelope glycoprotein, Mutation, Epitope, Neutralization, Vaccine design 7 15 http://journal.isv.org.ir/browse.php?a_code=A-10-79-1&slc_lang=en&sid=1 Raziyeh Zareh-Khoshchehreh rzarehkh@gmail.com 10031947532846006555 10031947532846006555 No Department of Virology, Faculty of Medical Sciences, Tarbiat Modares University, Tehran, Iran. Taravat Bamdad BAMDAD_T@modares.ac.ir 10031947532846006556 10031947532846006556 Yes Department of Virology, Faculty of Medical Sciences, Tarbiat Modares University, Tehran, Iran. Seyed Shahriar Arab sh.arab@modares.ac.ir 10031947532846006557 10031947532846006557 No Department of Biophysics, Faculty of biological Sciences, Tarbiat Modares University-TMU, Tehran, Iran. Mahdi Behdani Behdani@pasteur.ac.ir 10031947532846006558 10031947532846006558 No Department of Biotechnology, Venom and Biotherapeutics Molecules Laboratory, Biotechnology Research Center, Pasteur Institute of Iran, Tehran, Iran. Mahmoud Biglar mbiglar@tums.ac.ir 10031947532846006559 10031947532846006559 No Department of Pharmacy, Drug design and development research center, Tehran University of Medical Sciences, Tehran, Iran.