Expression, Purification and Immunogenic Description of a Hepatitis C Virus Recombinant CoreE1E2 Protein Expressed by Yeast Pichia pastoris.

Gradual development of a useful vaccine can be the main point in the control and eradication of Hepatitis C virus (HCV) infection. Hepatitis C Virus envelope glycoproteins are considered as the main HCV vaccine candidate. In this study, the Pichia pastoris expression system was used to express a recombinant HCV CoreE1E2 protein, which consists of Core (269 nt-841nt) E1 (842 nt-1417nt) and E2 (1418 nt-2506nt). By a codon optimization technique based on the P. pastoris expression system, we could increase the rate of recombinant proteins. Moreover, the purified protein can efficiently induce anti-CoreE1E2 antibodies in rabbits, and also by developing a homemade Enzyme-Linked ELISA kit we can detect antibody of HCV Iranian patients with genotype 1a. In our study, the virus-like particle of rCoreE1E2 with 70 nm size, was shown by Electron microscopy and proved the self-assembly in vitro in a yeast expression system. These findings of the present study indicate that the recombinant CoreE1E2 glycoprotein is effective in inducing neutralizing antibodies, and is an influential HCV vaccine candidate.