expression, purification and immunogenic description of a hepatitis c virus recombinant coree1e2 protein expressed by yeast pichia pastoris

background: 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. objectives: 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). materials and methods: 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. results: 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. conclusions: 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.