Protein Expression and Purification, Vol.50, No.1, 43-48, 2006
Preparation of hepatitis C virus structural and non-structural protein fragments and studies of their immunogenicity
Plasmids pQE-60 and pQE-30 containing 6x His-tag sequence were used for expression of fragments of HCV structural and nonstructural proteins in Escherichia coli (E. coli). The following fragments were used: core (1-98 aa), NS3 (202-482 aa), and tetramer of hypervariable region 1 (HVR1) of E2 protein. The constructed plasmids directed high levels of expression of HCV proteins in E. coli JM109. After purification by the metal-affinity chromatography on nickel nitrilotriacetic acid (Ni-NTA) agarose, the His-tagged HCV proteins were used for immunization of BALB/c mice. All three proteins were able to induce high levels of specific antibodies and, in the case of the NS3 and HVR1 tetramer, also to mount vigorous cell-proliferating responses. High immunogenicity of the tested fragments of HCV proteins shows them as good candidates for inclusion into the future HCV vaccine preparations. (c) 2006 Elsevier Inc. All rights reserved.