Recombinant Hepatitis C Virus E2 Genotype-1 produced in E. coli is a single polypeptide chain containing 226 amino acids (aa 482-671) and having a molecular mass of 25.4kDa (NCBI Accession#NP_671491).
HCV E2 is fused to a 36 amino acid His-tag at N-terminus.
HCV belongs to the Flaviviridae family and has a single-stranded positive-sense RNA genome. This genome encodes a single polyprotein, which is processed into at least 11 polypeptides, including three structural proteins (core, and envelope proteins E1 and E2), a small polypeptide named p7, the novel F protein, and six nonstructural (NS) proteins (NS2, NS3, NS4A, NS4B, NS5A, and NS5B) .
The E2 glycoprotein is one of the key structural proteins of HCV and plays a crucial role in the virus’s ability to infect host cells. It is the major target for neutralizing antibodies (NAbs), making it a critical focus for vaccine development . The E2 protein forms heterodimers with the E1 protein on the viral surface, facilitating the virus’s entry into host cells .
Recombinant E2 protein is produced using genetic engineering techniques to express the E2 glycoprotein in various host systems. This recombinant protein is used in research to study the immune response to HCV and to develop vaccines and therapeutic agents. The recombinant E2 protein can elicit broad neutralizing antibodies, making it a promising candidate for vaccine development .
Developing an effective HCV vaccine is challenging due to the high diversity across HCV genotypes. However, recombinant E2 proteins have shown potential in eliciting pangenotypic neutralizing antibodies, which can target multiple HCV genotypes . Recent studies have focused on optimizing the E2 protein to enhance its immunogenicity and efficacy in vaccine formulations .