摘要
Many studies have provided evidence that core antigen of hepatitis B virus (HBcAg) is extremely immunogenic, HBcAg can be function as both a T-cell-dependent antigen and a T-cell-independent antigen, and thus may be a promising candidate for therapeutic vaccine for control of chronic HBV infection. HBcAg is also an effective carrier for heterologous peptide epitopes. The preS1 is a surface protein of HBV and is immunogenic at the T and B cell level. The amino acid sequence 21–47 of preS1 is crucial for HBV binding to human hepatocytes as well as to PBMC and haematopoietic cell lines of the B cell lineage. Here we expressed a chimeric protein named HBVCS1, created by fusing the preS1 sequence 3–55 to the carboxyl terminus of the truncated HBcAg sequence 1–155 in E. coli. Analysis of its antigenicity and immunogenicity revealed that both HBc and preS1 epitopes are surface accessible, and that fusion of preS1 did not affect the HBc antigenicity and immunogenicity of the truncated HBc sequence. HBVCS1 induced strong anti-HBc and moderate anti-preS1 immune responses as well specific T-cell response in Balb/c mice. HBVCS1 vaccination reduced of the titer of HBsAg and HBV DNA in sera of HBV-Tg mice. These results indicate that HBVCS1 may have potential as a therapeutic vaccine for treatment of HBV chronic infection.