Immunoreactivity of HCV/HBV epitopes displayed in an epitope-presenting system.
It has been demonstrated that the immunodominant region of the HCV core protein and the hepatitis B surface antigen (HBsAg) have high degree of reactivity. In order to construct a chimeric protein that carries HCV and HBV epitopes and possesses immunogenicity to both HCV and HBV, four epitopes derived from residues aa2-21 (epitope C1), aa22-40 (epitope C2) of the core protein, residues aa315-328 (epitope E) of E1 protein of HCV, and residues aa124-147 (epitope S) of HBsAg were chosen to be displayed in a conformation-specific manner on the outer surface of the Flock House virus capsid protein and expressed in E. coli cells. The reactivity of these epitopes with antisera from hepatitis C and hepatitis B patients and induction of immune response in guinea pigs were determined. The results showed that when displayed in this system, the chimeric protein carrying only epitope S could react with anti-HBsAg positive human sera, elicit an anti-HBsAg response in guinea pigs. The chimeric protein carrying epitopes C1, C2 and E could react with antibodies to different HCV genotypes, elicit an anti-HCV response in guinea pigs. The chimeric protein carrying epitopes C1, C2, E, and S could react with antibodies against HCV and HBV, elicit anti-HCV and anti-HBsAg responses in guinea pigs. The results suggested that these epitopes displayed in this form could be considered for development of epitope-based vaccines against HCV/HBV infections.
Chen
Yuanding
Y
Institute of Medical Biology, Chinese Academy of Medical Sciences and Peking Union Medical College, Kunming 650118, Yunnan, China. chenyd@imbcams.com.cn
Xiong
Xinyu
X
Liu
Xiao
X
Li
Jiaqi
J
Wen
Yuling
Y
Chen
Yuna
Y
Dai
Qing
Q
Cao
Zhiliang
Z
Yu
Wenlin
W
D000595:Amino Acid Sequence; D000818:Animals; D002213:Capsid / Q000737:chemistry / Q000276:immunology; D003429:Cross Reactions; D006168:Guinea Pigs; D016174:Hepacivirus / Q000235:genetics / Q000276:immunology*; D006510:Hepatitis B Antibodies / Q000096:biosynthesis / Q000276:immunology; D006514:Hepatitis B Surface Antigens / Q000737:chemistry / Q000235:genetics / Q000276:immunology*; D006515:Hepatitis B virus / Q000235:genetics / Q000276:immunology*; D018937:Hepatitis C Antibodies / Q000096:biosynthesis / Q000276:immunology; D018936:Hepatitis C Antigens / Q000737:chemistry / Q000235:genetics / Q000276:immunology*; D006801:Humans; D016056:Immunodominant Epitopes / Q000737:chemistry / Q000235:genetics / Q000276:immunology*; D007304:Insect Viruses / Q000235:genetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics / Q000276:immunology; D019151:Peptide Library; D011487:Protein Conformation; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000276:immunology; D014758:Viral Core Proteins / Q000737:chemistry / Q000235:genetics / Q000276:immunology*; D014759:Viral Envelope Proteins / Q000737:chemistry / Q000235:genetics / Q000276:immunology*
C087035:E1 protein, Hepatitis C virus; D006510:Hepatitis B Antibodies; D006514:Hepatitis B Surface Antigens; D018937:Hepatitis C Antibodies; D018936:Hepatitis C Antigens; D016056:Immunodominant Epitopes; D010446:Peptide Fragments; D019151:Peptide Library; D011993:Recombinant Fusion Proteins; D014758:Viral Core Proteins; D014759:Viral Envelope Proteins; C499352:core protein p22, Hepatitis C virus