Inhibition of hepatitis B virus assembly with synthetic peptides derived from the viral surface and core antigens.
The long surface antigen (L-HBsAg) of hepatitis B virus (HBV) plays a central role in the production of infectious virions. During HBV morphogenesis, both the PreS and S domains of L-HBsAg form docking sites for the viral nucleocapsids. Thus, a compound that disrupts the interaction between the L-HBsAg and nucleocapsids could serve as a therapeutic agent against the virus based upon inhibition of morphogenesis. Synthetic peptides correspond to the binding sites in L-HBsAg inhibited the association of L-HBsAg with core antigen (HBcAg). A synthetic peptide carrying the epitope for a monoclonal antibody to the PreS1 domain competed weakly with L-HBsAg for HBcAg, but peptides corresponding to a linear sequence at the tip of the nucleocapsid spike did not, showing that the competing peptide does not resemble the tip of the spike.
Tan
Wen Siang
WS
Department of Biochemistry and Microbiology, Faculty of Science and Environmental Studies, Universiti Putra Malaysia, UPM 43400, Serdang, Selangor, Malaysia. wstan@fsas.upm.edu.my
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D004591:Electrophoresis, Polyacrylamide Gel; D006512:Hepatitis B Core Antigens / Q000378:metabolism / Q000494:pharmacology*; D006514:Hepatitis B Surface Antigens / Q000378:metabolism / Q000494:pharmacology*; D006515:Hepatitis B virus / Q000187:drug effects* / Q000502:physiology; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000494:pharmacology*; D011485:Protein Binding; D011817:Rabbits; D014771:Virion / Q000502:physiology; D019065:Virus Assembly / Q000187:drug effects / Q000502:physiology
D006512:Hepatitis B Core Antigens; D006514:Hepatitis B Surface Antigens; D010446:Peptide Fragments