title: Inhibition of hepatitis B virus assembly with synthetic peptides derived from the viral surface and core antigens.
abstract: 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.
authors.affiliation: Department of Biochemistry and Microbiology, Faculty of Science and Environmental Studies, Universiti Putra Malaysia, UPM 43400, Serdang, Selangor, Malaysia. wstan@fsas.upm.edu.my
authors.forename: Wen Siang
authors.initials: WS
authors.lastname: Tan
mesh_terms: 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
chemical_list: D006512:Hepatitis B Core Antigens; D006514:Hepatitis B Surface Antigens; D010446:Peptide Fragments