title: Mutational analysis of HBsAg assembly.
abstract: The 20-nm noninfectious empty envelope particles carrying the hepatitis B surface antigen are secreted in large excess from hepatocytes during a hepatitis B infection. Similar particles produced in cell lines or yeast are an efficient vaccine against hepatitis B virus. We have analyzed the assembly of 20-nm particles using a mutagenesis approach. Specific mutations were introduced into the S gene and the preS region encoding the viral envelope proteins using recombinant DNA techniques. The mutant genes were expressed in cell lines to identify the amino acid residues that are critical for the assembly and the secretion of the 20-nm particles.
authors.affiliation: Institute of Medical Microbiology, University of Mainz, Germany.
authors.forename: R
authors.initials: R
authors.lastname: Prange
authors.forename: C M
authors.initials: CM
authors.lastname: Mangold
authors.forename: R
authors.initials: R
authors.lastname: Hilfrich
authors.forename: R E
authors.initials: RE
authors.lastname: Streeck
mesh_terms: D000595:Amino Acid Sequence; D003545:Cysteine / Q000502:physiology; D006514:Hepatitis B Surface Antigens / Q000737:chemistry / Q000235:genetics*; D006515:Hepatitis B virus / Q000737:chemistry* / Q000235:genetics; D016297:Mutagenesis, Site-Directed; D010641:Phenotype; D017354:Point Mutation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011995:Recombination, Genetic; D017384:Sequence Deletion; D013755:Tetradecanoylphorbol Acetate / Q000378:metabolism; D019065:Virus Assembly
chemical_list: D006514:Hepatitis B Surface Antigens; D003545:Cysteine; D013755:Tetradecanoylphorbol Acetate