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</script>doi: 10.1159/000150410
pmid: 8666520
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.
Recombination, Genetic, Hepatitis B virus, Protein Folding, Hepatitis B Surface Antigens, Virus Assembly, Protein Structure, Secondary, Phenotype, Mutagenesis, Site-Directed, Point Mutation, Tetradecanoylphorbol Acetate, Amino Acid Sequence, Cysteine, Sequence Deletion
Recombination, Genetic, Hepatitis B virus, Protein Folding, Hepatitis B Surface Antigens, Virus Assembly, Protein Structure, Secondary, Phenotype, Mutagenesis, Site-Directed, Point Mutation, Tetradecanoylphorbol Acetate, Amino Acid Sequence, Cysteine, Sequence Deletion
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