Mutations of some critical amino acid residues in the hepatitis B virus surface antigen.
Amino acid substitutions at several positions in the surface antigen (HBsAg) of hepatitis B virus (HBV) in natural isolates and the products of recombinant DNA molecules have identified important residues for cross-reaction with specific antibodies (anti-HBs) and the induction of antibodies with certain serological specificities. In a further group of mutants described here, cysteine residues in a region believed to be significant of the a epitope have been changed to serines. Of the three adjacent cysteine residues at positions 137, 138 and 139, mutation of either of the flanking residues reduced cross-reactivity with polyclonal anti-HBs, while alteration of the central residue was relatively well-tolerated. Mutation of cysteine 149 to serine or of glycine 145 to arginine (imitating naturally occurring mutants), lysine, or glutamatic acid all led to loss of cross-reactivity with polyclonal antisera.
Bruce
S A
SA
Institute of Cell and Molecular Biology, University of Edinburgh, Scotland.
Murray
K
K
D000595:Amino Acid Sequence; D000596:Amino Acids; D004279:DNA, Viral; D006514:Hepatitis B Surface Antigens / Q000235:genetics*; D006515:Hepatitis B virus / Q000235:genetics*; D006801:Humans; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed
D000596:Amino Acids; D004279:DNA, Viral; D006514:Hepatitis B Surface Antigens