Mutations of some critical amino acid residues in the hepatitis B virus surface antigen

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Abstract
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.