1887

Abstract

To study the neutralizing epitopes of influenza B virus Yamagata group strains, two monoclonal antibodies (mAbs) were used to select escape mutants of the virus. mAbs 5H4 and 3A12 were found to react with B/Yamagata group strains in haemagglutination inhibition and neutralization tests; no reactivity with B/Victoria group strains was observed. Most of the mutants reacted poorly to polyclonal ferret antibody against the 1998 isolate. Analysis of the deduced amino acid sequences identified a single amino acid substitution at residue 141 (Gly→Arg) or 149 (Arg→Gly) in 5H4-escape mutants and 141 (Gly→Arg), 147 (Thr→Ile) or 148 (Ser→Gly) in 3A12-escape mutants. These residues are situated in close proximity in the ‘loop’ of the haemagglutinin molecule. These epitopes have been conserved in B/Yamagata group strains for almost 10 years in Japan but amino acid substitutions in the loop have been observed in clinical isolates only since 1999.

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2003-04-01
2020-11-24
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