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Short Communication |
1 Department of Parasitic Agents, Kobe Institute of Health, 4-6, Minatojima-nakamachi, Chuo-ku, Kobe 650-0046, Japan
2 Division of Virology, Department of Public Health, Osaka Prefectural Institute of Public Health, 3-69, 1-Chome, Nakamichi, Higashinari-ku, Osaka 537-0025, Japan
3 Department of Clinical Pathology, Osaka Medical College, 2-7 Daigaku-cho, Takatsuki 569-8686, Japan
Correspondence
Naoko Nakagawa
nknkgw{at}h2.dion.ne.jp
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.
DDBJ accession numbers of the nucleotide sequences reported in this paper are as follows: AB036446 for B/Kadoma/122/1999; AB036451 for B/Kadoma/506/1999; AB045009 for B/Kadoma/409/2000; AB071521for B/Kobe/69/2001-clone 1; AB083404 for B/Kobe/5/2002; AB083405 for B/Kobe/69/2001-clone 1-variant 1; AB036452 and AB036453 for B/Kadoma/122/1999-V1 and -V2; AB071525 to -33 for B/Kadoma/122/1999-V3 to -V11.
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