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Animal: RNA Viruses |
Division of Virology, Department Public Health, Osaka Prefectural Institute of Public Health, 3-69 1-Chome, Nakamichi, Higashinari-ku, Osaka 537-0025, Japan1
Department of Clinical Pathology, Osaka Medical College, 2-7 Daigaku-cho, Takatsuki 569-8686, Japan2
Author for correspondence: Naoko Nakagawa. Present address: Department of Parasitic Agents, Kobe Institute of Health, 4-6 Minatojima-nakamachi, Chuo-ku, Kobe 650-0046, Japan. Fax +81 78 302 0894. e-mail kih-info-1{at}mse.biglobe.ne.jp
To study the neutralizing epitopes of influenza B virus Victoria group strains, two monoclonal antibodies (MAbs) were used to select antigenic variants of the virus. MAbs 10B8 and 8E6 were found to react with B/Victoria group strains in three tests, peroxidase–antiperoxidase staining, haemagglutination inhibition and neutralization tests; no reactivity with B/Yamagata group strains was observed. Analysis of the deduced amino acid sequences of 10B8-induced variants identified a single amino acid deletion at residue 165 or 170, as well as a single amino acid substitution at residues 164 (Asp
Tyr), 165 (AsnSer or Thr) or 203 (LysThr or Asn). A single amino acid substitution at residue 241 (ProSer) was observed in 8E6-induced variants. Three-dimensional analysis showed that the epitopes for both MAbs were situated in close proximity to each other. Since B/Yamagata group strains are characterized by amino acid deletions at residues 164–166, the epitope for MAb 10B8 is strictly specific for B/Victoria group strains.
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