Nakagawa Naoko, Kubota Ritsuko, Nakagawa Toshimasa, Okuno Yoshinobu
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.
J Gen Virol. 2001 Sep;82(Pt 9):2169-2172. doi: 10.1099/0022-1317-82-9-2169.
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 (Asn-->Ser or Thr) or 203 (Lys-->Thr or Asn). A single amino acid substitution at residue 241 (Pro-->Ser) 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.
为研究乙型流感病毒维多利亚系毒株的中和表位，使用两种单克隆抗体（MAb）筛选该病毒的抗原变异体。在过氧化物酶-抗过氧化物酶染色、血凝抑制及中和试验这三项检测中，发现单克隆抗体10B8和8E6可与B/维多利亚系毒株发生反应；未观察到其与B/山形系毒株的反应性。对10B8诱导的变异体推导氨基酸序列的分析确定，在第165或170位残基处有一个氨基酸缺失，以及在第164位（天冬氨酸→酪氨酸）、165位（天冬酰胺→丝氨酸或苏氨酸）或203位（赖氨酸→苏氨酸或天冬酰胺）有一个氨基酸替换。在8E6诱导的变异体中观察到第241位残基（脯氨酸→丝氨酸）有一个氨基酸替换。三维分析表明，两种单克隆抗体的表位彼此紧邻。由于B/山形系毒株的特征是在第164 - 166位残基处有氨基酸缺失，单克隆抗体10B8的表位对B/维多利亚系毒株具有严格的特异性。
