Berton M T, Webster R G
Virology. 1985 Jun;143(2):583-94. doi: 10.1016/0042-6822(85)90396-4.
We have probed the antigenic structure of the influenza B virus hemagglutinin (HA) with monoclonal antibodies specific for the HA of influenza B virus, B/Oregon/5/80. Seventeen laboratory-selected antigenic variants of this virus were analyzed by hemagglutination-inhibition (HI) assays or ELISA and an operational antigenic map was constructed. In addition, the monoclonal antibodies were tested in a competitive binding assay to construct a topological map of the antigenic sites. In contrast to the influenza A virus HA, only a single immunodominant antigenic site composed of several overlapping clusters of epitopes was defined by the HI-positive antibodies. Three variants could be distinguished from the parental virus with polyclonal antisera by HI and infectivity reduction assays suggesting that changes in this antigenic site may be sufficient to provide an epidemiological advantage to influenza B viruses in nature. In addition, two nonoverlapping epitopes of unknown biological significance were identified in the competitive binding analysis by two monoclonal antibodies with no HI activity and little or no neutralizing activity. We previously identified single amino acid substitutions in the HAs of the antigenic variants used in this study (M. T. Berton, C. W. Naeve, and R. G. Webster (1984), J. Virol. 52, 919-927). These changes occurred in regions of the molecule which, by amino acid sequence alignment, appeared to correspond to proposed antigenic sites A and B on the H3 HA of influenza A virus. Correlation with the antigenic map established in this report, however, demonstrates that the amino acid residues actually contribute to a single antigenic site on the influenza B virus HA and suggests significant differences in the antigenic structures of the influenza A and B virus HAs.
我们用针对乙型流感病毒B/Oregon/5/80血凝素（HA）的单克隆抗体探究了乙型流感病毒HA的抗原结构。通过血凝抑制（HI）试验或酶联免疫吸附测定（ELISA）分析了该病毒的17个实验室筛选的抗原变体，并构建了一个实用的抗原图谱。此外，在竞争结合试验中对单克隆抗体进行了检测，以构建抗原位点的拓扑图。与甲型流感病毒HA不同，HI阳性抗体仅确定了一个由几个重叠表位簇组成的单一免疫显性抗原位点。通过HI和感染力降低试验，用多克隆抗血清可将三个变体与亲代病毒区分开来，这表明该抗原位点的变化可能足以使乙型流感病毒在自然界中具有流行病学优势。此外，在竞争结合分析中，通过两种无HI活性且几乎没有或没有中和活性的单克隆抗体，鉴定出了两个生物学意义未知的非重叠表位。我们之前在本研究中使用的抗原变体的HA中鉴定出了单个氨基酸替换（M. T. 伯顿、C. W. 内夫和R. G. 韦伯斯特（1984年），《病毒学杂志》52卷，919 - 927页）。这些变化发生在分子区域，通过氨基酸序列比对，这些区域似乎对应于甲型流感病毒H3 HA上提议的抗原位点A和B。然而，与本报告中建立的抗原图谱相关分析表明，这些氨基酸残基实际上构成了乙型流感病毒HA上的一个单一抗原位点，并表明甲型和乙型流感病毒HA的抗原结构存在显著差异。
