THE ANTIGENIC STRUCTURE OF THE INFLUENZA-B VIRUS HEMAGGLUTININ - OPERATIONAL AND TOPOLOGICAL MAPPING WITH MONOCLONAL-ANTIBODIES
THE ANTIGENIC STRUCTURE OF THE INFLUENZA-B VIRUS HEMAGGLUTININ - OPERATIONAL AND TOPOLOGICAL MAPPING WITH MONOCLONAL-ANTIBODIES
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DOI：
10.1016/0042-6822(85)90396-4
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发表时间：
1985-01-01
期刊：
影响因子：
3.7
通讯作者：
WEBSTER, RG
中科院分区：
文献类型：
--
作者：
BERTON, MT;WEBSTER, RG
用特异于B型流感病毒HA的单克隆抗体（B/俄勒冈州/5/80）探测B型流感病毒血凝素（HA）的抗原结构。用ELISA的血凝抑制（HI）试验分析了该病毒的17个实验室选择的抗原变异，并构建了可操作的抗原图谱。在竞争性结合测定中测试单克隆抗体以构建抗原位点的拓扑图。与甲型流感病毒HA相反，HI阳性抗体仅定义了由几个重叠的表位簇组成的单个免疫显性抗原位点。通过HI和感染性降低试验，可以用多克隆抗血清将三种变体与亲本病毒区分开来，这表明该抗原位点的变化可能足以为自然界中的流感B病毒提供流行病学优势。在竞争性结合分析中，通过2个单克隆抗体鉴定了两个生物学意义未知的非重叠表位，这些单克隆抗体没有HI活性和很少或没有中和活性。先前鉴定了本研究中使用的抗原变体的HA中的单个氨基酸取代。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上的拟议抗原位点A和B。与本报告中建立的抗原图谱的相关性表明，这些氨基酸残基实际上促成了B型流感病毒HA上的单个抗原位点，并表明甲型流感病毒和B型流感病毒HA的抗原结构存在显著差异。
The antigenic structure of the influenza B virus hemagglutinin (HA) was probed 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 of ELISA was probed and an operational antigenic map was constructed. 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. Two nonoverlapping epitopes of unknown biological significance were identified in the competitive binding analysis by 2 monoclonal antibodies with no HI activity and little or no neutralizing activity. Single amino acid substitutions in the HA of the antigenic variants used in this study were previously identified. 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 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 HA.