ANALYSES OF THE ANTIGENICITY OF INFLUENZA HEMAGGLUTININ AT THE PH OPTIMUM FOR VIRUS-MEDIATED MEMBRANE-FUSION
ANALYSES OF THE ANTIGENICITY OF INFLUENZA HEMAGGLUTININ AT THE PH OPTIMUM FOR VIRUS-MEDIATED MEMBRANE-FUSION
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DOI：
10.1099/0022-1317-64-8-1657
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发表时间：
1983-01-01
影响因子：
3.8
通讯作者：
WILEY, DC
中科院分区：
文献类型：
--
作者：
DANIELS, RS;DOUGLAS, AR;WILEY, DC
在膜融合的最佳pH下，与融合活性有关的流感病毒膜的血凝素糖蛋白（HA）经历构象变化。通过使HA分子与具有确定特异性的小鼠单克隆抗体反应，分析了这种变化对HA抗原性的影响。结果表明，抗原性的特异性变化发生在抗原位点B和D，并解释在分子的三维结构和低pH孵育对其的影响。这些结果还提供了证据的抗原性意义的氨基酸序列的变化在站点B的HA的天然分离物，并允许明确划定该网站分为两个区域。
At the pH optimum for membrane fusion the hemagglutinin glycoprotein (HA) of the influenza virus membrane which is implicated in the fusion activity undergoes a conformational change. The effects of this change on the antigenicity of the HA were analyzed by reacting the molecule with mouse monoclonal antibodies of defined specificity. The results obtained indicate that specific changes in antigenicity occur in antigenic sites B and D and are interpreted in terms of the 3-dimensional structure of the molecule and the effects of low pH incubation on it. The results also provide evidence for the antigenic significance of amino acid sequence changes in site B of the HA of natural isolates and allow clear delineation of this site into two regions.