CHANGES IN THE CONFORMATION OF INFLUENZA-VIRUS HEMAGGLUTININ AT THE PH OPTIMUM OF VIRUS-MEDIATED MEMBRANE-FUSION
CHANGES IN THE CONFORMATION OF INFLUENZA-VIRUS HEMAGGLUTININ AT THE PH OPTIMUM OF VIRUS-MEDIATED MEMBRANE-FUSION
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DOI：
10.1073/pnas.79.4.968
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发表时间：
1982-01-01
期刊：
影响因子：
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通讯作者：
WILEY, DC
中科院分区：
文献类型：
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作者：
SKEHEL, JJ;BAYLEY, PM;WILEY, DC
观察到流感病毒血凝素糖蛋白的构象变化发生在与病毒圆二色体膜融合活性最适的pH值。EM和沉淀物分析表明，在pH 5.2-4.9范围内，菠萝酶增溶血凝素(BHA)以蛋白质-蛋白质花环的形式聚集，并具有结合脂泡和非离子洗涤剂的能力。胰酶处理pH 5.0诱导构象中的BHA表明，聚集是BHA2组分的一种特性，构象变化也涉及BHA1。这些观察结果对糖蛋白在膜融合中的作用的意义进行了讨论。
A conformational change in the hemagglutinin glycoprotein of influenza virus was observed to occur at pH values corresponding to those optimal for the membrane fusion activity of the virus circular dichroism. EM and sedimentation analyses show that, in the pH range 5.2-4.9, bromelain-solubilized hemagglutinin (BHA) aggregates as protein-protein rosettes and acquires the ability to bind both lipid vesicles and nonionic detergent. Trypsin treatment of BHA in the pH 5.0-induced conformation indicates that aggregation is a property of the BHA2 component and that the conformational change also involves BHA1. The implications of these observations for the role of the glycoprotein in membrane fusion are discussed.