Jackson D C, Nestorowicz A
Virology. 1985 Aug;145(1):72-83. doi: 10.1016/0042-6822(85)90202-8.
At pH 5 influenza virus hemagglutinin undergoes an irreversible conformational change (J.J. Skehel, P. M. Bayley, E. B. Brown, S. R. Martin, M. D. Waterfield, J. M. White, I. A. Wilson, and D. C. Wiley (1982). Proc. Natl. Acad. Sci. USA 79, 968-972) which parallels the appearance of fusion activity of this molecule. This paper describes experiments which explore the conformational change using a panel of monoclonal antibodies which define four of the major antigenic sites of this protein. The results indicate that three of the major antigenic sites of hemagglutinin undergo changes when exposed to acid pH. These changes have little effect on the binding avidity of influenza virus to glycophorin, the major receptor present on the red blood cell surface. These findings have been used to postulate a mechanism where the molecule flexes around a central region resulting in rearrangement in space of its component domains on exposure to low pH.
在pH 5时，流感病毒血凝素会发生不可逆的构象变化（J.J. 斯凯尔、P.M. 贝利、E.B. 布朗、S.R. 马丁、M.D. 沃特菲尔德、J.M. 怀特、I.A. 威尔逊和D.C. 威利（1982年）。《美国国家科学院院刊》79卷，968 - 972页），这种变化与该分子融合活性的出现相平行。本文描述了一些实验，这些实验使用一组单克隆抗体来探索构象变化，这些单克隆抗体确定了该蛋白质的四个主要抗原位点。结果表明，血凝素的三个主要抗原位点在暴露于酸性pH时会发生变化。这些变化对流感病毒与血型糖蛋白（红细胞表面存在的主要受体）的结合亲和力影响很小。这些发现已被用于推测一种机制，即该分子围绕中心区域弯曲，导致其组成结构域在暴露于低pH时在空间上重新排列。
