使用抗血凝素单克隆抗体筛选出的流感病毒变体的受体结合和膜融合特性。
The receptor-binding and membrane-fusion properties of influenza virus variants selected using anti-haemagglutinin monoclonal antibodies.
作者信息
Daniels P S, Jeffries S, Yates P, Schild G C, Rogers G N, Paulson J C, Wharton S A, Douglas A R, Skehel J J, Wiley D C
出版信息
EMBO J. 1987 May;6(5):1459-65. doi: 10.1002/j.1460-2075.1987.tb02387.x.
Abstract
A monoclonal antibody raised against X-31 influenza virus reacted with the majority of natural H3N2 viruses isolated between 1968 and 1982. A number of variants of X-31 and of a receptor-binding mutant of X-31 were selected by the antibody during virus replication in eggs and MDCK cells. Antibody-binding assays indicated that the viruses selected were not antigenic variants and analyses using derivatized erythrocytes showed that their receptor-binding properties differed from those of the parent viruses. The amino acid substitutions in the variants were all located in the vicinity of the receptor-binding site and the structural consequences are discussed in relation to the three-dimensional structure of X-31 HA. In addition all of the variants fused membranes at higher pH than wild-type virus indicating that structural modifications in the distal globular region of HA influence the low pH-induced conformational change required for membrane fusion.
摘要
一种针对X-31流感病毒产生的单克隆抗体与1968年至1982年间分离出的大多数天然H3N2病毒发生反应。在病毒于鸡胚和MDCK细胞中复制期间，该抗体筛选出了许多X-31变体以及X-31的一种受体结合突变体。抗体结合试验表明，筛选出的病毒不是抗原变体，使用衍生化红细胞进行的分析表明，它们的受体结合特性与亲本病毒不同。变体中的氨基酸取代均位于受体结合位点附近，并结合X-31血凝素（HA）的三维结构讨论了其结构后果。此外，所有变体在比野生型病毒更高的pH值下融合膜，这表明HA远端球状区域的结构修饰影响了膜融合所需的低pH诱导的构象变化。
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