STRUCTURE OF THE INFLUENZA-VIRUS HEMAGGLUTININ COMPLEXED WITH ITS RECEPTOR, SIALIC-ACID
STRUCTURE OF THE INFLUENZA-VIRUS HEMAGGLUTININ COMPLEXED WITH ITS RECEPTOR, SIALIC-ACID
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DOI：
10.1038/333426a0
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发表时间：
1988-06-02
期刊：
影响因子：
64.8
通讯作者：
WILEY, DC
中科院分区：
文献类型：
--
作者：
WEIS, W;BROWN, JH;WILEY, DC
与细胞受体类似物复合的流感病毒血凝素的三维结构显示唾液酸与抗体结合位点包围的保守氨基酸口袋结合。唾液酸填充保守的口袋，证明它是流感病毒受体。抗体结合位点的接近表明抗体通过阻止病毒与细胞结合来中和病毒的感染性。这些结构表明了设计抗病毒药物的方法，可以阻止病毒附着在细胞上。
The three-dimensional structures of influenza virus haemagglutinins complexed with cell receptor analogues show sialic acids bound to a pocket of conserved amino acids surrounded by antibody-binding sites. Sialic acid fills the conserved pocket, demonstrating that it is the influenza virus receptor. The proximity of the antibody-binding sites suggests that antibodies neutralize virus infectivity by preventing virus-to-cell binding. The structures suggest approaches to the design of anti-viral drugs that could block attachment of viruses to cells.