Membrane environment can enhance the interaction of glycan binding protein to cell surface glycan receptors.
Membrane environment can enhance the interaction of glycan binding protein to cell surface glycan receptors.
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膜环境可以增强聚糖结合蛋白与细胞表面聚糖受体的相互作用。
DOI：
10.1021/cb5004114
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发表时间：
2014-08-15
影响因子：
4
通讯作者：
Zhu, X-Y
中科院分区：
文献类型：
--
作者：
Shen, Lei;Wang, Yini;Lin, Chia-I;Liu, Hung-wen;Guo, Athena;Zhu, X-Y
凝集素与宿主细胞表面聚糖受体的结合是决定大多数病毒毒力和种属特异性的关键步骤。这由甲型流感病毒的病毒蛋白血凝素（HA）例示，其结合特异性由宿主上皮细胞的聚糖受体上的末端唾液酸的连接模式调节。这种特异性决定了传播是否局限于特定的动物物种或物种之间的跳跃。在这里，我们显示，使用H5 N1禽流感作为模型，重组HA与α2-3连接的唾液酸的特异性结合可以通过与脂质膜表面的相互作用而显著增强。这种效应可以通过两阶段过程定量解释，其中HA与膜表面的弱结合先于与聚糖受体的更特异性和更紧密的结合。在模型系统中发现的弱蛋白-膜相互作用可能在甲型流感病毒的感染和发病机制中起重要的次要作用。
The binding of lectins to glycan receptors on the host cell surface is a key step contributing to the virulence and species specificity of most viruses. This is exemplified by the viral protein hemagglutinin (HA) of the influenza A virus, whose binding specificity is modulated by the linkage pattern of terminal sialic acids on glycan receptors of host epithelial cells. Such specificity dictates whether transmission is confined to a particular animal species or jumps between species. Here, we show, using H5N1 avian influenza as a model, that the specific binding of recombinant HA to α2-3 linked sialic acids can be enhanced dramatically by interaction with the surface of the lipid membrane. This effect can be quantitatively accounted for by a two-stage process in which weak association of HA with the membrane surface precedes more specific and tighter binding to the glycan receptor. The weak protein–membrane interaction discovered here in the model system may play an important secondary role in the infection and pathogenesis of the influenza A virus.
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