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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >A capsid protein of nonenveloped Bluetongue virus exhibits membrane fusion activity
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A capsid protein of nonenveloped Bluetongue virus exhibits membrane fusion activity

机译：非包膜蓝舌病毒的衣壳蛋白具有膜融合活性

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摘要

The outer capsid layer of Bluetongue virus, a member of the nonenveloped Reoviridae family, is composed of two proteins, a receptor-binding protein, VP2, and a second protein, VP5, which shares structural features with class I fusion proteins of enveloped viruses. In the replication cycle of Bluetongue virus VP5 acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm. Here, we show that VP5 can also act as a fusion protein and induce syncytium formation when it is fused to a transmembrane anchor and expressed on the cell surface. Fusion activity is strictly pH-depehdent and is triggered by short exposure to low pH. No cell-cell fusion is observed at neutral pH. Deletion of the first 40 amino acids, which can fold into two amphipathic helices, abolishes fusion activity. Syncytium formation by VP5 is inhibited in the presence of VP2 when it is expressed in a membrane-anchored form. The data indicate an interaction between the outer capsid protein VP2 and VPS and show that VP5 undergoes pH-dependent conformational changes that render it capable of interacting with cellular membranes. More importantly, our data show that a membrane permeabilization protein of a nonenveloped virus can evolve into a fusion protein by the addition of an appropriate transmembrane anchor. The results strongly suggest that the mechanism of membrane permeabilization by VP5 and membrane fusion by viral fusion proteins require similar structural features and conformational changes.
机译：蓝舌病毒的外衣壳层是无包膜呼肠孤病毒科的成员，它由两种蛋白质组成，即受体结合蛋白VP2和第二种蛋白VP5，与包膜病毒的I类融合蛋白具有相同的结构特征。在蓝舌病病毒的复制周期中，VP5充当膜透化蛋白，介导病毒颗粒从内体区室释放到细胞质中。在这里，我们显示VP5还可以充当融合蛋白，并在融合到跨膜锚上并在细胞表面表达时诱导合胞体形成。融合活性严格地依赖于pH，并且是由于短时暴露于低pH引起的。在中性pH下未观察到细胞-细胞融合。可以折叠成两个两亲性螺旋的前40个氨基酸缺失，消除了融合活性。当VP2以膜锚定形式表达时，在VP2存在下，VP5的合胞体形成受到抑制。数据表明外衣壳蛋白VP2和VPS之间存在相互作用，并表明VP5经历了pH依赖的构象变化，使其能够与细胞膜相互作用。更重要的是，我们的数据表明，通过添加适当的跨膜锚，非包膜病毒的膜通透蛋白可以演变为融合蛋白。结果强烈表明，VP5的膜通透性和病毒融合蛋白的膜融合机制需要相似的结构特征和构象变化。

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