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首页> 外文期刊>Virology >Characterization of the Equilibrium between the Native and Fusion-Inactive Conformation of Rabies Virus Glycoprotein Indicates That the Fusion Complex Is Made of Several Trimers
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Characterization of the Equilibrium between the Native and Fusion-Inactive Conformation of Rabies Virus Glycoprotein Indicates That the Fusion Complex Is Made of Several Trimers

机译：狂犬病毒糖蛋白的天然构象和融合失活构象之间的平衡特征表明融合复合物是由几个三聚体组成

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摘要

Rabies virus-induced membrane fusion is triggered at low pH and is mediated by the trimeric viral glycoprotein (G). G assumes three conformations: the native state (N) detected above pH 7; the activated state (A), which initiates the fusion process; and the fusion-inactive conformation (I) observed after prolonged incubation at low pH. Differently from other viral fusogenic glycoproteins, G in the I state recovers its native conformation when reincubated above pH 7. Here, we demonstrate that there is a thermodynamic equilibrium between the different states of G between pH 6 and pH 7.5. The study of this equilibrium at various pH values indicated that the conformational change toward I is induced by the protonation of at least three residues per trimer. Finally, studies on the mechanism leading to low pH induced fusion inactivation indicated that a large number of G molecules is required for stable hydrophobic interaction of the virus with the target membrane.
机译：狂犬病病毒诱导的膜融合在低pH值下触发，并由三聚体病毒糖蛋白（G）介导。 G假定为三个构象：pH高于7时检测到的原始状态（N）;激活状态（A），启动融合过程;在低pH条件下长时间孵育后观察到融合无活性构象（I）。与其他病毒融合糖蛋白不同，在pH高于7的条件下重新孵育时，处于I态的G会恢复其天然构象。在这里，我们证明了在pH介于6和7.5之间的G的不同状态之间存在热力学平衡。在各种pH值下对这种平衡的研究表明，每个三聚体至少有三个残基的质子化诱导了向I的构象变化。最后，对导致低pH诱导的融合失活的机理的研究表明，病毒与靶膜的稳定疏水相互作用需要大量G分子。

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