The Murid Herpesvirus-4 gL Regulates an Entry-Associated Conformation Change in gH
The Murid Herpesvirus-4 gL Regulates an Entry-Associated Conformation Change in gH
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DOI：
10.1371/journal.pone.0002811
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发表时间：
2008-07-30
期刊：
影响因子：
3.7
通讯作者：
Stevenson, Philip G.
中科院分区：
文献类型：
--
作者：
Gillet, Laurent;Colaco, Susanna;Stevenson, Philip G.
糖蛋白H(Gh)/gl异源二聚体是疱疹病毒膜融合的关键。然而，它是如何发挥作用的还没有被很好地理解。Murid疱疹病毒-4Gh与其他疱疹病毒一样，通过与g1结合而形成正常的病毒粒子构象。然而，Gh在病毒颗粒内吞后又转换回不依赖于gl的构象。这种转换与GB中的构象转换和衣壳释放相一致。缺乏gl的病毒粒子结构性地表达Gh的下游形式，过早地将gB转换为其下游形式，并表现出过早的衣壳释放，感染性差。这些数据表明，gl在调节Gh和Gb从细胞结合到膜融合的功能转换中起着关键作用。
The glycoprotein H (gH)/gL heterodimer is crucial for herpesvirus membrane fusion. Yet how it functions is not well understood. The Murid Herpesvirus-4 gH, like that of other herpesviruses, adopts its normal virion conformation by associating with gL. However, gH switched back to a gL-independent conformation after virion endocytosis. This switch coincided with a conformation switch in gB and with capsid release. Virions lacking gL constitutively expressed the downstream form of gH, prematurely switched gB to its down-stream form, and showed premature capsid release with poor infectivity. These data argue that gL plays a key role in regulating a gH and gB functional switch from cell binding to membrane fusion.