Mutagenic analysis of herpes simplex virus type 1 glycoprotein L reveals the importance of an arginine-rich region for function.
Mutagenic analysis of herpes simplex virus type 1 glycoprotein L reveals the importance of an arginine-rich region for function.
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单纯疱疹病毒 1 型糖蛋白 L 的诱变分析揭示了富含精氨酸的区域对于功能的重要性。
DOI：
10.1016/j.virol.2007.11.014
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发表时间：
2008
期刊：
影响因子：
3.7
通讯作者：
Geraghty,RobertJ
中科院分区：
文献类型：
--
作者：
Klyachkin,YuriM;Geraghty,RobertJ
单纯疱疹病毒1型（HSV-1）糖蛋白H和L（gH和gL）是病毒诱导的膜融合所必需的。gH在病毒体或感染细胞表面的表达由gL的伴侣样活性介导。我们以前已经表明，氨基酸155和161之间的区域是关键的gL分子伴侣样活性。在此，我们对该区域中的残基进行了Ala取代诱变，发现用Ala取代Cys 160、Arg 156、Arg 158或Arg 156/158/159导致结合gH但显示出gH运输和膜融合能力降低的gL突变体。用另一种带正电荷的氨基酸Lys取代Arg 156，恢复了功能。用Lys取代Arg 158恢复了gH运输和细胞融合的功能，但没有病毒进入。这些结果表明，gL的富含精氨酸的区域对功能至关重要。
Herpes simplex virus type 1 (HSV-1) glycoproteins H and L (gH and gL) are required for virus-induced membrane fusion. Expression of gH at the virion or infected cell surface is mediated by the chaperone-like activity of gL. We have previously shown that a region between amino acids 155 and 161 is critical for gL chaperone-like activity. Here, we conducted Ala substitution mutagenesis of residues in this region and found that substitution of Cys160, Arg156, Arg158, or Arg156/158/159 with Ala resulted in a gL mutant that bound gH but displayed a reduced ability in gH trafficking and membrane fusion. Substitution of Arg156 with another positively charged amino acid, Lys, restored function. Substitution of Arg158 with Lys restored function in gH trafficking and cell fusion but not virus entry. These results indicate that an arginine-rich region of gL is critical for function.