Crystal Structure of Herpes Simplex Virus 2 gD Bound to Nectin-1 Reveals a Conserved Mode of Receptor Recognition

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	Crystal Structure of Herpes Simplex Virus 2 gD Bound to Nectin-1 Reveals a Conserved Mode of Receptor Recognition
	Lu, Guangwen 1; Zhang, Na 1; Qi, Jianxun 1; Li, Yan 1; Chen, Zhujun 1; Zheng, Chunfu 2; Gao, George F.1,3,4,5; Yan, Jinghua 1
刊名	JOURNAL OF VIROLOGY
	2014-12-01
卷号	88 期号:23 页码:13678-13688
英文摘要	Herpes simplex virus 1 (HSV-1) and HSV-2 are among the most prevalent human pathogens. Both viruses can recognize, via the surface envelope glycoprotein D (gD), human nectin-1 as a functional receptor. Previous studies have successfully elucidated the molecular basis of the binding between HSV-1 gD and nectin-1 by cocrystallography. Despite a high sequence identity between HSV-1 and HSV-2 gDs, the atomic intermolecule details for the HSV-2-gD/nectin-1 interaction remain elusive. Here, we report the crystal structures of both the unbound and the nectin-1-bound HSV-2 gDs. The free-gD structure expectedly comprises an IgV-like core and the surface-exposed terminal extensions as observed in its HSV-1 counterpart but lacks traceable electron densities for a large portion of the terminal elements. These terminal residues were clearly traced in the complex structure as a definitive loop in the N terminus and an alpha-helix in the C terminus, thereby showing a conserved nectin-1-binding mode as reported for HSV-1 gD. The interface residues in nectin-1 were further mutated and tested for the gD interaction by surface plasmon resonance. The resultant binding patterns were similar for HSV-1 and HSV-2 gDs, further supporting a homologous receptor-binding basis by the two viruses for nectin-1. These data, together with a cell-based fusion assay showing a cross-inhibition of the gD/nectin-1-mediated cell-cell fusion by soluble HSV-1 and HSV-2 gDs, provided solid structural and functional evidence that HSV-1 and HSV-2 recognize nectin-1 via the same binding mode. Finally, we also demonstrated that nectin-1 I80 is an important residue involved in gD interaction.
WOS标题词	Science & Technology ; Life Sciences & Biomedicine
类目[WOS]	Virology
研究领域[WOS]	Virology
关键词[WOS]	CELL-SURFACE RECEPTORS ; PRO-FUSION DOMAIN ; GLYCOPROTEIN-D ; ENTRY MEDIATOR ; SOLUBLE FORMS ; POLIOVIRUS RECEPTOR ; MAXIMUM-LIKELIHOOD ; PSEUDORABIES VIRUS ; HEPARAN-SULFATE ; GENITAL HERPES
收录类别	SCI
语种	英语
WOS记录号	WOS:000344812800013
内容类型	期刊论文
源URL	[http://124.16.173.210/handle/834782/1337]
专题	天津工业生物技术研究所_蛋白质工程与疫苗实验室高福_期刊论文
作者单位	1.Chinese Acad Sci, Inst Microbiol, Key Lab Pathogen Microbiol & Immunol, Beijing, Peoples R China 2.Soochow Univ, Inst Biol & Med Sci, Suzhou, Peoples R China 3.Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Lab Prot Engn & Vaccines, Tianjin, Peoples R China 4.Chinese Acad Sci, Beijing Inst Life Sci, RNIH, Beijing, Peoples R China 5.Chinese Ctr Dis Control & Prevent China CDC, Off Director Gen, Beijing, Peoples R China
推荐引用方式 GB/T 7714	Lu, Guangwen,Zhang, Na,Qi, Jianxun,et al. Crystal Structure of Herpes Simplex Virus 2 gD Bound to Nectin-1 Reveals a Conserved Mode of Receptor Recognition[J]. JOURNAL OF VIROLOGY,2014,88(23):13678-13688.
APA	Lu, Guangwen.,Zhang, Na.,Qi, Jianxun.,Li, Yan.,Chen, Zhujun.,...&Yan, Jinghua.(2014).Crystal Structure of Herpes Simplex Virus 2 gD Bound to Nectin-1 Reveals a Conserved Mode of Receptor Recognition.JOURNAL OF VIROLOGY,88(23),13678-13688.
MLA	Lu, Guangwen,et al."Crystal Structure of Herpes Simplex Virus 2 gD Bound to Nectin-1 Reveals a Conserved Mode of Receptor Recognition".JOURNAL OF VIROLOGY 88.23(2014):13678-13688.