Crystal Structure of Herpes Simplex Virus 2 gD Bound to Nectin-1 Reveals a Conserved Mode of Receptor Recognition | |
Lu, Guangwen1; Zhang, Na1; Qi, Jianxun1; Li, Yan1; Chen, Zhujun1; Zheng, Chunfu2; Gao, George F.1,3,4,5; Yan, Jinghua1 | |
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. |
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