Binding of herpes simplex virus glycoprotein D to nectin-1 exploits host cell adhesion (Q27676007)

Yi Shi

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Jinghua Yan

Jinghua Yan

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Jianxun Qi

Jianxun Qi

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Guangwen Lu

Guangwen Lu

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author name string

Na Zhang

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Zhengfei Guo

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Zheng Fan

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Jiawei Wang

https://api.crossref.org/works/10.1038%2FNCOMMS1571

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language of work or name

English

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publication date

6 December 2011

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published in

Nature Communications

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volume

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page(s)

577

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1 reference

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Requirement of interaction of nectin-1alpha/HveC with afadin for efficient cell-cell spread of herpes simplex virus type 1.

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Soluble V domain of Nectin-1/HveC enables entry of herpes simplex virus type 1 (HSV-1) into HSV-resistant cells by binding to viral glycoprotein D

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Cell-to-cell spread of wild-type herpes simplex virus type 1, but not of syncytial strains, is mediated by the immunoglobulin-like receptors that mediate virion entry, nectin1 (PRR1/HveC/HIgR) and nectin2 (PRR2/HveB)

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Disruption of adherens junctions liberates nectin-1 to serve as receptor for herpes simplex virus and pseudorabies virus entry

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Herpes simplex virus triggers activation of calcium-signaling pathways

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Multiple receptor interactions trigger release of membrane and intracellular calcium stores critical for herpes simplex virus entry

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Structure-based mutagenesis of herpes simplex virus glycoprotein D defines three critical regions at the gD-HveA/HVEM binding interface

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Expression of entry receptor nectin-1 of herpes simplex virus 1 and/or herpes simplex virus 2 in normal and neoplastic human nervous system tissues

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