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Herpes simplex virus glycoprotein D bound to the human receptor HveA.

Abstract：

:Herpes simplex virus (HSV) infection requires binding of the viral envelope glycoprotein D (gD) to cell surface receptors. We report the X-ray structures of a soluble, truncated ectodomain of gD both alone and in complex with the ectodomain of its cellular receptor HveA. Two bound anions suggest possible binding sites for another gD receptor, a 3-O-sulfonated heparan sulfate. Unexpectedly, the structures reveal a V-like immunoglobulin (Ig) fold at the core of gD that is closely related to cellular adhesion molecules and flanked by large N- and C-terminal extensions. The receptor binding segment of gD, an N-terminal hairpin, appears conformationally flexible, suggesting that a conformational change accompanying binding might be part of the viral entry mechanism.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Carfí A,Willis SH,Whitbeck JC,Krummenacher C,Cohen GH,Eisenberg RJ,Wiley DC

doi

10.1016/s1097-2765(01)00298-2

subject

Has Abstract

pub_date

2001-07-01 00:00:00

pages

169-79

issue

1

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(01)00298-2

journal_volume

8

pub_type

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