Herpes simplex virus glycoprotein D bound to the human receptor HveA

Andrea Carfí, Sharon H. Willis, J. Charles Whitbeck, Claude Krummenacher, Gary H. Cohen, Roselyn J. Eisenberg, Don C. Wiley

Research output: Contribution to journalArticlepeer-review

296 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)169-179
Number of pages11
JournalMolecular Cell
Volume8
Issue number1
DOIs
StatePublished - 2001
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

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