Structural analysis of the mechanism of adenovirus binding to its human cellular receptor, CAR

Maria C. Bewley, Karen Springer, Yian Biao Zhang, Paul Freimuth, John M. Flanagan

Research output: Contribution to journalArticlepeer-review

382 Scopus citations

Abstract

Binding of virus particles to specific host cell surface receptors is known to be an obligatory step in infection even though the molecular basis for these interactions is not well characterized. The crystal structure of the adenovirus fiber knob domain in complex with domain I of its human cellular receptor, coxsackie and adenovirus receptor (CAR), is presented here. Surface-exposed loops on knob contact one face of CAR, forming a high- affinity complex. Topology mismatches between interacting surfaces create interfacial solvent-filled cavities and channels that may be targets for antiviral drug therapy. The structure identifies key determinants of binding specificity, which may suggest ways to modify the tropism of adenovirus-based gene therapy vectors.

Original languageEnglish (US)
Pages (from-to)1579-1583
Number of pages5
JournalScience
Volume286
Issue number5444
DOIs
StatePublished - Nov 19 1999

All Science Journal Classification (ASJC) codes

  • General

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