Echovirus 1 interaction with the human very late antigen-2 (integrin α2β1) I domain: Identification of two independent virus contact sites distinct from the metal ion-dependent adhesion site

Sandra L. King, Tetsuji Kamata, Jennifer A. Cunningham, Jonas Emsley, Robert C. Liddington, Yoshikazu Takada, Jeffrey M. Bergelson

Research output: Contribution to journalArticlepeer-review

38 Scopus citations

Abstract

The human integrin very late antigen (VLA)-2 (CD49b/CD29) mediates interactions with collagen and is the receptor for echovirus 1. Binding sites for both collagen and echovirus 1 have been mapped to the I domain within the α2 subunit of the VLA-2 α2β1 heterodimer. Although marine VLA-2 interacts with collagen, it does not bind virus. We have used isolated human-murine chimeric I domains expressed as glutathione S-transferase fusion proteins in Escherichia coli to identify two groups of amino acids, 199-201 and 212-216, independently involved in virus attachment. These residues are distinct from the metal ion-dependent adhesion site previously demonstrated to be essential for VLA-2 interactions with collagen. Mutations in three metal ion-dependent adhesion site residues that abolish adhesion to collagen had no effect on virus binding. These results confirm that different sites within the I domain are responsible for VLA-2 interaction with extracellular matrix proteins and with vital ligands.

Original languageEnglish (US)
Pages (from-to)28518-28522
Number of pages5
JournalJournal of Biological Chemistry
Volume272
Issue number45
DOIs
StatePublished - Nov 7 1997
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry

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