Journal of Biological Chemistry
Volume 272, Issue 45, 7 November 1997, Pages 28518-28522
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PROTEIN CHEMISTRY AND STRUCTURE
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*

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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 murine 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 viral ligands.

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*

This work was supported in part by National Institutes of Health Grants AI35667 (to J. M. B.), GM47157 and GM49899 (to Y. T.), and Training Grants AI07245 and AI07386.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The atomic coordinates for the VLA-2 I domain (code 1aox) have been deposited in the Protein Data Bank, Brookhaven National Laboratory, Upton, NY.