Echovirus 1 Interaction with the Human Very Late Antigen-2 (Integrin α2β1) I Domain

• Published in: The Journal of biological chemistry 1997-11, Vol.272 (45), p.28518-28522
• Main Authors: King, Sandra L., Kamata, Tetsuji, Cunningham, Jennifer A., Emsley, Jonas, Liddington, Robert C., Takada, Yoshikazu, Bergelson, Jeffrey M.
• Format: Article
• Language: English
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.272.45.28518

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.