The i domain is essential for echovirus 1 interaction with VLA-2

Jeffrey M. Bergelson, Nicole F. John, Satoshi Kawaguchi, Renata Pasqualini, Feodor Berdichevsky, Martin E. Hemler, Robert W. Finberg

Research output: Contribution to journalArticlepeer-review

22 Scopus citations


VLA-2, the α2β1 integrin, mediates cell adhesion to collagen and laminin, and is the receptor for the human pathogen echovirus 1. Because of its similarity to domains present in other proteins that interact with collagen, a 191 amino acid region within the α2 subunit (the I domain) has been proposed as a potential site for ligand interactions. Although the α2 subunits of human and murine VLA-2 are 84% identical, human α2 promotes virus binding whereas murine α2 does not. We used murine/human chimeric α2 molecules to identify regions of the human molecule essential for virus binding. Virus bound efficiently to a chimeric protein in which the human I domain was inserted into murine α2, indicating that the human I domain is responsible for specific virus interactions. Monoclonal antibodies that inhibited virus attachment all recognized epitopes within the human I do-main, further suggesting that virus interacts with this portion of the molecule. Similarly, antibodies that prevented VLA-2-mediated cell adhesion to collagen also mapped to the I domain. These results indicate that the I domain plays a role in VLA-2 interactions both with virus and with extracellular matrix ligands.

Original languageEnglish (US)
Pages (from-to)455-464
Number of pages10
JournalCell Communication and Adhesion
Issue number5
StatePublished - 1994
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Clinical Biochemistry
  • Cell Biology


  • Integrin
  • Ligand interactions
  • Picornavirus
  • Virus receptor


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