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The I domain is essential for echovirus 1 interaction with VLA-2
J M Bergelson1, N F St John, S Kawaguchi
1Laboratory of Infectious Diseases, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115.
Cell Adhesion and Communication
|October 1, 1994
Summary
The alpha 2 beta 1 integrin's I domain is crucial for echovirus 1 binding and cell adhesion to collagen. This key region mediates interactions with both viruses and extracellular matrix ligands.
Area of Science:
- Cell Biology
- Virology
- Immunology
Background:
- VLA-2 (alpha 2 beta 1 integrin) functions as a receptor for echovirus 1 and mediates cell adhesion to collagen and laminin.
- The I domain within the alpha 2 subunit of VLA-2 is a conserved region implicated in ligand interactions.
Purpose of the Study:
- To identify the specific regions of the human VLA-2 alpha 2 subunit responsible for echovirus 1 binding.
- To investigate the role of the I domain in VLA-2 interactions with both viral and extracellular matrix ligands.
Main Methods:
- Construction and analysis of murine/human chimeric alpha 2 molecules.
- Utilizing monoclonal antibodies to map binding sites for echovirus 1 and collagen.
Main Results:
- The human I domain, when inserted into the murine alpha 2 subunit, conferred efficient echovirus 1 binding.
- Monoclonal antibodies targeting the human I domain inhibited both virus attachment and VLA-2-mediated cell adhesion to collagen.
- Murine alpha 2, unlike human alpha 2, did not promote virus binding, despite high sequence identity.
Conclusions:
- The I domain of the VLA-2 alpha 2 subunit is essential for specific interactions with echovirus 1.
- The I domain plays a dual role, mediating interactions with both viral pathogens and extracellular matrix components like collagen.