Echovirus 1 interaction with the isolated VLA-2 I domain-Reference-Cited by-同舟云学术

Echovirus 1 interaction with the isolated VLA-2 I domain

Published:1995-05 Issue:5 Volume:69 Page:3237-3239
ISSN:0022-538X
Container-title:Journal of Virology
language:en
Short-container-title:J Virol

Author:

King S L¹,Cunningham J A¹,Finberg R W¹,Bergelson J M¹

Affiliation:

1. Laboratory of Infectious Diseases, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115, USA.

Abstract

The isolated I domain of the integrin VLA-2, produced as a bacterial fusion protein, specifically bound echovirus 1 and prevented virus attachment to cells. These results demonstrate that the receptor structures critical for virus attachment are contained solely within the VLA-2 I domain and that soluble receptor fragments are capable of preventing infection.

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/jvi.69.5.3237-3239.1995

Reference18 articles.

1. The integrin VLA-2 binds echovirus 1 and extracellular matrix ligands by different mechanisms;Bergelson J. M.;J. Clin. Invest.,1993

2. Identification of the integrin VLA-2 as a receptor for echovirus 1;Bergelson J. M.;Science,1992

3. Infection by echoviruses 1 and 8 depends on the ~2 subunit of human VLA-2;Bergelson J. M.;J. Virol.,1993

4. The I domain is essential for echovirus 1 interaction with VLA-2;Bergelson J. M.;Cell Adhesion Commun.,1994

5. Distinct cellular functions mediated by different VLA integrinsubunit cytoplasmic domains;Chan B. M. C.;Cell,1992

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