JVI Figure table search 04
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Londrigan, S. L.
Right arrow Articles by Coulson, B. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Londrigan, S. L.
Right arrow Articles by Coulson, B. S.

 Previous Article  |  Next Article 

Journal of Virology, September 2003, p. 9486-9501, Vol. 77, No. 17
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.17.9486-9501.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Monkey Rotavirus Binding to {alpha}2ß1 Integrin Requires the {alpha}2 I Domain and Is Facilitated by the Homologous ß1 Subunit

Sarah L. Londrigan,1,{dagger} Kate L. Graham,1 Yoshikazu Takada,2 Peter Halasz,1 and Barbara S. Coulson1*

Department of Microbiology and Immunology, The University of Melbourne, Melbourne, Victoria 3010, Australia,1 Department of Cell Biology, The Scripps Research Institute, La Jolla, California 923072

Received 28 January 2003/ Accepted 4 June 2003

Rotaviruses utilize integrins during virus-cell interactions that lead to infection. Cell binding and infection by simian rotavirus SA11 were inhibited by antibodies (Abs) to the inserted (I) domain of the {alpha}2 integrin subunit. To determine directly which integrins or other proteins bind rotaviruses, cell surface proteins precipitated by rotaviruses were compared with those precipitated by anti-{alpha}2ß1 Abs. Two proteins precipitated by SA11 and rhesus rotavirus RRV from MA104 and Caco-2 cells migrated indistinguishably from {alpha}2ß1 integrin, and SA11 precipitated ß1 from {alpha}2ß1-transfected CHO cells. These viruses specifically precipitated two MA104 cell proteins only, but an additional 160- to 165-kDa protein was precipitated by SA11 from Caco-2 cells. The role of the {alpha}2 I domain in rotavirus binding, infection, and growth was examined using CHO cell lines expressing wild-type or mutated human {alpha}2 or {alpha}2ß1. Infectious SA11 and RRV, but not human rotavirus Wa, specifically bound CHO cell-expressed human {alpha}2ß1 and, to a lesser extent, human {alpha}2 combined with hamster ß1. Binding was inhibited by anti-{alpha}2 I domain monoclonal Abs (MAbs), but not by non-I domain MAbs to {alpha}2, and required the presence of the {alpha}2 I domain. Amino acid residues 151, 221, and 254 in the metal ion-dependent adhesion site of the {alpha}2 I domain that are necessary for type I collagen binding to {alpha}2ß1 were not essential for rotavirus binding. Rotavirus-{alpha}2ß1 binding led to increased virus infection and RRV growth. SA11 and RRV require the {alpha}2 I domain for binding to {alpha}2ß1, and their binding to this integrin is distinguishable from that of collagen.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, Gate 11, The University of Melbourne, Melbourne, Victoria 3010, Australia. Phone: 61 38344 8823. Fax: 61 39347 1540. E-mail: barbarac{at}unimelb.edu.au.

{dagger} Present address: Autoimmunity and Transplantation Division, Walter and Eliza Hall Institute of Medical Research, Melbourne, Victoria 3050, Australia.

Journal of Virology, September 2003, p. 9486-9501, Vol. 77, No. 17
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.17.9486-9501.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. Mol. Cell. Biol. Microbiol. Mol. Biol. Rev.
Clin. Vaccine Immunol. ALL ASM JOURNALS

Copyright © 2003 by the American Society for Microbiology. All rights reserved.