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Journal of Virology, January 2000, p. 228-236, Vol. 74, No. 1
0022-538X/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Integrins alpha 2beta 1 and alpha 4beta 1 Can Mediate SA11 Rotavirus Attachment and Entry into Cells

Marilyn J. Hewish,1 Yoshikazu Takada,2 and Barbara S. Coulson1,*

Department of Microbiology and Immunology, The University of Melbourne, Parkville 3052, Victoria, Australia,1 and Department of Vascular Biology, The Scripps Research Institute, La Jolla, California 920372

Received 3 June 1999/Accepted 30 September 1999

Most mammalian rotaviruses contain tripeptide amino acid sequences in outer capsid proteins VP4 and VP7 which have been shown to act as ligands for integrins alpha 2beta 1 and alpha 4beta 1. Peptides containing these sequences and monoclonal antibodies directed to these integrins block rotavirus infection of cells. Here we report that SA11 rotavirus binding to and infection of K562 cells expressing alpha 2beta 1 or alpha 4beta 1 integrins via transfection is increased over virus binding to and infection of cells transfected with alpha 3 integrin or parent cells. The increased binding and growth were specifically blocked by a monoclonal antibody to the transfected integrin subunit but not by irrelevant antibodies. In our experiments, integrin activation with phorbol ester did not affect virus binding to cells. However, phorbol ester treatment of K562 parent and transfected cells induced endogenous gene expression of alpha 2beta 1 integrin, which was detectable by flow cytometry 16 h after treatment and quantitatively correlated with the increased level of SA11 virus growth observed after this time. Virus binding to K562 cells treated with phorbol ester 24 h previously and expressing alpha 2beta 1 was elevated over binding to control cells and was specifically blocked by the anti-alpha 2 monoclonal antibody AK7. Virus growth in alpha 4-transfected K562 cells which had also been induced to express alpha 2beta 1 integrin with phorbol ester occurred at a level approaching that in the permissive MA104 cell line. We therefore have demonstrated that two integrins, alpha 2beta 1 and alpha 4beta 1, are capable of acting as cellular receptors for SA11 rotavirus.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, The University of Melbourne, Gate 10, Royal Parade, Parkville 3052, Victoria, Australia. Phone: 61 3 93448823. Fax: 61 3 9347 1540. E-mail: b.coulson{at}microbiology.unimelb.edu.au.

Journal of Virology, January 2000, p. 228-236, Vol. 74, No. 1
0022-538X/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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