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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
2
1 and
4
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
2
1 and
4
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
2
1 or
4
1 integrins via transfection is increased over virus binding to and
infection of cells transfected with
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
2
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
2
1 was elevated over binding to control cells and was
specifically blocked by the anti-
2 monoclonal antibody AK7. Virus
growth in
4-transfected K562 cells which had also been induced to
express
2
1 integrin with phorbol ester occurred at a level
approaching that in the permissive MA104 cell line. We therefore have
demonstrated that two integrins,
2
1 and
4
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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