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Journal of Virology, July 2004, p. 6967-6973, Vol. 78, No. 13
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.13.6967-6973.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Integrin {alpha}vß6 Is an RGD-Dependent Receptor for Coxsackievirus A9

Çigdem H. Williams,1 Tommi Kajander,2 Timo Hyypiä,2,3 Terry Jackson,4 Dean Sheppard,5 and Glyn Stanway1*

Department of Biological Sciences, University of Essex, Colchester CO4 3SQ,1 Department of Molecular Biology, Institute for Animal Health, Pirbright, Surrey GU24 ONF, United Kingdom,4 Haartman Institute, Department of Virology, University of Helsinki, FIN-00014 Helsinki,2 Department of Medical Microbiology, University of Oulu, FIN-90014 Oulu, Finland,3 Lung Biology Center, Department of Medicine, San Francisco General Hospital, and Division of Pulmonary and Critical Care Medicine, Department of Medicine, University of California, San Francisco, California 941435

Received 27 October 2003/ Accepted 24 February 2004

Coxsackievirus A9 (CAV9), a member of the Enterovirus genus of Picornaviridae, is a common human pathogen and is one of a significant number of viruses containing a functional arginine-glycine-aspartic acid (RGD) motif in one of their capsid proteins. Previous studies identified the RGD-recognizing integrin {alpha}vß3 as its cellular receptor. However, integrin {alpha}vß6 has been shown to be an efficient receptor for another RGD-containing picornavirus, foot-and-mouth disease virus (FMDV). In view of the similarity in sequence context of the RGD motifs in CAV9 and FMDV, we investigated whether {alpha}vß6 can also serve as a receptor for CAV9. We found that CAV9 can bind to purified {alpha}vß6 and also to SW480 cells transfected with ß6 cDNA, allowing expression of {alpha}vß6 on their surface, but it cannot bind to mock-transfected cells. In addition, a higher yield of CAV9 was obtained in ß6-expressing cells than in mock-transfected cells. There was no similar enhancement in infection with an RGD-less CAV9 mutant. We also found ß6 on the surface of GMK cells, a cell line which CAV9 infects efficiently by an RGD-dependent mechanism. Significantly, this infection is blocked by an antibody to {alpha}vß6, while this antibody did not block the low level of infection by the RGD-less mutant. Thus, integrin {alpha}vß6 is an RGD-dependent receptor for CAV9 and may be important in natural CAV9 infections.

* Corresponding author. Mailing address: Department of Biological Sciences, University of Essex, Colchester CO4 3SQ, United Kingdom. Phone: 44 1206 873308. Fax: 44 1206 872592. E-mail: stanwg{at}essex.ac.uk.

Journal of Virology, July 2004, p. 6967-6973, Vol. 78, No. 13
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.13.6967-6973.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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