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Integrin _vß₆ Is an RGD-Dependent Receptor for Coxsackievirus A9

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

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 _vß₃ as its cellular receptor. However, integrin _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 _vß₆ can also serve as a receptor for CAV9. We found that CAV9 can bind to purified _vß₆ and also to SW480 cells transfected with ß₆ cDNA, allowing expression of _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 _vß₆, while this antibody did not block the low level of infection by the RGD-less mutant. Thus, integrin _vß₆ is an RGD-dependent receptor for CAV9 and may be important in natural CAV9 infections.

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