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Journal of Virology, July 2000, p. 5856-5862, Vol. 74, No. 13
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Human Parechovirus 1 Utilizes Integrins alpha vbeta 3 and alpha vbeta 1 as Receptors

Kathy Triantafilou,1,* Martha Triantafilou,1 Yoshikazu Takada,2 and Nelson Fernandez1

Department of Biological Sciences, University of Essex, Colchester, Essex CO4 3SQ, United Kingdom,1 and Department of Vascular Biology, The Scripps Research Institute, La Jolla, California 920372

Received 24 November 1999/Accepted 21 March 2000

Human parechovirus 1 (HPEV1) displays an arginine-glycine-aspartic acid (RGD) motif in the VP1 capsid protein, suggesting integrins as candidate receptors for HPEV1. A panel of monoclonal antibodies (MAbs) specific for integrins alpha vbeta 3, alpha vbeta 1, and alpha vbeta 5, which have the ability to recognize the RGD motif, and also a MAb specific for integrin alpha 2beta 1, an integrin that does not recognize the RGD motif, were tested on A549 cells. Our results showed that integrin alpha v-specific MAb reduced infectivity by 85%. To specify which alpha v integrins the virus utilizes, we tested MAbs specific to integrins alpha vbeta 3 and alpha vbeta 1 which reduced infectivity significantly, while a MAb specific for integrin alpha vbeta 5, as well as the MAb specific for alpha 2beta 1, showed no reduction. When a combination of MAbs specific for integrins alpha vbeta 3 and alpha vbeta 1 were used, virus infectivity was almost completely inhibited; this shows that integrins alpha vbeta 3 and alpha vbeta 1 are utilized by the virus. We therefore proceeded to test whether alpha v integrins' natural ligands fibronectin and vitronectin had an effect on HPEV1 infectivity. We found that vitronectin reduced significantly HPEV1 infectivity, whereas a combination of vitronectin and fibronectin abolished infection. To verify the use of integrins alpha vbeta 3 and alpha vbeta 1 as HPEV1 receptors, CHO cells transfected and expressing either integrin alpha vbeta 3 or integrin alpha vbeta 1 were used. It was shown that the virus could successfully infect these cells. However, in immunoprecipitation experiments using HPEV1 virions and allowing the virus to bind to solubilized A549 cell extract, we isolated and confirmed by Western blotting the alpha vbeta 3 heterodimer. In conclusion, we found that HPEV1 utilises both integrin alpha vbeta 3 and alpha vbeta 1 as receptors; however, in cells that express both integrins, HPEV1 may preferentially bind integrin alpha vbeta 3.

* Corresponding author. Mailing address: Department of Biological Sciences, Central Campus, University of Essex, Wivenhoe Park, Colchester, Essex CO4 3SQ, United Kingdom. Phone: 44 1206 873787. Fax: 44 01206 872592. E-mail: ktrian{at}essex.ac.uk.

Journal of Virology, July 2000, p. 5856-5862, Vol. 74, No. 13
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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