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Journal of Virology, January 2002, p. 633-643, Vol. 76, No. 2
0022-538X/01/$04.00+0     DOI: 10.1128/JVI.76.2.633-643.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

GRP78, a Coreceptor for Coxsackievirus A9, Interacts with Major Histocompatibility Complex Class I Molecules Which Mediate Virus Internalization

Kathy Triantafilou,1 Didier Fradelizi,2 Keith Wilson,3 and Martha Triantafilou1*

School of Biological Sciences, University of Portsmouth, Portsmouth PO1 2DY,1 Biotechnology Analytical Laboratories, Glaxo Smithkline Research and Development, Beckenham BR3 3BS, United Kingdom,3 Communications Intercellulaires et Autoimmunité, Hopital Cochin, U477 INSERM, 75014 Paris, France2

Received 8 June 2001/ Accepted 24 September 2001

It is becoming apparent that over the years cell infection by virus seems to have evolved into a multistep process in which many viruses employ distinct cell surface molecules for their attachment and cell entry. In this study the attachment and entry pathway of coxsackievirus A9 (CAV-9), a member of the Picornaviridae family, was investigated. It has been known that, although integrin {alpha}vß3 is utilized as a receptor, its presence alone is insufficient for CAV-9 infection and that CAV-9 also requires a 70-kDa major histocompatibility complex class I (MHC-I)-associated protein (MAP-70) as a coreceptor molecule. We document by protein isolation and peptide sequencing that the 70-kDa protein is GRP78, a member of the heat shock protein 70 family of stress proteins. Furthermore we show by using fluorescence resonance energy transfer (FRET) that GRP78 is also expressed on the cell surface and associates with MHC-I molecules. In addition CAV-9 infection of permissive cells requires GRP78 and also MHC-I molecules, which are essential for virus internalization. The identification of GRP78 as a coreceptor for CAV-9 and the revelation of GRP78 and MHC-I associations have provided new insights into the life cycle of CAV-9, which utilizes integrin {alpha}vß3 and GRP78 as receptor molecules whereas MHC-I molecules serve as the internalization pathway of this virus to mammalian cells.

* Corresponding author. Mailing address: University of Portsmouth, School of Biological Sciences, King Henry Bldg., King Henry I St., Portsmouth PO1 2DY, United Kingdom. Phone: 44 2392 842022. Fax: 44 2392 842070. E-mail: mtrian{at}hotmail.com.

Journal of Virology, January 2002, p. 633-643, Vol. 76, No. 2
0022-538X/01/$04.00+0     DOI: 10.1128/JVI.76.2.633-643.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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