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Journal of Virology, February 2003, p. 2559-2567, Vol. 77, No. 4
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.4.2559-2567.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

The Coxsackie B Virus and Adenovirus Receptor Resides in a Distinct Membrane Microdomain

Katherine J. D. Ashbourne Excoffon, Thomas Moninger, and Joseph Zabner*

Department of Internal Medicine, Roy J. and Lucille A. Carver College of Medicine, University of Iowa, Iowa City, Iowa 52242

Received 2 August 2002/ Accepted 19 November 2002

The coxsackie B virus and adenovirus receptor (CAR) is a member of the immunoglobulin superfamily. In addition to activity as a viral receptor, it may play a role in cellular adhesion. We asked what determines the cell membrane microdomain of CAR. We found that CAR is localized to a novel lipid-rich microdomain similar to that of the low-density lipoprotein receptor (LDLR) but distinct from that of a CAR variant that exhibited traditional lipid raft localization via fusion to a glycosylphosphatidylinositol (GPI) tail. The cytoplasmic tail determines its membrane localization, since deletion of this domain resulted in mislocalization. Results indicate that CAR, CAR-LDLR, and LDLR reside in a novel lipid raft that is distinct from caveolin-1-containing caveolae and GPI-linked proteins. Residence in a lipid-rich domain provides a mechanism that allows CAR to interact with other cell adhesion proteins and yet function as an adenovirus receptor.

* Corresponding author. Mailing address: Roy J. and Lucille A. Carver College of Medicine, University of Iowa, 500 EMRB, Iowa City, IA 52242. Phone: (319) 335-7608. Fax: (319) 335-7623. E-mail: joseph-zabner{at}uiowa.edu.

Journal of Virology, February 2003, p. 2559-2567, Vol. 77, No. 4
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.4.2559-2567.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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