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The coxsackie B virus and adenovirus receptor resides in a distinct membrane microdomain
Journal article   Open access   Peer reviewed

The coxsackie B virus and adenovirus receptor resides in a distinct membrane microdomain

Katherine J D Ashbourne Excoffon, Thomas Moninger and Joseph Zabner
Journal of virology, Vol.77(4), pp.2559-2567
02/2003
DOI: 10.1128/JVI.77.4.2559-2567.2003
PMCID: PMC141093
PMID: 12551994
url
https://doi.org/10.1128/JVI.77.4.2559-2567.2003View
Published (Version of record) Open Access

Abstract

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.
Cricetinae Membrane Microdomains - metabolism Receptors, Virus - metabolism Humans Membrane Microdomains - chemistry Receptors, LDL - metabolism Adenoviridae - pathogenicity Coxsackie and Adenovirus Receptor-Like Membrane Protein Receptors, Virus - genetics Microscopy, Electron Clathrin - pharmacology Endocytosis Animals Receptors, Virus - chemistry Cell Membrane - metabolism Adenoviridae - metabolism COS Cells Membrane Microdomains - genetics CHO Cells

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