Abstract
The coxsackievirus and adenovirus receptor (CAR) mediates attachment and infection by coxsackie B viruses and many adenoviruses. In human airway epithelia, as well as in transfected Madin-Darby canine kidney cells, CAR is expressed exclusively on the basolateral surface. Variants of CAR that lack the cytoplasmic domain or are attached to the cell membrane by a glycosylphosphatidylinositol anchor are expressed on both the apical and basolateral surfaces. We have examined the localization of CAR variants with progressive truncations of the cytoplasmic domain, as well as with mutations that ablate a potential PDZ (PSD95/dlg/ZO-1) interaction motif and a putative tyrosine-based sorting signal. In addition, we have examined the targeting of two murine CAR isoforms, with different C-terminal sequences. The results suggest that multiple regions within the CAR cytoplasmic domain contain information that is necessary for basolateral targeting.
Highlights
The coxsackievirus and adenovirus receptor (CAR)1 mediates attachment and infection by coxsackie B viruses as well as by many human adenoviruses [1,2,3]
The results suggest that multiple regions within the CAR cytoplasmic domain contain information that is necessary for basolateral targeting
Mutant constructs were stably expressed in Madin-Darby canine kidney (MDCK) cells, which were selected for Human CAR (hCAR) surface expression
Summary
The coxsackievirus and adenovirus receptor (CAR)1 mediates attachment and infection by coxsackie B viruses as well as by many human adenoviruses [1,2,3]. Variants of CAR that lack the cytoplasmic domain or are attached to the cell membrane by a glycosylphosphatidylinositol anchor are expressed on both the apical and basolateral surfaces.
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