HCAR and MCAR: The human and mouse cellular receptors for subgroup C adenoviruses and group B coxsackieviruses
Open Access
- 1 April 1997
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 94 (7) , 3352-3356
- https://doi.org/10.1073/pnas.94.7.3352
Abstract
The subgroup C of the adenoviruses (Ad) and the group B coxsackieviruses (CVB) are structurally unrelated viruses that are known to compete for an unidentified cell surface receptor. We now describe the isolation of cDNAs from human and mouse that encode the human CVB and Ad2 and 5 receptor (HCAR) and the mouse CVB Ad2 and 5 receptor (MCAR). Both are 46-kDa glycoproteins whose primary amino acid sequences are highly homologous. Structurally, HCAR and MCAR appear to be transmembrane proteins that contain two extracellular immunoglobulin-like domains and therefore belong to this superfamily. Transfection of either of these cDNA molecules into receptor-negative NIH 3T3 cells conferred susceptibility to CVB infection and permitted the expression of β-galactosidase from a recombinant Ad5 vector. In addition, HCAR and MCAR mRNAs could be detected on Northern blots of oligo(dT)-selected RNA from receptor-positive HeLa cells and TCMK-1 as well as several tissues of human and mouse origin that are known to be targets for Ad and CVB infections. Finally, Western blots using antibodies that inhibit virus binding to either the human or mouse CVB receptors detected 46-kDa proteins in HCAR- and MCAR-transfected cells, respectively. Taken together, these results confirm that the isolated cDNAs encode the receptors for the subgroup C Ad and CVB.Keywords
This publication has 22 references indexed in Scilit:
- The hepatitis B virus HBx protein is a dual specificity cytoplasmic activator of Ras and nuclear activator of transcription factors.The EMBO Journal, 1995
- The structure of coxsackievirus B3 at 3.5 å resolutionStructure, 1995
- Receptor proteins on newborn Balb/c mouse brain cells for coxsackievirus B3 are immunologically distinct from those on HeLa cellsVirus Research, 1995
- Crystal structure of the receptor-binding domain of adenovirus type 5 fiberprotein at 1.7 Å resolutionStructure, 1994
- Regulation of G1 progression by E2A and Id helix-loop-helix proteins.The EMBO Journal, 1994
- The Immunoglobulin Superfamily—Domains for Cell Surface RecognitionAnnual Review of Immunology, 1988
- Unrelated animal viruses share receptorsNature, 1976
- PERMISSIVITY OF MOUSE-MAN HYBRID CELL CLONES TO 3 ENTEROVIRUSES - POLIOVIRUS II, COXSACKIE B3 AND ECHOVIRUS 11 - ROLE OF HUMAN CHROMOSOME F-191976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- THE MAMMALIAN CELL-VIRUS RELATIONSHIPThe Journal of Experimental Medicine, 1961