A chimeric poliovirus/CD4 receptor confers susceptibility to poliovirus on mouse cells.
The human poliovirus receptor consists of three extracellular immunoglobulinlike domains, a transmembrane domain, and an intracytoplasmic domain. The amino-terminal variable-type domain (V domain) of the human poliovirus receptor is necessary and sufficient for its function as a viral receptor (H.-C. Selinka, A. Zibert, and E. Wimmer, Proc. Natl. Acad. Sci. USA 88:3598-3602, 1991). In this paper, data are presented showing that transfer of the putative poliovirus receptor-binding domain to a truncated receptor for the human immunodeficiency virus results in a functional receptor for poliovirus. After expression in mouse cells, this chimeric protein confers susceptibility to poliovirus. Thus, unlike human immunodeficiency virus, poliovirus can enter mouse cells by way of a truncated CD4 receptor if the specific binding domain for poliovirus is provided.
Selinka
H C
HC
Department of Microbiology, State University of New York, Stony Brook 11794-8621.
Zibert
A
A
Wimmer
E
E
D000818:Animals; D015704:CD4 Antigens / Q000378:metabolism*; D002478:Cells, Cultured; D002678:Chimera; D007700:Kinetics; D051379:Mice; D017955:Poliovirus / Q000378:metabolism*; D011991:Receptors, Virus / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000378:metabolism
D015704:CD4 Antigens; D011991:Receptors, Virus; D011993:Recombinant Fusion Proteins