Expression of the recombinant anchorless N-terminal domain of mouse hepatitis virus (MHV) receptor makes hamster of human cells susceptible to MHV infection.
Mouse hepatitis virus (MHV) receptor, the receptor for the murine coronavirus MHV, was expressed in MHV-resistant hamster and human cells as a series of mutant, recombinant glycoproteins with carboxy-terminal deletions lacking the cytoplasmic tail, transmembrane domain, and various amounts of the immunoglobulin constant-region-like domains. The soluble receptor glycoproteins containing the N-terminal virus-binding domain were released into the supernatant medium and inactivated the infectivity of MHV-A59 virions in a concentration-dependent manner. Surprisingly, some of the anchorless glycoproteins were found on the plasma membranes of transfected cells by flow cytometry, and these cells were rendered susceptible to infection with three strains of MHV. Thus, in the cells in which the anchorless, recombinant receptor glycoprotein is synthesized, some of the protein is bound to an unidentified moiety on the plasma membrane, which allows it to serve as a functional virus receptor.
Dveksler
G S
GS
Department of Patholgy, Uniformed Services University of the Health Sciences, Bethesda, Maryland 20814-4799, USA.
Gagneten
S E
SE
Scanga
C A
CA
Cardellichio
C B
CB
Holmes
K V
KV
D000595:Amino Acid Sequence; D000818:Animals; D006224:Cricetinae; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D006517:Murine hepatitis virus / Q000502:physiology*; D011991:Receptors, Virus / Q000235:genetics / Q000502:physiology*; D011994:Recombinant Proteins / Q000494:pharmacology; D014162:Transfection
D011991:Receptors, Virus; D011994:Recombinant Proteins