Differential receptor-functionality of the two distinct receptor proteins for mouse hepatitis virus.
We compared the virus-binding activity and receptor-functionality of the receptor proteins isolated from mouse hepatitis virus (MHV)-susceptible BALB/c mice (MHVR1) and MHV-resistant SJL mice (MHVR2). By using a soluble receptor protein which lacked the transmembrane and intracytoplasmic domains, virus overlay protein blot assay and neutralization tests showed that MHVR1 bound to JHM cl-2 virus with 300-500 times higher efficiency than to MHVR2. MHVR1 was revealed to have 10-30 fold higher receptor-functionality than MHVR2 when examined by measuring virus-binding to the receptor expressed on the cell surface. These findings suggested that the differences in susceptibility between BALB/c and SJL mice may depend upon the genotype of the MHV receptor.
Ohtsuka
N
N
National Institute of Neuroscience, NCNP, Tokyo, Japan.
Yamada
Y K
YK
Saeki
K
K
Taguchi
F
F
D000818:Animals; D015703:Antigens, CD; D002272:Carcinoembryonic Antigen; D015815:Cell Adhesion Molecules; D002460:Cell Line; D006023:Glycoproteins / Q000378:metabolism*; D051379:Mice; D008807:Mice, Inbred BALB C; D006517:Murine hepatitis virus / Q000378:metabolism*; D011991:Receptors, Virus / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000378:metabolism
D015703:Antigens, CD; C069847:CD66 antigens; D002272:Carcinoembryonic Antigen; C486183:Ceacam1 protein, mouse; C087701:Ceacam2 protein, mouse; D015815:Cell Adhesion Molecules; D006023:Glycoproteins; D011991:Receptors, Virus; D011993:Recombinant Fusion Proteins