Gs. Dveksler et al., MOUSE HEPATITIS-VIRUS RECEPTOR ACTIVITIES OF AN MHVR MPH CHIMERA AND MHVR MUTANTS LACKING N-LINKED GLYCOSYLATION OF THE N-TERMINAL DOMAIN/, Journal of virology, 69(1), 1995, pp. 543-546
Mouse hepatitis virus binds to the N-terminal domain of its receptor,
MHVR, a murine biliary glycoprotein with four immunoglobulin-like doma
ins (G. S. Dveksler, M. N. Pensiero, C. W. Dieffenbach, C. B. Cardelli
chio, A. A. Basile, P. E. Elia, and K. V. Holmes, Proc. Natl. Acad. Sc
i. USA 90:1716-1720, 1993). A recombinant protein with only the anchor
ed N-terminal domain was not a functional receptor, but a recombinant
protein with the N-terminal domain of MHVR linked to the second and th
ird immunoglobulin-like domains and anchor from the mouse poliovirus r
eceptor homolog, mph, was a functional receptor for mouse hepatitis vi
rus. The native four-domain MHVR has 16 potential N-linked glycosylati
on sites, including three on the N-terminal domain. Recombinant protei
ns lacking each one of these three sites or all three of them were fun
ctional receptors. Thus, glycosylation of the N-terminal domain is not
required, but a glycoprotein longer than the N-terminal domain is req
uired for virus receptor activity.