Previous Article | Next Article ![]()
Journal of Virology, February 2000, p. 1566-1571, Vol. 74, No. 3
Institute of Virology, Department of
Infectious Diseases and Immunology, Faculty of Veterinary Medicine,
and Institute of Biomembranes, Utrecht University, 3584 CL Utrecht, The
Netherlands
Received 21 June 1999/Accepted 19 October 1999
The type I glycoprotein S of coronavirus, trimers of which
constitute the typical viral spikes, is assembled into virions through
noncovalent interactions with the M protein. Here we demonstrate that
incorporation is mediated by the short carboxy-terminal segment comprising the transmembrane and endodomain. To this aim, we used the
virus-like particle (VLP) system that we developed earlier for the
mouse hepatitis virus strain A59 (MHV-A59) and which we describe now
also for the unrelated coronavirus feline infectious peritonitis virus
(FIPV; strain 79-1146). Two chimeric MHV-FIPV S proteins were
constructed, consisting of the ectodomain of the one virus and the
transmembrane and endodomain of the other. These proteins were tested
for their incorporation into VLPs of either species. They were found to
assemble only into viral particles of the species from which their
carboxy-terminal domain originated. Thus, the 64-terminal-residue
sequence suffices to draw the 1308 (MHV)- or 1433 (FIPV)-amino-acid-long mature S protein into VLPs. Both chimeric S
proteins appeared to cause cell fusion when expressed individually,
suggesting that they were biologically fully active. This was indeed
confirmed by incorporating one of the proteins into virions which
thereby acquired a new host cell tropism, as will be reported elsewhere.
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Assembly of Spikes into Coronavirus Particles Is
Mediated by the Carboxy-Terminal Domain of the Spike Protein
*
Corresponding author. Mailing address: Institute of
Virology, Faculty of Veterinary Medicine, Utrecht University, P.O. Box 80.165, 3508 TD Utrecht, The Netherlands. Phone: 31-30-2532462. Fax:
31-30-2536723. E-mail: P.Rottier{at}vet.uu.nl.
This article has been cited by other articles:
| J. Bacteriol. | Mol. Cell. Biol. | Microbiol. Mol. Biol. Rev. |
|---|
| Clin. Vaccine Immunol. | ALL ASM JOURNALS |
|---|