Previous Article | Next Article ![]()
Journal of Virology, June 2008, p. 6078-6083, Vol. 82, No. 12
0022-538X/08/$08.00+0 doi:10.1128/JVI.00074-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

B. J. Haijema,
,
P. Schellen,
P. Wichgers Schreur,
E. te Lintelo,
H. Vennema,
and
P. J. M. Rottier*
Virology Division, Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, Yalelaan 1, 3584 CL Utrecht, The Netherlands
Received 11 January 2008/ Accepted 31 March 2008
A longstanding enigmatic feature of the group 1 coronaviruses is the uncleaved phenotype of their spike protein, an exceptional property among class I fusion proteins. Here, however, we show that some group 1 coronavirus spike proteins carry a furin enzyme recognition motif and can actually be cleaved, as demonstrated for a feline coronavirus. Interestingly, this feature can be lost during cell culture adaptation by a single mutation in the cleavage motif; this, however, preserves a heparan sulfate binding motif and renders infection by the virus heparan sulfate dependent. We identified a similar cell culture adaptation for the human coronavirus OC43.
Published ahead of print on 9 April 2008.
These authors contributed equally.
Present address: Intervet Nederland B.V., Postbus 50, 5830 AB Boxmeer, The Netherlands.
Present address: Center for Infectious Diseases Control, National Institute for Public Health and the Environment (RIVM), Postbus 1, 3720 BA Bilthoven, The Netherlands.
This article has been cited by other articles:
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»