This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Godeke, G.-J.
Right arrow Articles by Rottier, P. J. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Godeke, G.-J.
Right arrow Articles by Rottier, P. J. M.

 Previous Article  |  Next Article 

Journal of Virology, February 2000, p. 1566-1571, Vol. 74, No. 3
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

Gert-Jan Godeke, Cornelis A. M. de Haan, John W. A. Rossen, Harry Vennema, and Peter J. M. Rottier*

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.

* 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.

Journal of Virology, February 2000, p. 1566-1571, Vol. 74, No. 3
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Yamada, Y., Liu, D. X. (2009). Proteolytic Activation of the Spike Protein at a Novel RRRR/S Motif Is Implicated in Furin-Dependent Entry, Syncytium Formation, and Infectivity of Coronavirus Infectious Bronchitis Virus in Cultured Cells. J. Virol. 83: 8744-8758 [Abstract] [Full Text]  
  • Boscarino, J. A., Logan, H. L., Lacny, J. J., Gallagher, T. M. (2008). Envelope Protein Palmitoylations Are Crucial for Murine Coronavirus Assembly. J. Virol. 82: 2989-2999 [Abstract] [Full Text]  
  • McBride, C. E., Li, J., Machamer, C. E. (2007). The Cytoplasmic Tail of the Severe Acute Respiratory Syndrome Coronavirus Spike Protein Contains a Novel Endoplasmic Reticulum Retrieval Signal That Binds COPI and Promotes Interaction with Membrane Protein. J. Virol. 81: 2418-2428 [Abstract] [Full Text]  
  • Han, M. G., Cheon, D.-S., Zhang, X., Saif, L. J. (2006). Cross-Protection against a Human Enteric Coronavirus and a Virulent Bovine Enteric Coronavirus in Gnotobiotic Calves. J. Virol. 80: 12350-12356 [Abstract] [Full Text]  
  • Neuman, B. W., Adair, B. D., Yoshioka, C., Quispe, J. D., Orca, G., Kuhn, P., Milligan, R. A., Yeager, M., Buchmeier, M. J. (2006). Supramolecular architecture of severe acute respiratory syndrome coronavirus revealed by electron cryomicroscopy.. J. Virol. 80: 7918-7928 [Abstract] [Full Text]  
  • Oostra, M., de Haan, C. A. M., de Groot, R. J., Rottier, P. J. M. (2006). Glycosylation of the Severe Acute Respiratory Syndrome Coronavirus Triple-Spanning Membrane Proteins 3a and M. J. Virol. 80: 2326-2336 [Abstract] [Full Text]  
  • Rottier, P. J. M., Nakamura, K., Schellen, P., Volders, H., Haijema, B. J. (2005). Acquisition of Macrophage Tropism during the Pathogenesis of Feline Infectious Peritonitis Is Determined by Mutations in the Feline Coronavirus Spike Protein. J. Virol. 79: 14122-14130 [Abstract] [Full Text]  
  • Hurst, K. R., Kuo, L., Koetzner, C. A., Ye, R., Hsue, B., Masters, P. S. (2005). A Major Determinant for Membrane Protein Interaction Localizes to the Carboxy-Terminal Domain of the Mouse Coronavirus Nucleocapsid Protein. J. Virol. 79: 13285-13297 [Abstract] [Full Text]  
  • Ye, R., Montalto-Morrison, C., Masters, P. S. (2004). Genetic Analysis of Determinants for Spike Glycoprotein Assembly into Murine Coronavirus Virions: Distinct Roles for Charge-Rich and Cysteine-Rich Regions of the Endodomain. J. Virol. 78: 9904-9917 [Abstract] [Full Text]  
  • Bosch, B. J., de Haan, C. A. M., Rottier, P. J. M. (2004). Coronavirus Spike Glycoprotein, Extended at the Carboxy Terminus with Green Fluorescent Protein, Is Assembly Competent. J. Virol. 78: 7369-7378 [Abstract] [Full Text]  
  • Buchholz, U. J., Bukreyev, A., Yang, L., Lamirande, E. W., Murphy, B. R., Subbarao, K., Collins, P. L. (2004). Contributions of the structural proteins of severe acute respiratory syndrome coronavirus to protective immunity. Proc. Natl. Acad. Sci. USA 101: 9804-9809 [Abstract] [Full Text]  
  • de Haan, C. A. M., Stadler, K., Godeke, G.-J., Bosch, B. J., Rottier, P. J. M. (2004). Cleavage Inhibition of the Murine Coronavirus Spike Protein by a Furin-Like Enzyme Affects Cell-Cell but Not Virus-Cell Fusion. J. Virol. 78: 6048-6054 [Abstract] [Full Text]  
  • Addie, D. D., Schaap, I. A. T., Nicolson, L., Jarrett, O. (2003). Persistence and transmission of natural type I feline coronavirus infection. J. Gen. Virol. 84: 2735-2744 [Abstract] [Full Text]  
  • Casais, R., Dove, B., Cavanagh, D., Britton, P. (2003). Recombinant Avian Infectious Bronchitis Virus Expressing a Heterologous Spike Gene Demonstrates that the Spike Protein Is a Determinant of Cell Tropism. J. Virol. 77: 9084-9089 [Abstract] [Full Text]  
  • Haijema, B. J., Volders, H., Rottier, P. J. M. (2003). Switching Species Tropism: an Effective Way To Manipulate the Feline Coronavirus Genome. J. Virol. 77: 4528-4538 [Abstract] [Full Text]  
  • Kuo, L., Masters, P. S. (2002). Genetic Evidence for a Structural Interaction between the Carboxy Termini of the Membrane and Nucleocapsid Proteins of Mouse Hepatitis Virus. J. Virol. 76: 4987-4999 [Abstract] [Full Text]  
  • Corse, E., Machamer, C. E. (2002). The Cytoplasmic Tail of Infectious Bronchitis Virus E Protein Directs Golgi Targeting. J. Virol. 76: 1273-1284 [Abstract] [Full Text]  
  • de Haan, C. A. M., Vennema, H., Rottier, P. J. M. (2000). Assembly of the Coronavirus Envelope: Homotypic Interactions between the M Proteins. J. Virol. 74: 4967-4978 [Abstract] [Full Text]  
  • Kuo, L., Godeke, G.-J., Raamsman, M. J. B., Masters, P. S., Rottier, P. J. M. (2000). Retargeting of Coronavirus by Substitution of the Spike Glycoprotein Ectodomain: Crossing the Host Cell Species Barrier. J. Virol. 74: 1393-1406 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»