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 Broer, R.
Right arrow Articles by Corver, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Broer, R.
Right arrow Articles by Corver, J.

 Previous Article  |  Next Article 

Journal of Virology, February 2006, p. 1302-1310, Vol. 80, No. 3
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.3.1302-1310.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Important Role for the Transmembrane Domain of Severe Acute Respiratory Syndrome Coronavirus Spike Protein during Entry

Rene Broer,1,{dagger} Bertrand Boson,2,{dagger} Willy Spaan,1 François-Loïc Cosset,2 and Jeroen Corver1*

Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center, 2300 RC Leiden, The Netherlands,1 Laboratoire de Vectorologie Rétrovirale et Thérapie Génique, INSERM U412, IFR128 BioSciences Lyon-Gerland, Ecole Normale Supérieure de Lyon, 46 allée d'Italie, 69364 Lyon Cedex 07, France2

Received 3 June 2005/ Accepted 11 November 2005

The spike protein (S) of severe acute respiratory syndrome coronavirus (SARS-CoV) is responsible for receptor binding and membrane fusion. It contains a highly conserved transmembrane domain that consists of three parts: an N-terminal tryptophan-rich domain, a central domain, and a cysteine-rich C-terminal domain. The cytoplasmic tail of S has previously been shown to be required for assembly. Here, the roles of the transmembrane and cytoplasmic domains of S in the infectivity and membrane fusion activity of SARS-CoV have been studied. SARS-CoV S-pseudotyped retrovirus (SARSpp) was used to measure S-mediated infectivity. In addition, the cell-cell fusion activity of S was monitored by a Renilla luciferase-based cell-cell fusion assay. SVSV-Cyt, an S chimera with a cytoplasmic tail derived from vesicular stomatitis virus G protein (VSV-G), and SMHV-TMDCyt, an S chimera with the cytoplasmic and transmembrane domains of mouse hepatitis virus, displayed wild-type-like activity in both assays. SVSV-TMDCyt, a chimera with the cytoplasmic and transmembrane domains of VSV-G, was impaired in the SARSpp and cell-cell fusion assays, showing 3 to 25% activity compared to the wild type, depending on the assay and the cells used. Examination of the oligomeric state of the chimeric S proteins in SARSpp revealed that SVSV-TMDCyt trimers were less stable than wild-type S trimers, possibly explaining the lowered fusogenicity and infectivity.

* Corresponding author. Mailing address: Leiden University Medical Center, Department of Medical Microbiology, E4-P, P.O. Box 9600, 2300 RC Leiden, The Netherlands. Phone: 31-715263649. Fax: 31-715266761. E-mail: j.corver{at}lumc.nl.

{dagger} R.B. and B.B. contributed equally to this work.

Journal of Virology, February 2006, p. 1302-1310, Vol. 80, No. 3
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.3.1302-1310.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Barry, C., Duncan, R. (2009). Multifaceted Sequence-Dependent and -Independent Roles for Reovirus FAST Protein Cytoplasmic Tails in Fusion Pore Formation and Syncytiogenesis. J. Virol. 83: 12185-12195 [Abstract] [Full Text]  
  • Shulla, A., Gallagher, T. (2009). Role of Spike Protein Endodomains in Regulating Coronavirus Entry. J. Biol. Chem. 284: 32725-32734 [Abstract] [Full Text]  
  • Schwegmann-Wessels, C., Glende, J., Ren, X., Qu, X., Deng, H., Enjuanes, L., Herrler, G. (2009). Comparison of vesicular stomatitis virus pseudotyped with the S proteins from a porcine and a human coronavirus. J. Gen. Virol. 90: 1724-1729 [Abstract] [Full Text]  
  • Yang, J., James, E., Roti, M., Huston, L., Gebe, J. A., Kwok, W. W. (2009). Searching immunodominant epitopes prior to epidemic: HLA class II-restricted SARS-CoV spike protein epitopes in unexposed individuals. Int Immunol 21: 63-71 [Abstract] [Full Text]  
  • Li, Z., Blissard, G. W. (2008). Functional Analysis of the Transmembrane (TM) Domain of the Autographa californica Multicapsid Nucleopolyhedrovirus GP64 Protein: Substitution of Heterologous TM Domains. J. Virol. 82: 3329-3341 [Abstract] [Full Text]  
  • Howard, M. W., Travanty, E. A., Jeffers, S. A., Smith, M. K., Wennier, S. T., Thackray, L. B., Holmes, K. V. (2008). Aromatic Amino Acids in the Juxtamembrane Domain of Severe Acute Respiratory Syndrome Coronavirus Spike Glycoprotein Are Important for Receptor-Dependent Virus Entry and Cell-Cell Fusion. J. Virol. 82: 2883-2894 [Abstract] [Full Text]  
  • Corver, J., Broer, R., van Kasteren, P., Spaan, W. (2007). GxxxG Motif of Severe Acute Respiratory Syndrome Coronavirus Spike Glycoprotein Transmembrane Domain Is Not Involved in Trimerization and Is Not Important for Entry. J. Virol. 81: 8352-8355 [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»