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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.



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