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Journal of Virology, August 2007, p. 8352-8355, Vol. 81, No. 15
0022-538X/07/$08.00+0     doi:10.1128/JVI.00014-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

GxxxG Motif of Severe Acute Respiratory Syndrome Coronavirus Spike Glycoprotein Transmembrane Domain Is Not Involved in Trimerization and Is Not Important for Entry{triangledown}

Jeroen Corver,* Rene Broer, Puck van Kasteren, and Willy Spaan

Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center, 2300 RC Leiden, The Netherlands

Received 3 January 2007/ Accepted 8 May 2007

Recently, a paper was published in which it was proposed that the GxxxG motif of the severe acute respiratory syndrome (SARS) coronavirus spike (S) protein transmembrane domain plays a vital role in oligomerization of the protein (E. Arbely, Z. Granot, I. Kass, J. Orly, and I. T. Arkin, Biochemistry 45:11349-11356, 2006). Here, we show that the GxxxG motif is not involved in SARS S oligomerization by trimerization analysis of S GxxxG mutant proteins. In addition, the capability of S to mediate entry of SARS S-pseudotyped particles overall was affected moderately in the mutant proteins, also arguing for a nonvital role for the GxxxG motif in SARS coronavirus entry.

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

{triangledown} Published ahead of print on 16 May 2007.

Journal of Virology, August 2007, p. 8352-8355, Vol. 81, No. 15
0022-538X/07/$08.00+0     doi:10.1128/JVI.00014-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.





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