GxxxG Motif of Severe Acute Respiratory Syndrome Coronavirus Spike Glycoprotein Transmembrane Domain Is Not Involved in Trimerization and Is Not Important for Entry
- 1 August 2007
- journal article
- Published by American Society for Microbiology in Journal of Virology
- Vol. 81 (15) , 8352-8355
- https://doi.org/10.1128/jvi.00014-07
Abstract
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.Keywords
This publication has 11 references indexed in Scilit:
- A Trimerizing GxxxG Motif Is Uniquely Inserted in the Severe Acute Respiratory Syndrome (SARS) Coronavirus Spike Protein Transmembrane DomainBiochemistry, 2006
- Important Role for the Transmembrane Domain of Severe Acute Respiratory Syndrome Coronavirus Spike Protein during EntryJournal of Virology, 2006
- Synthesis and Characterization of a Native, Oligomeric Form of Recombinant Severe Acute Respiratory Syndrome Coronavirus Spike GlycoproteinJournal of Virology, 2004
- Cellular entry of the SARS coronavirusTrends in Microbiology, 2004
- Oligomerization of the SARS-CoV S glycoprotein: dimerization of the N-terminus and trimerization of the ectodomainBiochemical and Biophysical Research Communications, 2004
- A Novel Coronavirus Associated with Severe Acute Respiratory SyndromeNew England Journal of Medicine, 2003
- The GxxxG motif: A framework for transmembrane helix-helix associationJournal of Molecular Biology, 2000
- TOXCAT: A measure of transmembrane helix association in a biological membraneProceedings of the National Academy of Sciences, 1999
- The transmembrane domain in viral fusion: Essential role for a conserved glycine residue in vesicular stomatitis virus G proteinProceedings of the National Academy of Sciences, 1998
- Evidence for a coiled-coil structure in the spike proteins of coronavirusesJournal of Molecular Biology, 1987