GxxxG motif of severe acute respiratory syndrome coronavirus spike glycoprotein transmembrane domain is not involved in trimerization and is not important for entry.
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.
Corver
Jeroen
J
Department of Medical Microbiology, Leiden University Medical Center, E4-P, P.O. Box 9600, 2300 RC Leiden, The Netherlands. j.corver@lumc.nl
Broer
Rene
R
van Kasteren
Puck
P
Spaan
Willy
W
D020816:Amino Acid Motifs; D000818:Animals; D002478:Cells, Cultured; D006801:Humans; D008562:Membrane Glycoproteins / Q000235:genetics / Q000378:metabolism; D051379:Mice; D008969:Molecular Sequence Data; D020836:Protein Structure, Quaternary; D045473:Severe acute respiratory syndrome-related coronavirus / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D045169:Severe Acute Respiratory Syndrome; D064370:Spike Glycoprotein, Coronavirus; D014759:Viral Envelope Proteins / Q000235:genetics / Q000378:metabolism; D053586:Virus Internalization
D008562:Membrane Glycoproteins; D064370:Spike Glycoprotein, Coronavirus; D014759:Viral Envelope Proteins; C578557:spike glycoprotein, SARS-CoV; C578553:spike protein, mouse hepatitis virus