GxxxG motif of severe acute respiratory syndrome coronavirus spike glycoprotein transmembrane domain is not involved in trimerization and is not important for entry
Identifieur interne : 000652 ( PascalFrancis/Curation ); précédent : 000651; suivant : 000653GxxxG motif of severe acute respiratory syndrome coronavirus spike glycoprotein transmembrane domain is not involved in trimerization and is not important for entry
Auteurs : Jeroen Corver [Pays-Bas] ; Rene Broer [Pays-Bas] ; Puck Van Kasteren [Pays-Bas] ; Willy Spaan [Pays-Bas]Source :
- Journal of virology [ 0022-538X ] ; 2007.
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- Pascal (Inist)
English descriptors
- KwdEn :
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.
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