GxxxG motif of severe acute respiratory syndrome coronavirus spike glycoprotein transmembrane domain is not involved in trimerization and is not important for entry

被引:7
作者
Corver, Jeroen [1 ]
Broer, Rene [1 ]
van Kasteren, Puck [1 ]
Spaan, Willy [1 ]
机构
[1] Leiden Univ, Med Ctr, Dept Med Microbiol, Ctr Infect Dis, NL-2300 RC Leiden, Netherlands
关键词
D O I
10.1128/JVI.00014-07
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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.
引用
收藏
页码:8352 / 8355
页数:4
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