Interaction of severe acute respiratory syndrome-coronavirus and NL63 coronavirus spike proteins with angiotensin converting enzyme-2

被引:57
|
作者
Mathewson, Alison C. [1 ]
Bishop, Alexandra [1 ]
Yao, Yongxiu [1 ]
Kemp, Fred [1 ]
Ren, Junyuan [1 ]
Chen, Hongying [1 ]
Xu, Xiaodong [1 ]
Berkhout, Ben [2 ]
van der Hoek, La [2 ]
Jones, Ian M. [1 ]
机构
[1] Univ Reading, Sch Biol Sci, Reading RG6 6AJ, Berks, England
[2] Univ Amsterdam, Acad Med Ctr, Ctr Infect & Immun Amsterdam CINIMA, Dept Med Microbiol,Lab Expt Virol, NL-1105 AZ Amsterdam, Netherlands
来源
基金
英国生物技术与生命科学研究理事会; 英国医学研究理事会;
关键词
D O I
10.1099/vir.0.2008/003962-0
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Although in different groups, the coronaviruses severe acute respiratory syndrome-coronavirus (SARS-CoV) and NL63 use the same receptor, angiotensin converting enzyme (ACE)-2, for entry into the host cell. Despite this common receptor, the consequence of entry is very different; severe respiratory distress in the case of SARS-CoV but frequently only a mild respiratory infection for NL63. Using a wholly recombinant system, we have investigated the ability of each virus receptor-binding protein, spike or S protein, to bind to ACE-2 in solution and on the cell surface. In both assays, we find that the NL63 S protein has a weaker interaction with ACE-2 than the SARS-CoV S protein, particularly in solution binding, but the residues required for contact are similar. We also confirm that the ACE-2-binding site of NL63 S lies between residues 190 and 739. A lower-affinity interaction with ACE-2 might partly explain the different pathological consequences of infection by SARS-CoV and NL63.
引用
收藏
页码:2741 / 2745
页数:5
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