Significant redox insensitivity of the functions of the SARS-CoV spike glycoprotein - Comparison with HIV envelope

被引:38
作者
Lavillette, D
Barbouche, R
Yao, YX
Boson, B
Cosset, FL
Jones, IM
Fenouillet, E
机构
[1] Fac Med Nord, IFR Jean Roche, F-13015 Marseille, France
[2] Inst Federat Rech, Ecole Normale Super, INSERM, U758, F-69007 Lyon, France
[3] Inst Super Biotechnol Monastir, Monastir 5000, Tunisia
[4] Univ Reading, Sch Anim & Microbial Sci, Reading RG6 6AJ, Berks, England
基金
英国医学研究理事会;
关键词
D O I
10.1074/jbc.M512529200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The capacity of the surface glycoproteins of enveloped viruses to mediate virus/cell binding and membrane fusion requires a proper thiol/disulfide balance. Chemical manipulation of their redox state using reducing agents or free sulfhydryl reagents affects virus/cell interaction. Conversely, natural thiol/disulfide rearrangements often occur during the cell interaction to trigger fusogenicity, hence the virus entry. We examined the relationship between the redox state of the 20 cysteine residues of the SARS-CoV (severe acute respiratory syndrome coronavirus) Spike glycoprotein S1 subdomain and its functional properties. Mature S1 exhibited similar to 4 unpaired cysteines, and chemically reduced S1 displaying up to similar to 6 additional unpaired cysteines still bound ACE2 and enabled fusion. In addition, virus/cell membrane fusion occurred in the presence of sulfhydryl-blocking reagents and oxidoreductase inhibitors. Thus, in contrast to various viruses including HIV (human immunodeficiency virus) examined in parallel, the functions of the SARS-CoV Spike glycoprotein exhibit a significant and surprising independence of redox state, which may contribute to the wide host range of the virus. These data suggest clues for molecularly engineering vaccine immunogens.
引用
收藏
页码:9200 / 9204
页数:5
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