Significant redox insensitivity of the functions of the SARS-CoV spike glycoprotein: comparison with HIV envelope.
Identifieur interne : 000302 ( France/Analysis ); précédent : 000301; suivant : 000303Significant redox insensitivity of the functions of the SARS-CoV spike glycoprotein: comparison with HIV envelope.
Auteurs : Dimitri Lavillette [France] ; Rym Barbouche ; Yongxiu Yao ; Bertrand Boson ; François-Loïc Cosset ; Ian M. Jones ; Emmanuel FenouilletSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2006.
Descripteurs français
- KwdFr :
- Antigènes du VIH (), Antigènes viraux, Cellules épithéliales, Cystéine (), Fusion membranaire (physiologie), Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Humains, Oxydoréduction, Pliage des protéines, Protéines de l'enveloppe virale (), Techniques de culture cellulaire, Thiols (analyse), Vaccins antiviraux, Virus du SRAS (pathogénicité).
- MESH :
- analyse : Thiols.
- pathogénicité : Virus du SRAS.
- physiologie : Fusion membranaire.
- Antigènes du VIH, Antigènes viraux, Cellules épithéliales, Cystéine, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Humains, Oxydoréduction, Pliage des protéines, Protéines de l'enveloppe virale, Techniques de culture cellulaire, Vaccins antiviraux.
English descriptors
- KwdEn :
- Antigens, Viral, Cell Culture Techniques, Cysteine (chemistry), Epithelial Cells, HIV Antigens (chemistry), Humans, Membrane Fusion (physiology), Membrane Glycoproteins (chemistry), Oxidation-Reduction, Protein Folding, SARS Virus (pathogenicity), Spike Glycoprotein, Coronavirus, Sulfhydryl Compounds (analysis), Viral Envelope Proteins (chemistry), Viral Vaccines.
- MESH :
- chemical , analysis : Sulfhydryl Compounds.
- chemical , chemistry : Cysteine, HIV Antigens, Membrane Glycoproteins, Viral Envelope Proteins.
- chemical : Antigens, Viral, Spike Glycoprotein, Coronavirus, Viral Vaccines.
- pathogenicity : SARS Virus.
- physiology : Membrane Fusion.
- Cell Culture Techniques, Epithelial Cells, Humans, Oxidation-Reduction, Protein Folding.
Abstract
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 approximately 4 unpaired cysteines, and chemically reduced S1 displaying up to approximately 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.
Url:
DOI: 10.1074/jbc.M512529200
PubMed: 16418166
Affiliations:
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pubmed:16418166Le document en format XML
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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 approximately 4 unpaired cysteines, and chemically reduced S1 displaying up to approximately 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.</div></front></TEI><affiliations><list><country><li>France</li></country><region><li>Auvergne-Rhône-Alpes</li><li>Rhône-Alpes</li></region><settlement><li>Lyon</li></settlement></list><tree><noCountry><name sortKey="Barbouche, Rym" sort="Barbouche, Rym" uniqKey="Barbouche R" first="Rym" last="Barbouche">Rym Barbouche</name><name sortKey="Boson, Bertrand" sort="Boson, Bertrand" uniqKey="Boson B" first="Bertrand" last="Boson">Bertrand Boson</name><name sortKey="Cosset, Francois Loic" sort="Cosset, Francois Loic" uniqKey="Cosset F" first="François-Loïc" last="Cosset">François-Loïc Cosset</name><name sortKey="Fenouillet, Emmanuel" sort="Fenouillet, Emmanuel" uniqKey="Fenouillet E" first="Emmanuel" last="Fenouillet">Emmanuel Fenouillet</name><name sortKey="Jones, Ian M" sort="Jones, Ian M" uniqKey="Jones I" first="Ian M" last="Jones">Ian M. Jones</name><name sortKey="Yao, Yongxiu" sort="Yao, Yongxiu" uniqKey="Yao Y" first="Yongxiu" last="Yao">Yongxiu Yao</name></noCountry><country name="France"><region name="Auvergne-Rhône-Alpes"><name sortKey="Lavillette, Dimitri" sort="Lavillette, Dimitri" uniqKey="Lavillette D" first="Dimitri" last="Lavillette">Dimitri Lavillette</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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