Receptor binding and priming of the spike protein of SARS-CoV-2 for membrane fusion

Infection with severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is initiated by virus binding to the ACE2 cell-surface receptors 1 – 4 , followed by fusion of the virus and cell membranes to release the virus genome into the cell. Both receptor binding and membrane fusion activities are...

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Vydané v:Nature (London) Ročník 588; číslo 7837; s. 327 - 330
Hlavní autori: Benton, Donald J., Wrobel, Antoni G., Xu, Pengqi, Roustan, Chloë, Martin, Stephen R., Rosenthal, Peter B., Skehel, John J., Gamblin, Steven J.
Médium: Journal Article
Jazyk:English
Vydavateľské údaje: London Nature Publishing Group UK 10.12.2020
Nature Publishing Group
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101/28
631/326/596/4130
631/535/1258/1259
82/80
ACE2
Angiotensin-converting enzyme 2
Angiotensin-Converting Enzyme 2 - chemistry
Angiotensin-Converting Enzyme 2 - metabolism
Angiotensin-Converting Enzyme 2 - ultrastructure
Binding
Binding sites
Binding sites (Biochemistry)
Cell membranes
Cell receptors
Cell surface
Cleavage
Coronaviruses
COVID-19
Cryoelectron Microscopy
Destabilization
Dissociation
Electron microscopy
Furin
Furin - metabolism
Fusion protein
Genomes
Glycoproteins
Health aspects
Humanities and Social Sciences
Humans
Membrane fusion
Membrane Fusion - physiology
Membrane proteins
Membranes
Microscopy
Models, Molecular
Monomers
multidisciplinary
Observations
Peptides
Physiological aspects
Post-translation
Priming
Protein Binding
Protein Folding
Protein Subunits - chemistry
Protein Subunits - metabolism
Proteins
Proteolysis
Receptors
Receptors, Coronavirus - chemistry
Receptors, Coronavirus - metabolism
Receptors, Coronavirus - ultrastructure
Science
Science (multidisciplinary)
Severe acute respiratory syndrome coronavirus 2
Species classification
Spike Glycoprotein, Coronavirus - chemistry
Spike Glycoprotein, Coronavirus - metabolism
Spike Glycoprotein, Coronavirus - ultrastructure
Spike protein
Trimers
Viral diseases
Viral proteins
Viruses
United Kingdom
ISSN:0028-0836, 1476-4687, 1476-4687
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Abstract Infection with severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is initiated by virus binding to the ACE2 cell-surface receptors 1 – 4 , followed by fusion of the virus and cell membranes to release the virus genome into the cell. Both receptor binding and membrane fusion activities are mediated by the virus spike glycoprotein 5 – 7 . As with other class-I membrane-fusion proteins, the spike protein is post-translationally cleaved, in this case by furin, into the S1 and S2 components that remain associated after cleavage 8 – 10 . Fusion activation after receptor binding is proposed to involve the exposure of a second proteolytic site (S2′), cleavage of which is required for the release of the fusion peptide 11 , 12 . Here we analyse the binding of ACE2 to the furin-cleaved form of the SARS-CoV-2 spike protein using cryo-electron microscopy. We classify ten different molecular species, including the unbound, closed spike trimer, the fully open ACE2-bound trimer and dissociated monomeric S1 bound to ACE2. The ten structures describe ACE2-binding events that destabilize the spike trimer, progressively opening up, and out, the individual S1 components. The opening process reduces S1 contacts and unshields the trimeric S2 core, priming the protein for fusion activation and dissociation of ACE2-bound S1 monomers. The structures also reveal refolding of an S1 subdomain after ACE2 binding that disrupts interactions with S2, which involves Asp614 13 – 15 and leads to the destabilization of the structure of S2 proximal to the secondary (S2′) cleavage site. Cryo-electron microscopy structures of consecutive binding events of ACE2 in complex with the spike protein of SARS-CoV-2 reveal the mechanisms of receptor binding by the spike protein and activation for membrane fusion by the spike protein of SARS-CoV-2.
AbstractList Infection with severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is initiated by virus binding to the ACE2 cell-surface receptors1-4, followed by fusion of the virus and cell membranes to release the virus genome into the cell. Both receptor binding and membrane fusion activities are mediated by the virus spike glycoprotein5-7. As with other class-I membrane-fusion proteins, the spike protein is post-translationally cleaved, in this case by furin, into the S1 and S2 components that remain associated after cleavage8-10. Fusion activation after receptor binding is proposed to involve the exposure of a second proteolytic site (S2'), cleavage of which is required for the release of the fusion peptide11,12. Here we analyse the binding of ACE2 to the furin-cleaved form of the SARS-CoV-2 spike protein using cryo-electron microscopy. We classify ten different molecular species, including the unbound, closed spike trimer, the fully open ACE2-bound trimer and dissociated monomeric S1 bound to ACE2. The ten structures describe ACE2-binding events that destabilize the spike trimer, progressively opening up, and out, the individual S1 components. The opening process reduces S1 contacts and unshields the trimeric S2 core, priming the protein for fusion activation and dissociation of ACE2-bound S1 monomers. The structures also reveal refolding of an S1 subdomain after ACE2 binding that disrupts interactions with S2, which involves Asp61413-15 and leads to the destabilization of the structure of S2 proximal to the secondary (S2') cleavage site.Infection with severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is initiated by virus binding to the ACE2 cell-surface receptors1-4, followed by fusion of the virus and cell membranes to release the virus genome into the cell. Both receptor binding and membrane fusion activities are mediated by the virus spike glycoprotein5-7. As with other class-I membrane-fusion proteins, the spike protein is post-translationally cleaved, in this case by furin, into the S1 and S2 components that remain associated after cleavage8-10. Fusion activation after receptor binding is proposed to involve the exposure of a second proteolytic site (S2'), cleavage of which is required for the release of the fusion peptide11,12. Here we analyse the binding of ACE2 to the furin-cleaved form of the SARS-CoV-2 spike protein using cryo-electron microscopy. We classify ten different molecular species, including the unbound, closed spike trimer, the fully open ACE2-bound trimer and dissociated monomeric S1 bound to ACE2. The ten structures describe ACE2-binding events that destabilize the spike trimer, progressively opening up, and out, the individual S1 components. The opening process reduces S1 contacts and unshields the trimeric S2 core, priming the protein for fusion activation and dissociation of ACE2-bound S1 monomers. The structures also reveal refolding of an S1 subdomain after ACE2 binding that disrupts interactions with S2, which involves Asp61413-15 and leads to the destabilization of the structure of S2 proximal to the secondary (S2') cleavage site.
Infection with severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is initiated by virus binding to the ACE2 cell-surface receptors.sup.1-4, followed by fusion of the virus and cell membranes to release the virus genome into the cell. Both receptor binding and membrane fusion activities are mediated by the virus spike glycoprotein.sup.5-7. As with other class-I membrane-fusion proteins, the spike protein is post-translationally cleaved, in this case by furin, into the S1 and S2 components that remain associated after cleavage.sup.8-10. Fusion activation after receptor binding is proposed to involve the exposure of a second proteolytic site (S2'), cleavage of which is required for the release of the fusion peptide.sup.11,12. Here we analyse the binding of ACE2 to the furin-cleaved form of the SARS-CoV-2 spike protein using cryo-electron microscopy. We classify ten different molecular species, including the unbound, closed spike trimer, the fully open ACE2-bound trimer and dissociated monomeric S1 bound to ACE2. The ten structures describe ACE2-binding events that destabilize the spike trimer, progressively opening up, and out, the individual S1 components. The opening process reduces S1 contacts and unshields the trimeric S2 core, priming the protein for fusion activation and dissociation of ACE2-bound S1 monomers. The structures also reveal refolding of an S1 subdomain after ACE2 binding that disrupts interactions with S2, which involves Asp614.sup.13-15 and leads to the destabilization of the structure of S2 proximal to the secondary (S2') cleavage site.
Infection with severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is initiated by virus binding to the ACE2 cell-surface receptors 1 – 4 , followed by fusion of the virus and cell membranes to release the virus genome into the cell. Both receptor binding and membrane fusion activities are mediated by the virus spike glycoprotein 5 – 7 . As with other class-I membrane-fusion proteins, the spike protein is post-translationally cleaved, in this case by furin, into the S1 and S2 components that remain associated after cleavage 8 – 10 . Fusion activation after receptor binding is proposed to involve the exposure of a second proteolytic site (S2′), cleavage of which is required for the release of the fusion peptide 11 , 12 . Here we analyse the binding of ACE2 to the furin-cleaved form of the SARS-CoV-2 spike protein using cryo-electron microscopy. We classify ten different molecular species, including the unbound, closed spike trimer, the fully open ACE2-bound trimer and dissociated monomeric S1 bound to ACE2. The ten structures describe ACE2-binding events that destabilize the spike trimer, progressively opening up, and out, the individual S1 components. The opening process reduces S1 contacts and unshields the trimeric S2 core, priming the protein for fusion activation and dissociation of ACE2-bound S1 monomers. The structures also reveal refolding of an S1 subdomain after ACE2 binding that disrupts interactions with S2, which involves Asp614 13 – 15 and leads to the destabilization of the structure of S2 proximal to the secondary (S2′) cleavage site. Cryo-electron microscopy structures of consecutive binding events of ACE2 in complex with the spike protein of SARS-CoV-2 reveal the mechanisms of receptor binding by the spike protein and activation for membrane fusion by the spike protein of SARS-CoV-2.
Infection with severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is initiated by virus binding to the ACE2 cell-surface receptors , followed by fusion of the virus and cell membranes to release the virus genome into the cell. Both receptor binding and membrane fusion activities are mediated by the virus spike glycoprotein . As with other class-I membrane-fusion proteins, the spike protein is post-translationally cleaved, in this case by furin, into the S1 and S2 components that remain associated after cleavage . Fusion activation after receptor binding is proposed to involve the exposure of a second proteolytic site (S2'), cleavage of which is required for the release of the fusion peptide . Here we analyse the binding of ACE2 to the furin-cleaved form of the SARS-CoV-2 spike protein using cryo-electron microscopy. We classify ten different molecular species, including the unbound, closed spike trimer, the fully open ACE2-bound trimer and dissociated monomeric S1 bound to ACE2. The ten structures describe ACE2-binding events that destabilize the spike trimer, progressively opening up, and out, the individual S1 components. The opening process reduces S1 contacts and unshields the trimeric S2 core, priming the protein for fusion activation and dissociation of ACE2-bound S1 monomers. The structures also reveal refolding of an S1 subdomain after ACE2 binding that disrupts interactions with S2, which involves Asp614 and leads to the destabilization of the structure of S2 proximal to the secondary (S2') cleavage site.
Infection with severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is initiated by virus binding to the ACE2 cell-surface receptors1–4, followed by fusion of the virus and cell membranes to release the virus genome into the cell. Both receptor binding and membrane fusion activities are mediated by the virus spike glycoprotein5–7. As with other class-I membrane-fusion proteins, the spike protein is post-translationally cleaved, in this case by furin, into the S1 and S2 components that remain associated after cleavage8–10. Fusion activation after receptor binding is proposed to involve the exposure of a second proteolytic site (S2′), cleavage of which is required for the release of the fusion peptide11,12. Here we analyse the binding of ACE2 to the furin-cleaved form of the SARS-CoV-2 spike protein using cryo-electron microscopy. We classify ten different molecular species, including the unbound, closed spike trimer, the fully open ACE2-bound trimer and dissociated monomeric S1 bound to ACE2. The ten structures describe ACE2-binding events that destabilize the spike trimer, progressively opening up, and out, the individual S1 components. The opening process reduces S1 contacts and unshields the trimeric S2 core, priming the protein for fusion activation and dissociation of ACE2-bound S1 monomers. The structures also reveal refolding of an S1 subdomain after ACE2 binding that disrupts interactions with S2, which involves Asp61413–15 and leads to the destabilization of the structure of S2 proximal to the secondary (S2′) cleavage site.
Infection with severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is initiated by virus binding to the ACE2 cell-surface receptors1-4, followed by fusion of the virus and cell membranes to release the virus genome into the cell. Both receptor binding and membrane fusion activities are mediated by the virus spike glycoprotein5-7. As with other class-I membrane-fusion proteins, the spike protein is post-translationally cleaved, in this case by furin, into the S1 and S2 components that remain associated after cleavage8-10. Fusion activation after receptor binding is proposed to involve the exposure of a second proteolytic site (S2'), cleavage of which is required for the release ofthe fusion peptide11,12. Here we analyse the binding of ACE2 to the furin-cleaved form of the SARS-CoV-2 spike protein using cryo-electron microscopy. We classify ten different molecular species, including the unbound, closed spike trimer, the fully open ACE2-bound trimer and dissociated monomeric S1 bound to ACE2. The ten structures describe ACE2-binding events that destabilize the spike trimer, progressively opening up, and out, the individual S1 components. The opening process reduces S1 contacts and unshields the trimeric S2 core, priming the protein for fusion activation and dissociation of ACE2-bound S1 monomers. The structures also reveal refolding of an S1 subdomain after ACE2 binding that disrupts interactions with S2, which involves Asp61413-15 and leads to the destabilization ofthe structure of S2 proximal to the secondary (S2') cleavage site.
Infection with severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is initiated by virus binding to the ACE2 cell-surface receptors.sup.1-4, followed by fusion of the virus and cell membranes to release the virus genome into the cell. Both receptor binding and membrane fusion activities are mediated by the virus spike glycoprotein.sup.5-7. As with other class-I membrane-fusion proteins, the spike protein is post-translationally cleaved, in this case by furin, into the S1 and S2 components that remain associated after cleavage.sup.8-10. Fusion activation after receptor binding is proposed to involve the exposure of a second proteolytic site (S2'), cleavage of which is required for the release of the fusion peptide.sup.11,12. Here we analyse the binding of ACE2 to the furin-cleaved form of the SARS-CoV-2 spike protein using cryo-electron microscopy. We classify ten different molecular species, including the unbound, closed spike trimer, the fully open ACE2-bound trimer and dissociated monomeric S1 bound to ACE2. The ten structures describe ACE2-binding events that destabilize the spike trimer, progressively opening up, and out, the individual S1 components. The opening process reduces S1 contacts and unshields the trimeric S2 core, priming the protein for fusion activation and dissociation of ACE2-bound S1 monomers. The structures also reveal refolding of an S1 subdomain after ACE2 binding that disrupts interactions with S2, which involves Asp614.sup.13-15 and leads to the destabilization of the structure of S2 proximal to the secondary (S2') cleavage site. Cryo-electron microscopy structures of consecutive binding events of ACE2 in complex with the spike protein of SARS-CoV-2 reveal the mechanisms of receptor binding by the spike protein and activation for membrane fusion by the spike protein of SARS-CoV-2.
Audience Academic
Author Xu, Pengqi
Rosenthal, Peter B.
Benton, Donald J.
Roustan, Chloë
Skehel, John J.
Martin, Stephen R.
Gamblin, Steven J.
Wrobel, Antoni G.
AuthorAffiliation 1 Strutural Biology of Disease Processes Laboratory, Francis Crick Institute, London, UK
4 Structural Biology Science Technology Platform, Francis Crick Institute, London, UK
2 Precision Medicine Center, The Seventh Affiliated Hospital, Sun Yat-sen University, Shenzhen, China
3 Francis Crick Institute, London, Uk
5 Structural Biology of Cells and Viruses Laboratory, Francis Crick Institute, London, UK
AuthorAffiliation_xml – name: 2 Precision Medicine Center, The Seventh Affiliated Hospital, Sun Yat-sen University, Shenzhen, China
– name: 3 Francis Crick Institute, London, Uk
– name: 4 Structural Biology Science Technology Platform, Francis Crick Institute, London, UK
– name: 1 Strutural Biology of Disease Processes Laboratory, Francis Crick Institute, London, UK
– name: 5 Structural Biology of Cells and Viruses Laboratory, Francis Crick Institute, London, UK
Author_xml – sequence: 1
  givenname: Donald J.
  orcidid: 0000-0001-6748-9339
  surname: Benton
  fullname: Benton, Donald J.
  email: donald.benton@crick.ac.uk
  organization: Strutural Biology of Disease Processes Laboratory, Francis Crick Institute
– sequence: 2
  givenname: Antoni G.
  orcidid: 0000-0002-6680-5587
  surname: Wrobel
  fullname: Wrobel, Antoni G.
  email: antoni.wrobel@crick.ac.uk
  organization: Strutural Biology of Disease Processes Laboratory, Francis Crick Institute
– sequence: 3
  givenname: Pengqi
  surname: Xu
  fullname: Xu, Pengqi
  organization: Precision Medicine Center, The Seventh Affiliated Hospital, Sun Yat-sen University, Francis Crick Institute
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  givenname: Chloë
  surname: Roustan
  fullname: Roustan, Chloë
  organization: Structural Biology Science Technology Platform, Francis Crick Institute
– sequence: 5
  givenname: Stephen R.
  surname: Martin
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  organization: Strutural Biology of Disease Processes Laboratory, Francis Crick Institute
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  givenname: Peter B.
  orcidid: 0000-0002-0387-2862
  surname: Rosenthal
  fullname: Rosenthal, Peter B.
  organization: Structural Biology of Cells and Viruses Laboratory, Francis Crick Institute
– sequence: 7
  givenname: John J.
  surname: Skehel
  fullname: Skehel, John J.
  organization: Strutural Biology of Disease Processes Laboratory, Francis Crick Institute
– sequence: 8
  givenname: Steven J.
  orcidid: 0000-0001-5331-639X
  surname: Gamblin
  fullname: Gamblin, Steven J.
  email: steve.gamblin@crick.ac.uk
  organization: Strutural Biology of Disease Processes Laboratory, Francis Crick Institute
BackLink https://www.ncbi.nlm.nih.gov/pubmed/32942285$$D View this record in MEDLINE/PubMed
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SSID ssj0005174
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Snippet Infection with severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is initiated by virus binding to the ACE2 cell-surface receptors 1 – 4 , followed...
Infection with severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is initiated by virus binding to the ACE2 cell-surface receptors , followed by...
Infection with severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is initiated by virus binding to the ACE2 cell-surface receptors.sup.1-4, followed...
Infection with severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is initiated by virus binding to the ACE2 cell-surface receptors1-4, followed by...
Infection with severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is initiated by virus binding to the ACE2 cell-surface receptors1–4, followed by...
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proquest
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springer
SourceType Open Access Repository
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Enrichment Source
Publisher
StartPage 327
SubjectTerms 101/28
631/326/596/4130
631/535/1258/1259
82/80
ACE2
Angiotensin-converting enzyme 2
Angiotensin-Converting Enzyme 2 - chemistry
Angiotensin-Converting Enzyme 2 - metabolism
Angiotensin-Converting Enzyme 2 - ultrastructure
Binding
Binding sites
Binding sites (Biochemistry)
Cell membranes
Cell receptors
Cell surface
Cleavage
Coronaviruses
COVID-19
Cryoelectron Microscopy
Destabilization
Dissociation
Electron microscopy
Furin
Furin - metabolism
Fusion protein
Genomes
Glycoproteins
Health aspects
Humanities and Social Sciences
Humans
Membrane fusion
Membrane Fusion - physiology
Membrane proteins
Membranes
Microscopy
Models, Molecular
Monomers
multidisciplinary
Observations
Peptides
Physiological aspects
Post-translation
Priming
Protein Binding
Protein Folding
Protein Subunits - chemistry
Protein Subunits - metabolism
Proteins
Proteolysis
Receptors
Receptors, Coronavirus - chemistry
Receptors, Coronavirus - metabolism
Receptors, Coronavirus - ultrastructure
Science
Science (multidisciplinary)
Severe acute respiratory syndrome coronavirus 2
Species classification
Spike Glycoprotein, Coronavirus - chemistry
Spike Glycoprotein, Coronavirus - metabolism
Spike Glycoprotein, Coronavirus - ultrastructure
Spike protein
Trimers
Viral diseases
Viral proteins
Viruses
Title Receptor binding and priming of the spike protein of SARS-CoV-2 for membrane fusion
URI https://link.springer.com/article/10.1038/s41586-020-2772-0
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https://pubmed.ncbi.nlm.nih.gov/PMC7116727
Volume 588
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