Structure-guided covalent stabilization of coronavirus spike glycoprotein trimers in the closed conformation

SARS-CoV-2 is the causative agent of the COVID-19 pandemic, with 10 million infections and more than 500,000 fatalities by June 2020. To initiate infection, the SARS-CoV-2 spike (S) glycoprotein promotes attachment to the host cell surface and fusion of the viral and host membranes. Prefusion SARS-C...

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Published inNature structural & molecular biology Vol. 27; no. 10; pp. 942 - 949
Main Authors McCallum, Matthew, Walls, Alexandra C., Bowen, John E., Corti, Davide, Veesler, David
Format Journal Article
LanguageEnglish
Published New York Nature Publishing Group US 01.10.2020
Nature Publishing Group
Subjects
101/28
631/326/596/4130
631/535/1258/1259
Antibodies, Monoclonal - metabolism
Antibodies, Neutralizing - metabolism
Betacoronavirus - chemistry
Betacoronavirus - genetics
Betacoronavirus - immunology
Betacoronavirus - metabolism
Biochemistry
Biological Microscopy
Biomedical and Life Sciences
Causes of
Conformation
Coronaviruses
Cryoelectron Microscopy
Disulfides - chemistry
Electrophoresis, Polyacrylamide Gel
Enzyme-Linked Immunosorbent Assay
Epidemics
Genetic aspects
Glycoproteins
Health aspects
Humans
Life Sciences
Membrane Biology
Models, Molecular
Mutation
Properties
Protein Conformation
Protein Domains
Protein Engineering
Protein Multimerization
Protein Stability
Protein Structure
Proteins
SARS-CoV-2
Spike Glycoprotein, Coronavirus - chemistry
Spike Glycoprotein, Coronavirus - genetics
Spike Glycoprotein, Coronavirus - immunology
Spike Glycoprotein, Coronavirus - metabolism
United States
Virulence (Microbiology)
United States
Online AccessGet full text

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Abstract SARS-CoV-2 is the causative agent of the COVID-19 pandemic, with 10 million infections and more than 500,000 fatalities by June 2020. To initiate infection, the SARS-CoV-2 spike (S) glycoprotein promotes attachment to the host cell surface and fusion of the viral and host membranes. Prefusion SARS-CoV-2 S is the main target of neutralizing antibodies and the focus of vaccine design. However, its limited stability and conformational dynamics are limiting factors for developing countermeasures against this virus. We report here the design of a construct corresponding to the prefusion SARS-CoV-2 S ectodomain trimer, covalently stabilized by a disulfide bond in the closed conformation. Structural and antigenicity analyses show we successfully shut S in the closed state without otherwise altering its architecture. We demonstrate that this strategy is applicable to other β-coronaviruses, such as SARS-CoV and MERS-CoV, and might become an important tool for structural biology, serology, vaccine design and immunology studies. The conformational dynamics of SARS-CoV-2 spike are constrained by engineering a disulfide bond that locks the protein in a closed conformation, a strategy that was also applied to SARS-CoV and MERS-CoV.
AbstractList SARS-CoV-2 is the causative agent of the COVID-19 pandemic, with 10 million infections and more than 500,000 fatalities by June 2020. To initiate infection, the SARS-CoV-2 spike (S) glycoprotein promotes attachment to the host cell surface and fusion of the viral and host membranes. Prefusion SARS-CoV-2 S is the main target of neutralizing antibodies and the focus of vaccine design. However, its limited stability and conformational dynamics are limiting factors for developing countermeasures against this virus. We report here the design of a construct corresponding to the prefusion SARS-CoV-2 S ectodomain trimer, covalently stabilized by a disulfide bond in the closed conformation. Structural and antigenicity analyses show we successfully shut S in the closed state without otherwise altering its architecture. We demonstrate that this strategy is applicable to other [beta]-coronaviruses, such as SARS-CoV and MERS-CoV, and might become an important tool for structural biology, serology, vaccine design and immunology studies.
SARS-CoV-2 is the causative agent of the COVID-19 pandemic, with 10 million infections and more than 500,000 fatalities by June 2020. To initiate infection, the SARS-CoV-2 spike (S) glycoprotein promotes attachment to the host cell surface and fusion of the viral and host membranes. Prefusion SARS-CoV-2 S is the main target of neutralizing antibodies and the focus of vaccine design. However, its limited stability and conformational dynamics are limiting factors for developing countermeasures against this virus. We report here the design of a construct corresponding to the prefusion SARS-CoV-2 S ectodomain trimer, covalently stabilized by a disulfide bond in the closed conformation. Structural and antigenicity analyses show we successfully shut S in the closed state without otherwise altering its architecture. We demonstrate that this strategy is applicable to other β-coronaviruses, such as SARS-CoV and MERS-CoV, and might become an important tool for structural biology, serology, vaccine design and immunology studies.
SARS-CoV-2 is the causative agent of the COVID-19 pandemic, with 10 million infections and more than 500,000 fatalities by June 2020. To initiate infection, the SARS-CoV-2 spike (S) glycoprotein promotes attachment to the host cell surface and fusion of the viral and host membranes. Prefusion SARS-CoV-2 S is the main target of neutralizing antibodies and the focus of vaccine design. However, its limited stability and conformational dynamics are limiting factors for developing countermeasures against this virus. We report here the design of a construct corresponding to the prefusion SARS-CoV-2 S ectodomain trimer, covalently stabilized by a disulfide bond in the closed conformation. Structural and antigenicity analyses show we successfully shut S in the closed state without otherwise altering its architecture. We demonstrate that this strategy is applicable to other β-coronaviruses, such as SARS-CoV and MERS-CoV, and might become an important tool for structural biology, serology, vaccine design and immunology studies.SARS-CoV-2 is the causative agent of the COVID-19 pandemic, with 10 million infections and more than 500,000 fatalities by June 2020. To initiate infection, the SARS-CoV-2 spike (S) glycoprotein promotes attachment to the host cell surface and fusion of the viral and host membranes. Prefusion SARS-CoV-2 S is the main target of neutralizing antibodies and the focus of vaccine design. However, its limited stability and conformational dynamics are limiting factors for developing countermeasures against this virus. We report here the design of a construct corresponding to the prefusion SARS-CoV-2 S ectodomain trimer, covalently stabilized by a disulfide bond in the closed conformation. Structural and antigenicity analyses show we successfully shut S in the closed state without otherwise altering its architecture. We demonstrate that this strategy is applicable to other β-coronaviruses, such as SARS-CoV and MERS-CoV, and might become an important tool for structural biology, serology, vaccine design and immunology studies.
SARS-CoV-2 is the causative agent of the COVID-19 pandemic, with 10 million infections and more than 500,000 fatalities by June 2020. To initiate infection, the SARS-CoV-2 spike (S) glycoprotein promotes attachment to the host cell surface and fusion of the viral and host membranes. Prefusion SARS-CoV-2 S is the main target of neutralizing antibodies and the focus of vaccine design. However, its limited stability and conformational dynamics are limiting factors for developing countermeasures against this virus. We report here the design of a construct corresponding to the prefusion SARS-CoV-2 S ectodomain trimer, covalently stabilized by a disulfide bond in the closed conformation. Structural and antigenicity analyses show we successfully shut S in the closed state without otherwise altering its architecture. We demonstrate that this strategy is applicable to other β-coronaviruses, such as SARS-CoV and MERS-CoV, and might become an important tool for structural biology, serology, vaccine design and immunology studies. The conformational dynamics of SARS-CoV-2 spike are constrained by engineering a disulfide bond that locks the protein in a closed conformation, a strategy that was also applied to SARS-CoV and MERS-CoV.
SARS-CoV-2 is the causative agent of the COVID-19 pandemic, with 10 million infections and more than 500,000 fatalities by June 2020. To initiate infection, the SARS-CoV-2 spike (S) glycoprotein promotes attachment to the host cell surface and fusion of the viral and host membranes. Prefusion SARS-CoV-2 S is the main target of neutralizing antibodies and the focus of vaccine design. However, its limited stability and conformational dynamics are limiting factors for developing countermeasures against this virus. We report here the design of a construct corresponding to the prefusion SARS-CoV-2 S ectodomain trimer, covalently stabilized by a disulfide bond in the closed conformation. Structural and antigenicity analyses show we successfully shut S in the closed state without otherwise altering its architecture. We demonstrate that this strategy is applicable to other [beta]-coronaviruses, such as SARS-CoV and MERS-CoV, and might become an important tool for structural biology, serology, vaccine design and immunology studies. The conformational dynamics of SARS-CoV-2 spike are constrained by engineering a disulfide bond that locks the protein in a closed conformation, a strategy that was also applied to SARS-CoV and MERS-CoV.
Audience Academic
Author Bowen, John E.
Corti, Davide
Veesler, David
Walls, Alexandra C.
McCallum, Matthew
Author_xml – sequence: 1
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  surname: McCallum
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  fullname: Walls, Alexandra C.
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  orcidid: 0000-0002-6019-8675
  surname: Veesler
  fullname: Veesler, David
  email: dveesler@uw.edu
  organization: Department of Biochemistry, University of Washington
BackLink https://www.ncbi.nlm.nih.gov/pubmed/32753755$$D View this record in MEDLINE/PubMed
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Snippet SARS-CoV-2 is the causative agent of the COVID-19 pandemic, with 10 million infections and more than 500,000 fatalities by June 2020. To initiate infection,...
SARS-CoV-2 is the causative agent of the COVID-19 pandemic, with 10 million infections and more than 500,000 fatalities by June 2020. To initiate infection,...
SourceID pubmedcentral
proquest
gale
pubmed
crossref
springer
SourceType Open Access Repository
Aggregation Database
Index Database
Enrichment Source
Publisher
StartPage 942
SubjectTerms 101/28
631/326/596/4130
631/535/1258/1259
Antibodies, Monoclonal - metabolism
Antibodies, Neutralizing - metabolism
Betacoronavirus - chemistry
Betacoronavirus - genetics
Betacoronavirus - immunology
Betacoronavirus - metabolism
Biochemistry
Biological Microscopy
Biomedical and Life Sciences
Causes of
Conformation
Coronaviruses
Cryoelectron Microscopy
Disulfides - chemistry
Electrophoresis, Polyacrylamide Gel
Enzyme-Linked Immunosorbent Assay
Epidemics
Genetic aspects
Glycoproteins
Health aspects
Humans
Life Sciences
Membrane Biology
Models, Molecular
Mutation
Properties
Protein Conformation
Protein Domains
Protein Engineering
Protein Multimerization
Protein Stability
Protein Structure
Proteins
SARS-CoV-2
Spike Glycoprotein, Coronavirus - chemistry
Spike Glycoprotein, Coronavirus - genetics
Spike Glycoprotein, Coronavirus - immunology
Spike Glycoprotein, Coronavirus - metabolism
United States
Virulence (Microbiology)
Title Structure-guided covalent stabilization of coronavirus spike glycoprotein trimers in the closed conformation
URI https://link.springer.com/article/10.1038/s41594-020-0483-8
https://www.ncbi.nlm.nih.gov/pubmed/32753755
https://www.proquest.com/docview/2430666375
https://pubmed.ncbi.nlm.nih.gov/PMC7541350
Volume 27
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