Structure-based design of prefusion-stabilized SARS-CoV-2 spikes
The development of therapeutic antibodies and vaccines against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is focused on the spike (S) protein that decorates the viral surface. A version of the spike ectodomain that includes two proline substitutions (S-2P) and stabilizes the prefus...
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| Published in | Science (American Association for the Advancement of Science) Vol. 369; no. 6510; pp. 1501 - 1505 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
The American Association for the Advancement of Science
18.09.2020
American Association for the Advancement of Science |
| Subjects | |
| Online Access | Get full text |
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| Abstract | The development of therapeutic antibodies and vaccines against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is focused on the spike (S) protein that decorates the viral surface. A version of the spike ectodomain that includes two proline substitutions (S-2P) and stabilizes the prefusion conformation has been used to determine high-resolution structures. However, even S-2P is unstable and difficult to produce in mammalian cells. Hsieh
et al.
characterized many individual and combined structure-guided substitutions and identified a variant, named HexaPro, that retains the prefusion conformation but shows higher expression than S-2P and can also withstand heating and freezing. This version of the protein is likely to be useful in the development of vaccines and diagnostics.
Science
, this issue p.
1501
The design of stabilizing mutations in the SARS-CoV-2 spike protein allows for high-yield production of a critical vaccine antigen.
The coronavirus disease 2019 (COVID-19) pandemic has led to accelerated efforts to develop therapeutics and vaccines. A key target of these efforts is the spike (S) protein, which is metastable and difficult to produce recombinantly. We characterized 100 structure-guided spike designs and identified 26 individual substitutions that increased protein yields and stability. Testing combinations of beneficial substitutions resulted in the identification of HexaPro, a variant with six beneficial proline substitutions exhibiting higher expression than its parental construct (by a factor of 10) as well as the ability to withstand heat stress, storage at room temperature, and three freeze-thaw cycles. A cryo–electron microscopy structure of HexaPro at a resolution of 3.2 angstroms confirmed that it retains the prefusion spike conformation. High-yield production of a stabilized prefusion spike protein will accelerate the development of vaccines and serological diagnostics for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). |
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| AbstractList | The coronavirus disease 2019 (COVID-19) pandemic has led to accelerated efforts to develop therapeutics and vaccines. A key target of these efforts is the spike (S) protein, which is metastable and difficult to produce recombinantly. We characterized 100 structure-guided spike designs and identified 26 individual substitutions that increased protein yields and stability. Testing combinations of beneficial substitutions resulted in the identification of HexaPro, a variant with six beneficial proline substitutions exhibiting higher expression than its parental construct (by a factor of 10) as well as the ability to withstand heat stress, storage at room temperature, and three freeze-thaw cycles. A cryo-electron microscopy structure of HexaPro at a resolution of 3.2 angstroms confirmed that it retains the prefusion spike conformation. High-yield production of a stabilized prefusion spike protein will accelerate the development of vaccines and serological diagnostics for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2).The coronavirus disease 2019 (COVID-19) pandemic has led to accelerated efforts to develop therapeutics and vaccines. A key target of these efforts is the spike (S) protein, which is metastable and difficult to produce recombinantly. We characterized 100 structure-guided spike designs and identified 26 individual substitutions that increased protein yields and stability. Testing combinations of beneficial substitutions resulted in the identification of HexaPro, a variant with six beneficial proline substitutions exhibiting higher expression than its parental construct (by a factor of 10) as well as the ability to withstand heat stress, storage at room temperature, and three freeze-thaw cycles. A cryo-electron microscopy structure of HexaPro at a resolution of 3.2 angstroms confirmed that it retains the prefusion spike conformation. High-yield production of a stabilized prefusion spike protein will accelerate the development of vaccines and serological diagnostics for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Stabilizing the prefusion SARS-CoV-2 spikeThe development of therapeutic antibodies and vaccines against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is focused on the spike (S) protein that decorates the viral surface. A version of the spike ectodomain that includes two proline substitutions (S-2P) and stabilizes the prefusion conformation has been used to determine high-resolution structures. However, even S-2P is unstable and difficult to produce in mammalian cells. Hsieh et al. characterized many individual and combined structure-guided substitutions and identified a variant, named HexaPro, that retains the prefusion conformation but shows higher expression than S-2P and can also withstand heating and freezing. This version of the protein is likely to be useful in the development of vaccines and diagnostics.Science, this issue p. 1501The coronavirus disease 2019 (COVID-19) pandemic has led to accelerated efforts to develop therapeutics and vaccines. A key target of these efforts is the spike (S) protein, which is metastable and difficult to produce recombinantly. We characterized 100 structure-guided spike designs and identified 26 individual substitutions that increased protein yields and stability. Testing combinations of beneficial substitutions resulted in the identification of HexaPro, a variant with six beneficial proline substitutions exhibiting higher expression than its parental construct (by a factor of 10) as well as the ability to withstand heat stress, storage at room temperature, and three freeze-thaw cycles. A cryo–electron microscopy structure of HexaPro at a resolution of 3.2 angstroms confirmed that it retains the prefusion spike conformation. High-yield production of a stabilized prefusion spike protein will accelerate the development of vaccines and serological diagnostics for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). The development of therapeutic antibodies and vaccines against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is focused on the spike (S) protein that decorates the viral surface. A version of the spike ectodomain that includes two proline substitutions (S-2P) and stabilizes the prefusion conformation has been used to determine high-resolution structures. However, even S-2P is unstable and difficult to produce in mammalian cells. Hsieh et al. characterized many individual and combined structure-guided substitutions and identified a variant, named HexaPro, that retains the prefusion conformation but shows higher expression than S-2P and can also withstand heating and freezing. This version of the protein is likely to be useful in the development of vaccines and diagnostics. Science , this issue p. 1501 The design of stabilizing mutations in the SARS-CoV-2 spike protein allows for high-yield production of a critical vaccine antigen. The coronavirus disease 2019 (COVID-19) pandemic has led to accelerated efforts to develop therapeutics and vaccines. A key target of these efforts is the spike (S) protein, which is metastable and difficult to produce recombinantly. We characterized 100 structure-guided spike designs and identified 26 individual substitutions that increased protein yields and stability. Testing combinations of beneficial substitutions resulted in the identification of HexaPro, a variant with six beneficial proline substitutions exhibiting higher expression than its parental construct (by a factor of 10) as well as the ability to withstand heat stress, storage at room temperature, and three freeze-thaw cycles. A cryo–electron microscopy structure of HexaPro at a resolution of 3.2 angstroms confirmed that it retains the prefusion spike conformation. High-yield production of a stabilized prefusion spike protein will accelerate the development of vaccines and serological diagnostics for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). The COVID-19 pandemic has led to accelerated efforts to develop therapeutics and vaccines. A key target of these efforts is the spike (S) protein, which is metastable and difficult to produce recombinantly. Here, we characterized 100 structure-guided spike designs and identified 26 individual substitutions that increased protein yields and stability. Testing combinations of beneficial substitutions resulted in the identification of HexaPro, a variant with six beneficial proline substitutions exhibiting ~10-fold higher expression than its parental construct and the ability to withstand heat stress, storage at room temperature, and three freeze-thaw cycles. A 3.2 Å-resolution cryo-EM structure of HexaPro confirmed that it retains the prefusion spike conformation. High-yield production of a stabilized prefusion spike protein will accelerate the development of vaccines and serological diagnostics for SARS-CoV-2. The coronavirus disease 2019 (COVID-19) pandemic has led to accelerated efforts to develop therapeutics and vaccines. A key target of these efforts is the spike (S) protein, which is metastable and difficult to produce recombinantly. We characterized 100 structure-guided spike designs and identified 26 individual substitutions that increased protein yields and stability. Testing combinations of beneficial substitutions resulted in the identification of HexaPro, a variant with six beneficial proline substitutions exhibiting higher expression than its parental construct (by a factor of 10) as well as the ability to withstand heat stress, storage at room temperature, and three freeze-thaw cycles. A cryo-electron microscopy structure of HexaPro at a resolution of 3.2 angstroms confirmed that it retains the prefusion spike conformation. High-yield production of a stabilized prefusion spike protein will accelerate the development of vaccines and serological diagnostics for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). |
| Author | Schaub, Jeffrey M. DiVenere, Andrea M. Javanmardi, Kamyab Lee, Alison G. Hjorth, Christy K. Maynard, Jennifer A. Ippolito, Gregory C. Nguyen, Annalee W. Wang, Nianshuang Liu, Yutong Park, Juyeon Finkelstein, Ilya J. Goldsmith, Jory A. Wrapp, Daniel Byrne, Patrick O. Lavinder, Jason J. Johnson, Nicole V. McLellan, Jason S. Chou, Chia-Wei Hsieh, Ching-Lin Kuo, Hung-Che Ludes-Meyers, John Amengor, Dzifa Le, Kevin C. |
| Author_xml | – sequence: 1 givenname: Ching-Lin orcidid: 0000-0002-3665-5717 surname: Hsieh fullname: Hsieh, Ching-Lin organization: Department of Molecular Biosciences, University of Texas, Austin, TX 78712, USA – sequence: 2 givenname: Jory A. surname: Goldsmith fullname: Goldsmith, Jory A. organization: Department of Molecular Biosciences, University of Texas, Austin, TX 78712, USA – sequence: 3 givenname: Jeffrey M. orcidid: 0000-0002-1130-2675 surname: Schaub fullname: Schaub, Jeffrey M. organization: Department of Molecular Biosciences, University of Texas, Austin, TX 78712, USA – sequence: 4 givenname: Andrea M. surname: DiVenere fullname: DiVenere, Andrea M. organization: Department of Chemical Engineering, University of Texas, Austin, TX 78712, USA – sequence: 5 givenname: Hung-Che surname: Kuo fullname: Kuo, Hung-Che organization: Department of Molecular Biosciences, University of Texas, Austin, TX 78712, USA – sequence: 6 givenname: Kamyab surname: Javanmardi fullname: Javanmardi, Kamyab organization: Department of Molecular Biosciences, University of Texas, Austin, TX 78712, USA – sequence: 7 givenname: Kevin C. orcidid: 0000-0001-5098-7737 surname: Le fullname: Le, Kevin C. organization: Department of Chemical Engineering, University of Texas, Austin, TX 78712, USA – sequence: 8 givenname: Daniel orcidid: 0000-0002-0538-9647 surname: Wrapp fullname: Wrapp, Daniel organization: Department of Molecular Biosciences, University of Texas, Austin, TX 78712, USA – sequence: 9 givenname: Alison G. surname: Lee fullname: Lee, Alison G. organization: Department of Molecular Biosciences, University of Texas, Austin, TX 78712, USA – sequence: 10 givenname: Yutong orcidid: 0000-0003-0626-8094 surname: Liu fullname: Liu, Yutong organization: Department of Chemical Engineering, University of Texas, Austin, TX 78712, USA – sequence: 11 givenname: Chia-Wei orcidid: 0000-0001-9618-338X surname: Chou fullname: Chou, Chia-Wei organization: Department of Molecular Biosciences, University of Texas, Austin, TX 78712, USA – sequence: 12 givenname: Patrick O. orcidid: 0000-0002-6462-8951 surname: Byrne fullname: Byrne, Patrick O. organization: Department of Molecular Biosciences, University of Texas, Austin, TX 78712, USA – sequence: 13 givenname: Christy K. surname: Hjorth fullname: Hjorth, Christy K. organization: Department of Molecular Biosciences, University of Texas, Austin, TX 78712, USA – sequence: 14 givenname: Nicole V. orcidid: 0000-0003-4351-125X surname: Johnson fullname: Johnson, Nicole V. organization: Department of Molecular Biosciences, University of Texas, Austin, TX 78712, USA – sequence: 15 givenname: John surname: Ludes-Meyers fullname: Ludes-Meyers, John organization: Department of Molecular Biosciences, University of Texas, Austin, TX 78712, USA – sequence: 16 givenname: Annalee W. orcidid: 0000-0003-1268-7164 surname: Nguyen fullname: Nguyen, Annalee W. organization: Department of Chemical Engineering, University of Texas, Austin, TX 78712, USA – sequence: 17 givenname: Juyeon orcidid: 0000-0001-9549-4645 surname: Park fullname: Park, Juyeon organization: Department of Molecular Biosciences, University of Texas, Austin, TX 78712, USA – sequence: 18 givenname: Nianshuang surname: Wang fullname: Wang, Nianshuang organization: Department of Molecular Biosciences, University of Texas, Austin, TX 78712, USA – sequence: 19 givenname: Dzifa orcidid: 0000-0001-5705-3259 surname: Amengor fullname: Amengor, Dzifa organization: Department of Molecular Biosciences, University of Texas, Austin, TX 78712, USA – sequence: 20 givenname: Jason J. orcidid: 0000-0001-6044-1332 surname: Lavinder fullname: Lavinder, Jason J. organization: Department of Molecular Biosciences, University of Texas, Austin, TX 78712, USA., Department of Chemical Engineering, University of Texas, Austin, TX 78712, USA – sequence: 21 givenname: Gregory C. orcidid: 0000-0002-7565-7002 surname: Ippolito fullname: Ippolito, Gregory C. organization: Department of Molecular Biosciences, University of Texas, Austin, TX 78712, USA., Department of Oncology, Dell Medical School, University of Texas, Austin, TX 78712, USA – sequence: 22 givenname: Jennifer A. orcidid: 0000-0002-0363-8486 surname: Maynard fullname: Maynard, Jennifer A. organization: Department of Chemical Engineering, University of Texas, Austin, TX 78712, USA – sequence: 23 givenname: Ilya J. orcidid: 0000-0002-9371-2431 surname: Finkelstein fullname: Finkelstein, Ilya J. organization: Department of Molecular Biosciences, University of Texas, Austin, TX 78712, USA., Center for Systems and Synthetic Biology, University of Texas, Austin, TX 78712, USA – sequence: 24 givenname: Jason S. orcidid: 0000-0003-3991-542X surname: McLellan fullname: McLellan, Jason S. organization: Department of Molecular Biosciences, University of Texas, Austin, TX 78712, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/32703906$$D View this record in MEDLINE/PubMed |
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| Snippet | The development of therapeutic antibodies and vaccines against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is focused on the spike (S) protein... The coronavirus disease 2019 (COVID-19) pandemic has led to accelerated efforts to develop therapeutics and vaccines. A key target of these efforts is the... Stabilizing the prefusion SARS-CoV-2 spikeThe development of therapeutic antibodies and vaccines against severe acute respiratory syndrome coronavirus 2... The COVID-19 pandemic has led to accelerated efforts to develop therapeutics and vaccines. A key target of these efforts is the spike (S) protein, which is... |
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| SubjectTerms | Amino Acid Substitution Antibodies Betacoronavirus - chemistry Biochem Coronaviridae Coronavirus Infections - prevention & control Coronaviruses COVID-19 COVID-19 Vaccines Cryoelectron Microscopy Freeze thaw cycles Freeze-thaw durability Freeze-thawing Freezing Heat stress Heat tolerance Humans Pandemics Proline Proline - chemistry Protein Domains Protein Stability Proteins Respiratory diseases Room temperature SARS-CoV-2 Severe acute respiratory syndrome coronavirus 2 Spike Glycoprotein, Coronavirus - chemistry Vaccines Viral diseases Viral Vaccines - chemistry Virology |
| Title | Structure-based design of prefusion-stabilized SARS-CoV-2 spikes |
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