The Architecture of Inactivated SARS-CoV-2 with Postfusion Spikes Revealed by Cryo-EM and Cryo-ET
The ongoing global pandemic of coronavirus disease 2019 (COVID-19) resulted from the outbreak of SARS-CoV-2 in December 2019. Currently, multiple efforts are being made to rapidly develop vaccines and treatments to fight COVID-19. Current vaccine candidates use inactivated SARS-CoV-2 viruses; theref...
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| Published in | Structure (London) Vol. 28; no. 11; pp. 1218 - 1224.e4 |
|---|---|
| Main Authors | , , , , , , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Ltd
03.11.2020
Cell Press |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0969-2126 1878-4186 1878-4186 |
| DOI | 10.1016/j.str.2020.10.001 |
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| Abstract | The ongoing global pandemic of coronavirus disease 2019 (COVID-19) resulted from the outbreak of SARS-CoV-2 in December 2019. Currently, multiple efforts are being made to rapidly develop vaccines and treatments to fight COVID-19. Current vaccine candidates use inactivated SARS-CoV-2 viruses; therefore, it is important to understand the architecture of inactivated SARS-CoV-2. We have genetically and structurally characterized β-propiolactone-inactivated viruses from a propagated and purified clinical strain of SARS-CoV-2. We observed that the virus particles are roughly spherical or moderately pleiomorphic. Although a small fraction of prefusion spikes are found, most spikes appear nail shaped, thus resembling a postfusion state, where the S1 protein of the spike has disassociated from S2. Cryoelectron tomography and subtomogram averaging of these spikes yielded a density map that closely matches the overall structure of the SARS-CoV postfusion spike and its corresponding glycosylation site. Our findings have major implications for SARS-CoV-2 vaccine design, especially those using inactivated viruses.
[Display omitted]
•β-propiolactone-inactivated SARS-CoV-2 viruses display postfusion spikes•Cryo-ET structure of SARS-CoV-2 postfusion spikes was determined at 11 Å resolution•This study calls for crucial structural characterization of vaccine candidates
Several vaccine candidates using inactivated SARS-CoV-2 viruses are under development. Liu et al. used state-of-the-art cryoelectron microscopy technologies to characterize the architecture of inactivated SARS-CoV-2 viruses. They found that the viral spikes are mostly in a postfusion state, which is not desirable for vaccine development. |
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| AbstractList | The ongoing global pandemic of coronavirus disease 2019 (COVID-19) resulted from the outbreak of SARS-CoV-2 in December 2019. Currently, multiple efforts are being made to rapidly develop vaccines and treatments to fight COVID-19. Current vaccine candidates use inactivated SARS-CoV-2 viruses; therefore, it is important to understand the architecture of inactivated SARS-CoV-2. We have genetically and structurally characterized β-propiolactone-inactivated viruses from a propagated and purified clinical strain of SARS-CoV-2. We observed that the virus particles are roughly spherical or moderately pleiomorphic. Although a small fraction of prefusion spikes are found, most spikes appear nail shaped, thus resembling a postfusion state, where the S1 protein of the spike has disassociated from S2. Cryoelectron tomography and subtomogram averaging of these spikes yielded a density map that closely matches the overall structure of the SARS-CoV postfusion spike and its corresponding glycosylation site. Our findings have major implications for SARS-CoV-2 vaccine design, especially those using inactivated viruses.
•
β-propiolactone-inactivated SARS-CoV-2 viruses display postfusion spikes
•
Cryo-ET structure of SARS-CoV-2 postfusion spikes was determined at 11 Å resolution
•
This study calls for crucial structural characterization of vaccine candidates
Several vaccine candidates using inactivated SARS-CoV-2 viruses are under development. Liu et al. used state-of-the-art cryoelectron microscopy technologies to characterize the architecture of inactivated SARS-CoV-2 viruses. They found that the viral spikes are mostly in a postfusion state, which is not desirable for vaccine development. The ongoing global pandemic of coronavirus disease 2019 (COVID-19) resulted from the outbreak of SARS-CoV-2 in December 2019. Currently, multiple efforts are being made to rapidly develop vaccines and treatments to fight COVID-19. Current vaccine candidates use inactivated SARS-CoV-2 viruses; therefore, it is important to understand the architecture of inactivated SARS-CoV-2. We have genetically and structurally characterized β-propiolactone-inactivated viruses from a propagated and purified clinical strain of SARS-CoV-2. We observed that the virus particles are roughly spherical or moderately pleiomorphic. Although a small fraction of prefusion spikes are found, most spikes appear nail shaped, thus resembling a postfusion state, where the S1 protein of the spike has disassociated from S2. Cryoelectron tomography and subtomogram averaging of these spikes yielded a density map that closely matches the overall structure of the SARS-CoV postfusion spike and its corresponding glycosylation site. Our findings have major implications for SARS-CoV-2 vaccine design, especially those using inactivated viruses.The ongoing global pandemic of coronavirus disease 2019 (COVID-19) resulted from the outbreak of SARS-CoV-2 in December 2019. Currently, multiple efforts are being made to rapidly develop vaccines and treatments to fight COVID-19. Current vaccine candidates use inactivated SARS-CoV-2 viruses; therefore, it is important to understand the architecture of inactivated SARS-CoV-2. We have genetically and structurally characterized β-propiolactone-inactivated viruses from a propagated and purified clinical strain of SARS-CoV-2. We observed that the virus particles are roughly spherical or moderately pleiomorphic. Although a small fraction of prefusion spikes are found, most spikes appear nail shaped, thus resembling a postfusion state, where the S1 protein of the spike has disassociated from S2. Cryoelectron tomography and subtomogram averaging of these spikes yielded a density map that closely matches the overall structure of the SARS-CoV postfusion spike and its corresponding glycosylation site. Our findings have major implications for SARS-CoV-2 vaccine design, especially those using inactivated viruses. The ongoing global pandemic of coronavirus disease 2019 (COVID-19) resulted from the outbreak of SARS-CoV-2 in December 2019. Currently, multiple efforts are being made to rapidly develop vaccines and treatments to fight COVID-19. Current vaccine candidates use inactivated SARS-CoV-2 viruses; therefore, it is important to understand the architecture of inactivated SARS-CoV-2. We have genetically and structurally characterized β-propiolactone-inactivated viruses from a propagated and purified clinical strain of SARS-CoV-2. We observed that the virus particles are roughly spherical or moderately pleiomorphic. Although a small fraction of prefusion spikes are found, most spikes appear nail shaped, thus resembling a postfusion state, where the S1 protein of the spike has disassociated from S2. Cryoelectron tomography and subtomogram averaging of these spikes yielded a density map that closely matches the overall structure of the SARS-CoV postfusion spike and its corresponding glycosylation site. Our findings have major implications for SARS-CoV-2 vaccine design, especially those using inactivated viruses. The ongoing global pandemic of coronavirus disease 2019 (COVID-19) resulted from the outbreak of SARS-CoV-2 in December 2019. Currently, multiple efforts are being made to rapidly develop vaccines and treatments to fight COVID-19. Current vaccine candidates use inactivated SARS-CoV-2 viruses; therefore, it is important to understand the architecture of inactivated SARS-CoV-2. We have genetically and structurally characterized β-propiolactone-inactivated viruses from a propagated and purified clinical strain of SARS-CoV-2. We observed that the virus particles are roughly spherical or moderately pleiomorphic. Although a small fraction of prefusion spikes are found, most spikes appear nail shaped, thus resembling a postfusion state, where the S1 protein of the spike has disassociated from S2. Cryoelectron tomography and subtomogram averaging of these spikes yielded a density map that closely matches the overall structure of the SARS-CoV postfusion spike and its corresponding glycosylation site. Our findings have major implications for SARS-CoV-2 vaccine design, especially those using inactivated viruses. [Display omitted] •β-propiolactone-inactivated SARS-CoV-2 viruses display postfusion spikes•Cryo-ET structure of SARS-CoV-2 postfusion spikes was determined at 11 Å resolution•This study calls for crucial structural characterization of vaccine candidates Several vaccine candidates using inactivated SARS-CoV-2 viruses are under development. Liu et al. used state-of-the-art cryoelectron microscopy technologies to characterize the architecture of inactivated SARS-CoV-2 viruses. They found that the viral spikes are mostly in a postfusion state, which is not desirable for vaccine development. |
| Author | Mendonça, Luiza Liu, Yingxia Ju, Bin Ma, Xiaomin Liu, Jiwei Yang, Yang Liu, Lei Wu, Jing Liu, Congcong Zhu, Yanan Zhang, Zheng Tang, Xian Zhang, Peijun Xu, Shuman Gao, Yuanzhu Shen, Chenguang Yuan, Jing Wang, Peiyi Liu, Chuang Ni, Tao Liu, Weilong Liu, Zheng Wei, Jinli |
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for Infectious Disease, Shenzhen Third People's Hospital, Shenzhen 518112, Guangdong Province, China – sequence: 6 givenname: Jiwei surname: Liu fullname: Liu, Jiwei organization: Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, UK – sequence: 7 givenname: Tao surname: Ni fullname: Ni, Tao organization: Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, UK – sequence: 8 givenname: Bin surname: Ju fullname: Ju, Bin organization: Institute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People's Hospital, Shenzhen 518112, Guangdong Province, China – sequence: 9 givenname: Congcong orcidid: 0000-0002-8675-9100 surname: Liu fullname: Liu, Congcong organization: Cryo-EM Center, Southern University of Science and Technology, Shenzhen 518055, Guangdong Province, China – sequence: 10 givenname: Xian surname: Tang fullname: Tang, Xian organization: Institute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People's Hospital, Shenzhen 518112, Guangdong Province, China – sequence: 11 givenname: Jinli surname: Wei fullname: Wei, Jinli organization: Institute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People's Hospital, Shenzhen 518112, Guangdong Province, China – sequence: 12 givenname: Xiaomin surname: Ma fullname: Ma, Xiaomin organization: Department of Biology, Southern University of Science and Technology, Shenzhen 518055, Guangdong Province, China – sequence: 13 givenname: Yanan surname: Zhu fullname: Zhu, Yanan organization: Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, UK – sequence: 14 givenname: Weilong surname: Liu fullname: Liu, Weilong organization: Institute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People's Hospital, Shenzhen 518112, Guangdong Province, China – sequence: 15 givenname: Shuman surname: Xu fullname: Xu, Shuman organization: Cryo-EM Center, Southern University of Science and Technology, Shenzhen 518055, Guangdong Province, China – sequence: 16 givenname: Yingxia surname: Liu fullname: Liu, Yingxia organization: Institute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People's Hospital, Shenzhen 518112, Guangdong Province, China – sequence: 17 givenname: Jing surname: Yuan fullname: Yuan, Jing organization: Department for Infectious Diseases, Shenzhen Third People's Hospital, Shenzhen, Guangdong Province 518112, China – sequence: 18 givenname: Jing surname: Wu fullname: Wu, Jing organization: Cryo-EM Center, Southern University of Science and Technology, Shenzhen 518055, Guangdong Province, China – sequence: 19 givenname: Zheng surname: Liu fullname: Liu, Zheng organization: Cryo-EM Center, Southern University of Science and Technology, Shenzhen 518055, Guangdong Province, China – sequence: 20 givenname: Zheng surname: Zhang fullname: Zhang, Zheng email: zhangzheng1975@aliyun.com organization: Institute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People's Hospital, Shenzhen 518112, Guangdong Province, China – sequence: 21 givenname: Lei surname: Liu fullname: Liu, Lei email: liulei3322@aliyun.com organization: Institute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People's Hospital, Shenzhen 518112, Guangdong Province, China – sequence: 22 givenname: Peiyi surname: Wang fullname: Wang, Peiyi email: wangpy@sustech.edu.cn organization: Department of Biology, Southern University of Science and Technology, Shenzhen 518055, Guangdong Province, China – sequence: 23 givenname: Peijun orcidid: 0000-0003-1803-691X surname: Zhang fullname: Zhang, Peijun email: peijun@strubi.ox.ac.uk organization: Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, UK |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/33058760$$D View this record in MEDLINE/PubMed |
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| Keywords | COVID-19 SARS-CoV-2 vaccine postfusion β-propiolactone-inactivated viruses subtomogram averaging glycosylation cryo-ET cryo-EM spike |
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| SubjectTerms | Animals Betacoronavirus - drug effects Betacoronavirus - immunology Betacoronavirus - ultrastructure Chlorocebus aethiops Coronavirus Infections - immunology Coronavirus Infections - prevention & control COVID-19 COVID-19 Vaccines cryo-EM cryo-ET Cryoelectron Microscopy Disinfectants - pharmacology Electron Microscope Tomography glycosylation Humans postfusion Propiolactone - pharmacology SARS-CoV-2 Short spike Spike Glycoprotein, Coronavirus - ultrastructure subtomogram averaging vaccine Vaccines, Inactivated - immunology Vero Cells Viral Vaccines - immunology Virion - drug effects Virion - ultrastructure β-propiolactone-inactivated viruses |
| Title | The Architecture of Inactivated SARS-CoV-2 with Postfusion Spikes Revealed by Cryo-EM and Cryo-ET |
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