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Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains

Author

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  • Yuan Yuan

    (School of Life Sciences, University of Science and Technology of China
    CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences)

  • Duanfang Cao

    (National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences)

  • Yanfang Zhang

    (CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences
    Laboratory of Protein Engineering and Vaccines, Tianjin Institute of Biotechnology)

  • Jun Ma

    (National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences)

  • Jianxun Qi

    (CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences)

  • Qihui Wang

    (CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences)

  • Guangwen Lu

    (State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, and Collaborative Innovation Center of Biotherapy)

  • Ying Wu

    (School of Basic Medical Sciences, Wuhan University)

  • Jinghua Yan

    (CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences
    Shenzhen Key Laboratory of Pathogen and Immunity, Shenzhen Third People's Hospital
    Center for Influenza Research and Early-warning, Chinese Academy of Sciences (CASCIRE)
    Medical School, University of Chinese Academy of Sciences)

  • Yi Shi

    (CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences
    Shenzhen Key Laboratory of Pathogen and Immunity, Shenzhen Third People's Hospital
    Center for Influenza Research and Early-warning, Chinese Academy of Sciences (CASCIRE)
    Medical School, University of Chinese Academy of Sciences)

  • Xinzheng Zhang

    (National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences
    Center for Biological Imaging, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences)

  • George F. Gao

    (School of Life Sciences, University of Science and Technology of China
    CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences
    Laboratory of Protein Engineering and Vaccines, Tianjin Institute of Biotechnology
    Shenzhen Key Laboratory of Pathogen and Immunity, Shenzhen Third People's Hospital)

Abstract

The envelope spike (S) proteins of MERS-CoV and SARS-CoV determine the virus host tropism and entry into host cells, and constitute a promising target for the development of prophylactics and therapeutics. Here, we present high-resolution structures of the trimeric MERS-CoV and SARS-CoV S proteins in its pre-fusion conformation by single particle cryo-electron microscopy. The overall structures resemble that from other coronaviruses including HKU1, MHV and NL63 reported recently, with the exception of the receptor binding domain (RBD). We captured two states of the RBD with receptor binding region either buried (lying state) or exposed (standing state), demonstrating an inherently flexible RBD readily recognized by the receptor. Further sequence conservation analysis of six human-infecting coronaviruses revealed that the fusion peptide, HR1 region and the central helix are potential targets for eliciting broadly neutralizing antibodies.

Suggested Citation

  • Yuan Yuan & Duanfang Cao & Yanfang Zhang & Jun Ma & Jianxun Qi & Qihui Wang & Guangwen Lu & Ying Wu & Jinghua Yan & Yi Shi & Xinzheng Zhang & George F. Gao, 2017. "Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains," Nature Communications, Nature, vol. 8(1), pages 1-9, April.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms15092
    DOI: 10.1038/ncomms15092
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    Cited by:

    1. Tugba Taskin Tok & Sivakumar J T Gowder, 2020. "An Updated Review on Covid-19 with Special Reference to Structural Elucidation and Functional Properties," Biomedical Journal of Scientific & Technical Research, Biomedical Research Network+, LLC, vol. 31(4), pages 24345-24351, November.
    2. Anna R. Mäkelä & Hasan Uğurlu & Liina Hannula & Ravi Kant & Petja Salminen & Riku Fagerlund & Sanna Mäki & Anu Haveri & Tomas Strandin & Lauri Kareinen & Jussi Hepojoki & Suvi Kuivanen & Lev Levanov &, 2023. "Intranasal trimeric sherpabody inhibits SARS-CoV-2 including recent immunoevasive Omicron subvariants," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    3. Wenjuan Du & Oliver Debski-Antoniak & Dubravka Drabek & Rien Haperen & Melissa Dortmondt & Joline Lee & Ieva Drulyte & Frank J. M. Kuppeveld & Frank Grosveld & Daniel L. Hurdiss & Berend-Jan Bosch, 2024. "Neutralizing antibodies reveal cryptic vulnerabilities and interdomain crosstalk in the porcine deltacoronavirus spike protein," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    4. Weiwei Ji & Qi Peng & Xueqiong Fang & Zehou Li & Yaxin Li & Cunfa Xu & Shuqing Zhao & Jizong Li & Rong Chen & Guoxiang Mo & Zhanyong Wei & Ying Xu & Bin Li & Shuijun Zhang, 2022. "Structures of a deltacoronavirus spike protein bound to porcine and human receptors," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    5. Timothy J. C. Tan & Zongjun Mou & Ruipeng Lei & Wenhao O. Ouyang & Meng Yuan & Ge Song & Raiees Andrabi & Ian A. Wilson & Collin Kieffer & Xinghong Dai & Kenneth A. Matreyek & Nicholas C. Wu, 2023. "High-throughput identification of prefusion-stabilizing mutations in SARS-CoV-2 spike," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    6. Jimin Lee & Cameron Stewart & Alexandra Schäfer & Elizabeth M. Leaf & Young-Jun Park & Daniel Asarnow & John M. Powers & Catherine Treichel & Kaitlin R. Sprouse & Davide Corti & Ralph Baric & Neil P. , 2024. "A broadly generalizable stabilization strategy for sarbecovirus fusion machinery vaccines," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    7. Zhennan Zhao & Jingya Zhou & Mingxiong Tian & Min Huang & Sheng Liu & Yufeng Xie & Pu Han & Chongzhi Bai & Pengcheng Han & Anqi Zheng & Lutang Fu & Yuanzhu Gao & Qi Peng & Ying Li & Yan Chai & Zengyua, 2022. "Omicron SARS-CoV-2 mutations stabilize spike up-RBD conformation and lead to a non-RBM-binding monoclonal antibody escape," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    8. Zhennan Zhao & Yufeng Xie & Bin Bai & Chunliang Luo & Jingya Zhou & Weiwei Li & Yumin Meng & Linjie Li & Dedong Li & Xiaomei Li & Xiaoxiong Li & Xiaoyun Wang & Junqing Sun & Zepeng Xu & Yeping Sun & W, 2023. "Structural basis for receptor binding and broader interspecies receptor recognition of currently circulating Omicron sub-variants," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    9. David Chmielewski & Eric A. Wilson & Grigore Pintilie & Peng Zhao & Muyuan Chen & Michael F. Schmid & Graham Simmons & Lance Wells & Jing Jin & Abhishek Singharoy & Wah Chiu, 2023. "Structural insights into the modulation of coronavirus spike tilting and infectivity by hinge glycans," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    10. Cheng-Yu Huang & Piotr Draczkowski & Yong-Sheng Wang & Chia-Yu Chang & Yu-Chun Chien & Yun-Han Cheng & Yi-Min Wu & Chun-Hsiung Wang & Yuan-Chih Chang & Yen-Chen Chang & Tzu-Jing Yang & Yu-Xi Tsai & Ka, 2022. "In situ structure and dynamics of an alphacoronavirus spike protein by cryo-ET and cryo-EM," Nature Communications, Nature, vol. 13(1), pages 1-16, December.

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