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  1. Article ; Online: Cryo-EM analysis of the post-fusion structure of the SARS-CoV spike glycoprotein.

    Fan, Xiaoyi / Cao, Duanfang / Kong, Lingfei / Zhang, Xinzheng

    Nature communications

    2020  Volume 11, Issue 1, Page(s) 3618

    Abstract: ... bound linker region upstream of the HR2 motif. The structures of pre- and post-fusion SARS-CoV S ... electron microscopy to show that the post-fusion SARS-CoV S2 forms a further rotated HR1-HR2 six-helix bundle and a tightly ... by mediating host-viral membrane fusion. However, structural information of the post-fusion S2 ...

    Abstract Global emergencies caused by the severe acute respiratory syndrome coronavirus (SARS-CoV), Middle-East respiratory syndrome coronavirus (MERS-CoV) and SARS-CoV-2 significantly endanger human health. The spike (S) glycoprotein is the key antigen and its conserved S2 subunit contributes to viral entry by mediating host-viral membrane fusion. However, structural information of the post-fusion S2 from these highly pathogenic human-infecting coronaviruses is still lacking. We used single-particle cryo-electron microscopy to show that the post-fusion SARS-CoV S2 forms a further rotated HR1-HR2 six-helix bundle and a tightly bound linker region upstream of the HR2 motif. The structures of pre- and post-fusion SARS-CoV S glycoprotein dramatically differ, resembling that of the Mouse hepatitis virus (MHV) and other class I viral fusion proteins. This structure suggests potential targets for the development of vaccines and therapies against a wide range of SARS-like coronaviruses.
    MeSH term(s) Amino Acid Motifs ; Betacoronavirus/chemistry ; Betacoronavirus/physiology ; COVID-19 ; Coronavirus/chemistry ; Coronavirus/classification ; Coronavirus Infections/virology ; Cryoelectron Microscopy ; Humans ; Membrane Fusion ; Models, Molecular ; Pandemics ; Pneumonia, Viral/virology ; Protein Conformation ; Protein Multimerization ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus/chemistry ; Virus Internalization
    Chemical Substances Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2
    Keywords covid19
    Language English
    Publishing date 2020-07-17
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-020-17371-6
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Cryo-EM analysis of the post-fusion structure of the SARS-CoV spike glycoprotein

    Fan, Xiaoyi / Cao, Duanfang / Kong, Lingfei / Zhang, Xinzheng

    Nat Commun

    Abstract: ... bound linker region upstream of the HR2 motif. The structures of pre- and post-fusion SARS-CoV S ... electron microscopy to show that the post-fusion SARS-CoV S2 forms a further rotated HR1-HR2 six-helix bundle and a tightly ... by mediating host-viral membrane fusion. However, structural information of the post-fusion S2 ...

    Abstract Global emergencies caused by the severe acute respiratory syndrome coronavirus (SARS-CoV), Middle-East respiratory syndrome coronavirus (MERS-CoV) and SARS-CoV-2 significantly endanger human health. The spike (S) glycoprotein is the key antigen and its conserved S2 subunit contributes to viral entry by mediating host-viral membrane fusion. However, structural information of the post-fusion S2 from these highly pathogenic human-infecting coronaviruses is still lacking. We used single-particle cryo-electron microscopy to show that the post-fusion SARS-CoV S2 forms a further rotated HR1-HR2 six-helix bundle and a tightly bound linker region upstream of the HR2 motif. The structures of pre- and post-fusion SARS-CoV S glycoprotein dramatically differ, resembling that of the Mouse hepatitis virus (MHV) and other class I viral fusion proteins. This structure suggests potential targets for the development of vaccines and therapies against a wide range of SARS-like coronaviruses.
    Keywords covid19
    Publisher WHO
    Document type Article
    Note WHO #Covidence: #651635
    Database COVID19

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  3. Article ; Online: Cryo-EM analysis of the post-fusion structure of the SARS-CoV spike glycoprotein

    Xiaoyi Fan / Duanfang Cao / Lingfei Kong / Xinzheng Zhang

    Nature Communications, Vol 11, Iss 1, Pp 1-

    2020  Volume 10

    Abstract: ... of SARS-CoV post-fusion S2 trimer, providing insights into the fusion mechanism that could be useful ... between the viral membrane and the of cell host membrane. Here the authors report a cryo-EM structure ... The spike (S) protein of coronaviruses is responsible for receptor recognition and the fusion ...

    Abstract The spike (S) protein of coronaviruses is responsible for receptor recognition and the fusion between the viral membrane and the of cell host membrane. Here the authors report a cryo-EM structure of SARS-CoV post-fusion S2 trimer, providing insights into the fusion mechanism that could be useful for therapeutic development against coronaviruses.
    Keywords Science ; Q
    Language English
    Publishing date 2020-07-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article ; Online: Conformational dynamics of SARS-CoV-2 trimeric spike glycoprotein in complex with receptor ACE2 revealed by cryo-EM.

    Xu, Cong / Wang, Yanxing / Liu, Caixuan / Zhang, Chao / Han, Wenyu / Hong, Xiaoyu / Wang, Yifan / Hong, Qin / Wang, Shutian / Zhao, Qiaoyu / Wang, Yalei / Yang, Yong / Chen, Kaijian / Zheng, Wei / Kong, Liangliang / Wang, Fangfang / Zuo, Qinyu / Huang, Zhong / Cong, Yao

    Science advances

    2021  Volume 7, Issue 1

    Abstract: ... EM structures of a tightly closed SARS-CoV-2 S trimer with packed fusion peptide and an ACE2-bound S ... The recent outbreaks of SARS-CoV-2 pose a global health emergency. The SARS-CoV-2 trimeric spike (S ... domain (RBD), the associated ACE2-RBD exhibits continuous swing motions. Notably, the SARS-CoV-2 S trimer ...

    Abstract The recent outbreaks of SARS-CoV-2 pose a global health emergency. The SARS-CoV-2 trimeric spike (S) glycoprotein interacts with the human ACE2 receptor to mediate viral entry into host cells. We report the cryo-EM structures of a tightly closed SARS-CoV-2 S trimer with packed fusion peptide and an ACE2-bound S trimer at 2.7- and 3.8-Å resolution, respectively. Accompanying ACE2 binding to the up receptor-binding domain (RBD), the associated ACE2-RBD exhibits continuous swing motions. Notably, the SARS-CoV-2 S trimer appears much more sensitive to the ACE2 receptor than the SARS-CoV S trimer regarding receptor-triggered transformation from the closed prefusion state to the fusion-prone open state, potentially contributing to the superior infectivity of SARS-CoV-2. We defined the RBD T470-T478 loop and Y505 as viral determinants for specific recognition of SARS-CoV-2 RBD by ACE2. Our findings depict the mechanism of ACE2-induced S trimer conformational transitions from the ground prefusion state toward the postfusion state, facilitating development of anti-SARS-CoV-2 vaccines and therapeutics.
    MeSH term(s) Angiotensin-Converting Enzyme 2/chemistry ; Animals ; Cryoelectron Microscopy ; Enzyme-Linked Immunosorbent Assay ; Humans ; Image Processing, Computer-Assisted ; Ligands ; Mice ; Mice, Inbred BALB C ; Mutation ; Peptides/chemistry ; Polysaccharides ; Principal Component Analysis ; Protein Binding ; Protein Domains ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus/chemistry
    Chemical Substances Ligands ; Peptides ; Polysaccharides ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2 ; ACE2 protein, human (EC 3.4.17.23) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23)
    Language English
    Publishing date 2021-01-01
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2810933-8
    ISSN 2375-2548 ; 2375-2548
    ISSN (online) 2375-2548
    ISSN 2375-2548
    DOI 10.1126/sciadv.abe5575
    Database MEDical Literature Analysis and Retrieval System OnLINE

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