Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor.
Jun Lan,Jiwan Ge,Jinfang Yu,Sisi Shan,Huan Zhou,Shilong Fan,Qi Zhang,Xuanling Shi,Qisheng Wang,Linqi Zhang,Xinquan Wang +10 more
TLDR
High-resolution crystal structures of the receptor-binding domain of the spike protein of SARS-CoV-2 and SARS -CoV in complex with ACE2 provide insights into the binding mode of these coronaviruses and highlight essential ACE2-interacting residues.Abstract:
A new and highly pathogenic coronavirus (severe acute respiratory syndrome coronavirus-2, SARS-CoV-2) caused an outbreak in Wuhan city, Hubei province, China, starting from December 2019 that quickly spread nationwide and to other countries around the world1–3. Here, to better understand the initial step of infection at an atomic level, we determined the crystal structure of the receptor-binding domain (RBD) of the spike protein of SARS-CoV-2 bound to the cell receptor ACE2. The overall ACE2-binding mode of the SARS-CoV-2 RBD is nearly identical to that of the SARS-CoV RBD, which also uses ACE2 as the cell receptor4. Structural analysis identified residues in the SARS-CoV-2 RBD that are essential for ACE2 binding, the majority of which either are highly conserved or share similar side chain properties with those in the SARS-CoV RBD. Such similarity in structure and sequence strongly indicate convergent evolution between the SARS-CoV-2 and SARS-CoV RBDs for improved binding to ACE2, although SARS-CoV-2 does not cluster within SARS and SARS-related coronaviruses1–3,5. The epitopes of two SARS-CoV antibodies that target the RBD are also analysed for binding to the SARS-CoV-2 RBD, providing insights into the future identification of cross-reactive antibodies. High-resolution crystal structures of the receptor-binding domain of the spike protein of SARS-CoV-2 and SARS-CoV in complex with ACE2 provide insights into the binding mode of these coronaviruses and highlight essential ACE2-interacting residues.read more
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Syncytia formation by SARS-CoV-2-infected cells.
Julian Buchrieser,Julian Buchrieser,Jérémy Dufloo,Jérémy Dufloo,Jérémy Dufloo,Mathieu Hubert,Mathieu Hubert,Blandine Monel,Blandine Monel,Delphine Planas,Delphine Planas,Maaran Michael Rajah,Maaran Michael Rajah,Maaran Michael Rajah,Cyril Planchais,Françoise Porrot,Françoise Porrot,Florence Guivel-Benhassine,Florence Guivel-Benhassine,Sylvie van der Werf,Sylvie van der Werf,Nicoletta Casartelli,Nicoletta Casartelli,Hugo Mouquet,Timothée Bruel,Timothée Bruel,Olivier Schwartz,Olivier Schwartz +27 more
TL;DR: The results show that SARS‐CoV‐2 pathological effects are modulated by cellular proteins that either inhibit or facilitate syncytia formation.
Journal ArticleDOI
Nanotechnology for COVID-19: Therapeutics and Vaccine Research.
Gaurav Chauhan,Marc J. Madou,Marc J. Madou,Sourav Kalra,Vianni Chopra,Deepa Ghosh,Sergio O. Martinez-Chapa +6 more
TL;DR: Recent as well as ongoing nanotechnology-based therapeutic and prophylactic strategies to fight against this pandemic are discussed, outlining the key areas for nanoscientists to step in.
Journal ArticleDOI
Structural and functional ramifications of antigenic drift in recent SARS-CoV-2 variants.
Meng Yuan,Deli Huang,Chang-Chun D Lee,Nicholas C. Wu,Abigail M. Jackson,Xueyong Zhu,Hejun Liu,Linghang Peng,Marit J. van Gils,Rogier W. Sanders,Rogier W. Sanders,Dennis R. Burton,Dennis R. Burton,S. Momsen Reincke,S. Momsen Reincke,Harald Prüss,Harald Prüss,Jakob Kreye,Jakob Kreye,David Nemazee,Andrew B. Ward,Ian A. Wilson +21 more
TL;DR: In this paper, the effects of SARS-CoV-2 mutations on angiotensin-converting enzyme 2 binding were investigated using COVID-19 patients, and the results have implications for next-generation vaccines and antibody therapies.
Journal ArticleDOI
Global pandemics interconnected - obesity, impaired metabolic health and COVID-19.
TL;DR: In this paper, the authors highlight how obesity and impaired metabolic health increase complications and mortality in COVID-19 and summarize the consequences of SARS-CoV-2 infection for organ function and risk of NCDs.
Journal ArticleDOI
Conformational dynamics of SARS-CoV-2 trimeric spike glycoprotein in complex with receptor ACE2 revealed by cryo-EM.
Cong Xu,Cong Xu,Yanxing Wang,Caixuan Liu,Caixuan Liu,Chao Zhang,W. Han,W. Han,Xiaoyu Hong,Xiaoyu Hong,Yifan Wang,Yifan Wang,Qin Hong,Qin Hong,S. Wang,S. Wang,Qiaoyu Zhao,Qiaoyu Zhao,Yalei Wang,Yong Yang,Kaijian Chen,Kaijian Chen,Wei Zheng,Wei Zheng,Liangliang Kong,Fangfang Wang,Qinyu Zuo,Zhong Huang,Yao Cong,Yao Cong +29 more
TL;DR: The 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.
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TL;DR: Identification and characterization of a new coronavirus (2019-nCoV), which caused an epidemic of acute respiratory syndrome in humans in Wuhan, China, and it is shown that this virus belongs to the species of SARSr-CoV, indicates that the virus is related to a bat coronav virus.
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