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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ACE2 and ACE: structure-based insights into mechanism, regulation and receptor recognition by SARS-CoV.
TL;DR: A comparative analysis of methodologies and findings is provided to describe how structural biology techniques like X-ray crystallography and cryo-electron microscopy have enabled remarkable discoveries into the structure–function relationship of ACE and ACE2.
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COVID-19: Coronavirus replication, pathogenesis, and therapeutic strategies.
TL;DR: Human coronaviruses, along with influenza virus, human metapneumov virus, respiratory syncytial virus, and rhinovirus, are endemic and cause approximately 15% to 30% of annual respiratory tract infections.
Journal ArticleDOI
The evolutionary history of ACE2 usage within the coronavirus subgenus Sarbecovirus
Heather L. Wells,Michael Letko,Michael Letko,Gorka Lasso,Benard Ssebide,Julius Nziza,Denis K. Byarugaba,Denis K. Byarugaba,Isamara Navarrete-Macias,Eliza Liang,Michael R. Cranfield,Michael R. Cranfield,Barbara A. Han,Morgan W. Tingley,Maria A. Diuk-Wasser,Tracey Goldstein,Christine K. Johnson,Jonna A. K. Mazet,Kartik Chandran,Vincent J. Munster,Kirsten V. K. Gilardi,Kirsten V. K. Gilardi,Simon J. Anthony +22 more
TL;DR: In this article, a new sarbecovirus from Rwanda and Uganda that is phylogenetically intermediate to severe acute respiratory syndrome coronavirus 1 (SARS-CoV-1) and SARS CoV-2 is reported.
Journal ArticleDOI
Development and Validation of a Multiplex, Bead-Based Assay to Detect Antibodies Directed Against SARS-CoV-2 Proteins.
Robert A. Bray,Jar How Lee,Peter Brescia,Deepali Kumar,Thoa Nong,Remi Shih,E. Steve Woodle,Jonathan S. Maltzman,Jonathan S. Maltzman,Howard M. Gebel +9 more
TL;DR: This new assay provides a novel tool to interrogate the spectrum of immune responses to SAR-CoV-2 and is uniquely suitable for use in the transplant setting.
Journal ArticleDOI
AGTR2 , One Possible Novel Key Gene for the Entry of SARS-CoV-2 Into Human Cells
Chunmei Cui,Chuanbo Huang,Wanlu Zhou,Xiangwen Ji,Fenghong Zhang,Liang Wang,Yuan Zhou,Qinghua Cui +7 more
TL;DR: Simulation of 3D structure based protein-protein interaction reveals that AGTR2 (angiotensin II receptor type 2), a G-protein coupled receptor, has interaction with SARS-CoV-2 and is highly expressed in lung with a high tissue specificity, and it is suggested that AGTR2 could be a putative novel gene for the entry of Sars-Cov-2 into human cells.
References
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