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
Citations
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SARS-CoV-2 proteome microarray for global profiling of COVID-19 specific IgG and IgM responses
He wei Jiang,Yang Li,Hai nan Zhang,Wei Wang,Xiao Yang,Huan Qi,Hua Li,Dong Men,Jie Zhou,Sheng-Ce Tao +9 more
TL;DR: A systemic view of the SARS-CoV-2 specific IgG and IgM responses is presented and provides insights to aid the development of effective diagnostic, therapeutic and vaccination strategies.
Journal ArticleDOI
ACE2: Evidence of role as entry receptor for SARS-CoV-2 and implications in comorbidities.
TL;DR: A critical summary of the current knowledge highlighting the limitations and remaining gaps that need to be addressed to fully characterize ACE2 function in SARS-CoV-2 infection and associated pathogenesis is provided.
Journal ArticleDOI
Broad and potent activity against SARS-like viruses by an engineered human monoclonal antibody.
C. Garrett Rappazzo,Longping V. Tse,Chengzi I. Kaku,Daniel Wrapp,Mrunal Sakharkar,Deli Huang,Laura M. Deveau,Thomas J. Yockachonis,Andrew S. Herbert,Michael B. Battles,Cecilia M. O’Brien,Michael E. Brown,James C. Geoghegan,Jonathan P. Belk,Linghang Peng,Linlin Yang,Yixuan J. Hou,Trevor Scobey,Dennis R. Burton,David Nemazee,John M. Dye,James E. Voss,Bronwyn M. Gunn,Jason S. McLellan,Ralph S. Baric,Lisa E. Gralinski,Laura M. Walker +26 more
TL;DR: In this article, the authors employed a directed evolution approach to engineer three severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) antibodies for enhanced neutralization breadth and potency.
Posted ContentDOI
Complete mapping of mutations to the SARS-CoV-2 spike receptor-binding domain that escape antibody recognition.
Allison J. Greaney,Allison J. Greaney,Tyler N. Starr,Pavlo Gilchuk,Seth J. Zost,Elad Binshtein,Andrea N. Loes,Andrea N. Loes,Sarah K Hilton,John Huddleston,Rachel Eguia,Katharine H.D. Crawford,Katharine H.D. Crawford,Adam S. Dingens,Rachel S. Nargi,Rachel E. Sutton,Naveenchandra Suryadevara,Paul W. Rothlauf,Paul W. Rothlauf,Zhuoming Liu,Sean P. J. Whelan,Robert H. Carnahan,James E. Crowe,Jesse D. Bloom,Jesse D. Bloom,Jesse D. Bloom +25 more
TL;DR: A deep mutational scanning method is described to map how all amino-acid mutations in the RBD affect antibody binding, and a complete escape-mutation maps enable rational design of antibody therapeutics and assessment of the antigenic consequences of viral evolution.
Journal ArticleDOI
Higher infectivity of the SARS-CoV-2 new variants is associated with K417N/T, E484K, and N501Y mutants: An insight from structural data.
Abbas Khan,Tauqir Zia,Muhammad Suleman,Taimoor Khan,Syed Shujait Ali,Aamir Ali Abbasi,Anwar Mohammad,Dong-Qing Wei +7 more
TL;DR: In this article, a structural and biophysical analysis of the Spike glycoprotein of SARS-CoV-2 new variants has been carried out to understand the binding and structural dynamics of the new mutations in the RBD domain of Spike protein.
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