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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SARS-CoV-2: Structure, Biology, and Structure-Based Therapeutics Development.
TL;DR: This review briefly summarized the current advances in SARS-CoV-2 research, including the epidemic situation and epidemiological characteristics of the caused disease COVID-19, and introduced the protein structures and structure-based therapeutics development including antibodies, antiviral compounds, and vaccines.
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SARS-CoV-2 binds platelet ACE2 to enhance thrombosis in COVID-19
Si Zhang,Yangyang Liu,Xiaofang Wang,Li Yang,Haishan Li,Yuyan Wang,Mengduan Liu,Xiaoyan Zhao,Youhua Xie,Yan Yang,Shenghui Zhang,Zhichao Fan,Jianzeng Dong,Zhenghong Yuan,Zhongren Ding,Yi Zhang,Liang Hu +16 more
TL;DR: A novel function of SARS-CoV-2 on platelet activation via binding of Spike to ACE2 is uncovered, which may participate in thrombus formation and inflammatory responses in COVID-19 patients.
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Omicron Variant (B.1.1.529): Infectivity, Vaccine Breakthrough, and Antibody Resistance
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Antibody escape of SARS-CoV-2 Omicron BA.4 and BA.5 from vaccine and BA.1 serum
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TL;DR: In this article , the neutralization of BA.4 and BA.5 has been studied using a range of vaccine and naturally immune serum and panels of monoclonal antibodies.
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SARS-CoV-2 and bat RaTG13 spike glycoprotein structures inform on virus evolution and furin-cleavage effects.
A.G. Wrobel,D.J. Benton,Pengqi Xu,Pengqi Xu,Chloe Roustan,Stephen R. Martin,Peter B. Rosenthal,John J. Skehel,Steven J. Gamblin +8 more
TL;DR: Cryo-EM and functional analyses of furin-cleaved spike from SARS-CoV-2 and the closely related spike from bat virus RaTG13 reveal differences in protein stability and binding to human receptor ACE2.
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