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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Immunity to SARS-CoV-2: Lessons Learned.
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TL;DR: In this article, the authors summarize the latest and rapidly developing understanding of immunity to SARS-CoV-2 infection, including what we have learned about the key antigens, their importance in vaccine development, the immediate immune response to severe acute respiratory syndrome coronavirus 2, breadth of coverage of emerging SARS CoV2 variants, contributions of preexisting immunity to related coronaviruses, and duration of immunity.
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Replication of SARS-CoV-2 Omicron BA.2 variant in ex vivo cultures of the human upper and lower respiratory tract
Kenrie P Y Hui,Ka Chun Ng,John C. W. Ho,H. Yeung,Rachel Hiu Ha Ching,Haogao Gu,Joseph CK Chung,Velda Ling Yu Chow,Ko-Yung Sit,M. K. Hsin,Timmy W.K. Au,Leo L.M. Poon,Malik Peiris,John M. Nicholls,Michael C. W. Chan +14 more
TL;DR: In this paper , the authors characterized the replication competence and respiratory tissue tropism of three Omicron variants (BA.1, BA.2 and BA.3) in human nasal, bronchial and lung tissues cultured ex vivo.
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Thermodynamics of the Interaction between the Spike Protein of Severe Acute Respiratory Syndrome Coronavirus-2 and the Receptor of Human Angiotensin-Converting Enzyme 2. Effects of Possible Ligands.
Cristina García-Iriepa,Cécilia Hognon,Antonio Francés-Monerris,Antonio Francés-Monerris,Isabel Iriepa,Tom Miclot,Tom Miclot,Giampaolo Barone,Antonio Monari,Marco Marazzi +9 more
TL;DR: A rational evaluation of the molecular mechanisms behind the formation of the protein complex of SARS-CoV-2 is proposed and rationales that could be useful for the subsequent wise molecular design for the treatment of COVID-19 cases are suggested.
Journal ArticleDOI
Structural and Functional Characterization of SARS-CoV-2 RBD Domains Produced in Mammalian Cells.
Christoph Gstöttner,Tao Zhang,Anja Resemann,Sophia Ruben,Stuart Pengelley,Detlev Suckau,Tim Welsink,Manfred Wuhrer,Elena Domínguez-Vega +8 more
TL;DR: In this article, structural and functional characterization of RBDs expressed in Chinese hamster ovary (CHO) and human embryonic kidney 293 (HEK293) cells was performed using a multilevel mass spectrometric approach.
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