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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Clinical Trials of Repurposed Antivirals for SARS-CoV-2.
TL;DR: The first open-label, randomized, controlled trials are showing poor efficacy of these repurposed drugs, highlighting the necessity of identifying and characterizing specific and potent SARS-CoV-2 antivirals.
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Dynamics of antibodies to SARS-CoV-2 in convalescent plasma donors
Maurice Steenhuis,Gerard van Mierlo,Ninotska I. L. Derksen,Pleuni Ooijevaar-de Heer,Simone Kruithof,Floris L. Loeff,Lea C. Berkhout,Federica Linty,Chantal B.E.M. Reusken,Johan Reimerink,Boris M. Hogema,Hans L. Zaaijer,Leo van de Watering,Francis Swaneveld,Marit J. van Gils,Berend Jan Bosch,Marieke van Ham,Anja ten Brinke,Gestur Vidarsson,Ellen van der Schoot,Theo Rispens +20 more
TL;DR: In this paper, the authors measured antibody responses to the receptor-binding domain (RBD) of the SARS-CoV-2 spike protein and the nucleocapsid protein in 844 longitudinal samples from 151 RT-PCR-positive SARS CoV2 convalescent adults during the first 250 days after onset of symptoms.
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Genomics insights of SARS-CoV-2 (COVID-19) into target-based drug discovery.
P. Chellapandi,S. Saranya +1 more
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Engaging the spikes: heparan sulfate facilitates SARS-CoV-2 spike protein binding to ACE2 and potentiates viral infection.
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Universal coronavirus vaccines: the time to start is now
TL;DR: Research on influenza immunity and vaccine development may provide valuable lessons for coronavirus efforts, especially considering similarities in rapid evolutionary potential.
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