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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Kinetics of Viral Clearance and Antibody Production Across Age Groups in Children with Severe Acute Respiratory Syndrome Coronavirus 2 Infection.
TL;DR: In this paper, a retrospective analysis of children tested for SARS-CoV-2 by reverse transcription (RT) polymerase chain reaction (PCR) and immunoglobulin G antibody at a quaternary-care, free-standing pediatric hospital between March 13, 2020, and June 21, 2020 was performed.
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Nanotraps for the containment and clearance of SARS-CoV-2.
Min Chen,Jillian Rosenberg,Xiaolei Cai,Andy Chao Hsuan Lee,Jiuyun Shi,Mindy Nguyen,Thirushan Wignakumar,Vikranth Mirle,Arianna Joy Edobor,John J. Fung,Jessica S. Donington,Kumaran Shanmugarajah,Yiliang Lin,Eugene B. Chang,Glenn Randall,Pablo Penaloza-MacMaster,Bozhi Tian,Maria Lucia Madariaga,Jun Huang +18 more
TL;DR: In this paper, Nanotrap surfaces were functionalized with either recombinant ACE2 proteins or anti-SARS-CoV-2 neutralizing antibodies and phagocytosis-specific phosphatidylserines.
Journal ArticleDOI
The Role of the SARS-CoV-2 S-Protein Glycosylation in the Interaction of SARS-CoV-2/ACE2 and Immunological Responses.
Eleazar Ramírez Hernández,Luis Fernando Hernández-Zimbrón,Nayeli Martínez Zuñiga,Juan José Leal-García,Violeta Ignacio Hernández,Luis Eduardo Ucharima-Corona,Eduardo Pérez Campos,Edgar Zenteno +7 more
TL;DR: In this paper, the implications of the CoV2 S protein glycosylation in the SARS-CoV-2/ACE2 interaction and the immunological response are discussed.
Journal ArticleDOI
Targeted intracellular degradation of SARS-CoV-2 via computationally optimized peptide fusions.
Pranam Chatterjee,Manvitha Ponnapati,Christian Kramme,Alexandru M Plesa,Alexandru M Plesa,George M. Church,George M. Church,Joseph M. Jacobson +7 more
TL;DR: A novel computational platform for engineering peptide fusions that bind to the SARS-CoV-2 spike protein and tag it for proteasomal degradation is presented and an optimal variant in human cells is experimentally validated, showing that it inhibits production of infection-competent virus.
Journal ArticleDOI
ACE-2-Derived Biomimetic Peptides for the Inhibition of Spike Protein of SARS-CoV-2.
Saroj Kumar Panda,Parth Sarthi Sen Gupta,Satyaranjan Biswal,Abhik Kumar Ray,Malay Kumar Rana +4 more
TL;DR: A peptide derived from simultaneous mutation of all the non-interacting residues of hace-2 yields two-fold stronger interaction than hACE-2 and turns out here to be the best peptide-inhibitor of the novel coronavirus.
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