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      Blocking Coronavirus 19 Infection via the SARS-CoV-2 Spike Protein: Initial Steps

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          Abstract

          Recent crystal structure data for protein–protein interactions featuring the SARS-CoV-2 spike protein will inevitably trigger a new wave of research in this area that was not possible before. This Viewpoint outlines a few of the ways that it is already happening.

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          Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein

          Alexandra C Walls, Young-Jun Park, M. Alejandra Tortorici … (2020)
          Summary The emergence of SARS-CoV-2 has resulted in >90,000 infections and >3,000 deaths. Coronavirus spike (S) glycoproteins promote entry into cells and are the main target of antibodies. We show that SARS-CoV-2 S uses ACE2 to enter cells and that the receptor-binding domains of SARS-CoV-2 S and SARS-CoV S bind with similar affinities to human ACE2, correlating with the efficient spread of SARS-CoV-2 among humans. We found that the SARS-CoV-2 S glycoprotein harbors a furin cleavage site at the boundary between the S1/S2 subunits, which is processed during biogenesis and sets this virus apart from SARS-CoV and SARS-related CoVs. We determined cryo-EM structures of the SARS-CoV-2 S ectodomain trimer, providing a blueprint for the design of vaccines and inhibitors of viral entry. Finally, we demonstrate that SARS-CoV S murine polyclonal antibodies potently inhibited SARS-CoV-2 S mediated entry into cells, indicating that cross-neutralizing antibodies targeting conserved S epitopes can be elicited upon vaccination.
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            Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor

            Jun Lan, Jiwan Ge, Jinfang Yu … (2020)
            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.
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              Structural basis of receptor recognition by SARS-CoV-2

              Jian Ku Shang, Gang Ye, Ke Chuang Shi … (2020)
              Summary A novel SARS-like coronavirus (SARS-CoV-2) recently emerged and is rapidly spreading in humans 1,2 . A key to tackling this epidemic is to understand the virus’s receptor recognition mechanism, which regulates its infectivity, pathogenesis and host range. SARS-CoV-2 and SARS-CoV recognize the same receptor - human ACE2 (hACE2) 3,4 . Here we determined the crystal structure of SARS-CoV-2 receptor-binding domain (RBD) (engineered to facilitate crystallization) in complex of hACE2. Compared with SARS-CoV RBD, a hACE2-binding ridge in SARS-CoV-2 RBD takes a more compact conformation; moreover, several residue changes in SARS-CoV-2 RBD stabilize two virus-binding hotspots at the RBD/hACE2 interface. These structural features of SARS-CoV-2 RBD enhance its hACE2-binding affinity. Additionally, we showed that RaTG13, a bat coronavirus closely related to SARS-CoV-2, also uses hACE2 as its receptor. The differences among SARS-CoV-2, SARS-CoV and RaTG13 in hACE2 recognition shed light on potential animal-to-human transmission of SARS-CoV-2. This study provides guidance for intervention strategies targeting receptor recognition by SARS-CoV-2.
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                Author and article information

                Journal
                Journal ID (nlm-ta): ACS Med Chem Lett
                Journal ID (iso-abbrev): ACS Med Chem Lett
                Journal ID (publisher-id): ml
                Journal ID (coden): amclct
                Title: ACS Medicinal Chemistry Letters
                Publisher: American Chemical Society
                ISSN (Electronic): 1948-5875
                Publication date (Electronic): 18 May 2020
                Publication date PMC-release: 18 May 2020
                Electronic Location Identifier: acsmedchemlett.0c00233
                Affiliations
                [1]Texas A&M University , Department of Chemistry, Box 30012, College Station, Texas 77842, United States
                Author notes
                Article
                DOI: 10.1021/acsmedchemlett.0c00233
                PMC ID: 7241730
                SO-VID: 8b8df475-4dba-4808-8f25-ddb6d85cd3b9
                Copyright © Copyright © 2020 American Chemical Society
                License:

                This article is made available via the PMC Open Access Subset for unrestricted RESEARCH re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.

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                Subject: Viewpoint
                Custom metadata
                document-id-old-9 ml0c00233
                document-id-new-14 ml0c00233
                ccc-price

                ScienceOpen disciplines: Pharmaceutical chemistry
                Keywords: sars-cov-2,spike protein,peptide,monoclonal antibody
                Data availability:
                ScienceOpen disciplines: Pharmaceutical chemistry
                Keywords: sars-cov-2, spike protein, peptide, monoclonal antibody

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