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      The role of growth factor receptors in viral infections: An opportunity for drug repurposing against emerging viral diseases such as COVID‐19?

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          Abstract

          Growth factor receptors are known to be involved in the process of viral infection. Many viruses not only use growth factor receptors to physically attach to the cell surface and internalize, but also divert receptor tyrosine kinase signaling in order to replicate. Thus, repurposing drugs that have initially been developed to target growth factor receptors and their signaling in cancer may prove to be a fast track to effective therapies against emerging new viral infections, including the coronavirus disease 19 (COVID‐19).

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          SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor

          Markus Hoffmann, Hannah Kleine-Weber, Simon Schroeder … (2020)
          Summary The recent emergence of the novel, pathogenic SARS-coronavirus 2 (SARS-CoV-2) in China and its rapid national and international spread pose a global health emergency. Cell entry of coronaviruses depends on binding of the viral spike (S) proteins to cellular receptors and on S protein priming by host cell proteases. Unravelling which cellular factors are used by SARS-CoV-2 for entry might provide insights into viral transmission and reveal therapeutic targets. Here, we demonstrate that SARS-CoV-2 uses the SARS-CoV receptor ACE2 for entry and the serine protease TMPRSS2 for S protein priming. A TMPRSS2 inhibitor approved for clinical use blocked entry and might constitute a treatment option. Finally, we show that the sera from convalescent SARS patients cross-neutralized SARS-2-S-driven entry. Our results reveal important commonalities between SARS-CoV-2 and SARS-CoV infection and identify a potential target for antiviral intervention.
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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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              Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2

              Renhong Yan, Yuanyuan Zhang, Yaning Li … (2020)
              How SARS-CoV-2 binds to human cells Scientists are racing to learn the secrets of severe acute respiratory syndrome–coronavirus 2 (SARS-CoV-2), which is the cause of the pandemic disease COVID-19. The first step in viral entry is the binding of the viral trimeric spike protein to the human receptor angiotensin-converting enzyme 2 (ACE2). Yan et al. present the structure of human ACE2 in complex with a membrane protein that it chaperones, B0AT1. In the context of this complex, ACE2 is a dimer. A further structure shows how the receptor binding domain of SARS-CoV-2 interacts with ACE2 and suggests that it is possible that two trimeric spike proteins bind to an ACE2 dimer. The structures provide a basis for the development of therapeutics targeting this crucial interaction. Science, this issue p. 1444
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                Author and article information

                Contributors
                Hubert Hondermarck: hubert.hondermarck@newcastle.edu.au
                Journal
                Journal ID (nlm-ta): FASEB Bioadv
                Journal ID (iso-abbrev): FASEB Bioadv
                Journal ID (doi): 10.1096/(ISSN)2573-9832
                Journal ID (publisher-id): FBA2
                Title: FASEB BioAdvances
                Publisher: John Wiley and Sons Inc. (Hoboken )
                ISSN (Electronic): 2573-9832
                Publication date (Electronic): 11 April 2020
                Publication date Collection: May 2020
                Volume: 2
                Issue: 5 ( doiID: 10.1096/fba2.v2.5 )
                Pages: 296-303
                Affiliations
                [ 1 ] School of Biomedical Sciences and Pharmacy Faculty of Health and Medicine University of Newcastle Callaghan NSW Australia
                [ 2 ] Hunter Medical Research Institute University of Newcastle New Lambton Heights NSW Australia
                [ 3 ] Institute of Medical Biology Glycotherapeutics Group A*STAR Singapore
                [ 4 ] Lee Kong Chian School of Medicine Nanyang Technology University‐Imperial College London Singapore
                Author notes
                [*] [* ] Correspondence

                Hubert Hondermarck, School of Biomedical Sciences and Pharmacy, Life Sciences Building (LSB3‐35), University of Newcastle, Callaghan NSW 2308, Australia.

                Email: hubert.hondermarck@ 123456newcastle.edu.au

                Article
                Publisher ID: FBA21124
                DOI: 10.1096/fba.2020-00015
                PMC ID: 7211041
                PubMed ID: 32395702
                SO-VID: 2471d31c-25ef-48db-a3c5-a44c43b07f86
                Copyright © © 2020 The Authors.
                License:

                This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

                History
                Date received : 01 April 2020
                Date accepted : 01 April 2020
                Page count
                Figures: 1, Tables: 1, Pages: 8, Words: 5632
                Funding
                Funded by: University of Newcastle
                Categories
                Subject: Hypothesis
                Subject: Hypothesis
                Custom metadata
                source-schema-version-number 2.0
                cover-date May 2020
                details-of-publishers-convertor Converter:WILEY_ML3GV2_TO_JATSPMC version:5.8.1 mode:remove_FC converted:09.05.2020

                Keywords: cancer drugs,covid‐19,growth factors,heparan sulfate,heparin,inhibitors,sars‐cov‐2,tyrosine kinase,virus
                Data availability:
                Keywords: cancer drugs, covid‐19, growth factors, heparan sulfate, heparin, inhibitors, sars‐cov‐2, tyrosine kinase, virus

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