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      Studying the Effects of ACE2 Mutations on the Stability, Dynamics, and Dissociation Process of SARS-CoV-2 S1/hACE2 Complexes

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          Abstract

          A highly infectious coronavirus, SARS-CoV-2, has spread in many countries. This virus recognizes its receptor, angiotensin-converting enzyme 2 (ACE2), using the receptor binding domain of its spike protein subunit S1. Many missense mutations are reported in various human populations for the ACE2 gene. In the current study, we predict the affinity of many ACE2 variants for binding to S1 protein using different computational approaches. The dissociation process of S1 from some variants of ACE2 is studied in the current work by molecular dynamics approaches. We study the relation between structural dynamics of ACE2 in closed and open states and its affinity for S1 protein of SARS-CoV-2.

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          A pneumonia outbreak associated with a new coronavirus of probable bat origin

          Peng Zhou, Xing-Lou Yang, Xian-Guang Wang … (2020)
          Since the outbreak of severe acute respiratory syndrome (SARS) 18 years ago, a large number of SARS-related coronaviruses (SARSr-CoVs) have been discovered in their natural reservoir host, bats 1–4 . Previous studies have shown that some bat SARSr-CoVs have the potential to infect humans 5–7 . Here we report the identification and characterization of a new coronavirus (2019-nCoV), which caused an epidemic of acute respiratory syndrome in humans in Wuhan, China. The epidemic, which started on 12 December 2019, had caused 2,794 laboratory-confirmed infections including 80 deaths by 26 January 2020. Full-length genome sequences were obtained from five patients at an early stage of the outbreak. The sequences are almost identical and share 79.6% sequence identity to SARS-CoV. Furthermore, we show that 2019-nCoV is 96% identical at the whole-genome level to a bat coronavirus. Pairwise protein sequence analysis of seven conserved non-structural proteins domains show that this virus belongs to the species of SARSr-CoV. In addition, 2019-nCoV virus isolated from the bronchoalveolar lavage fluid of a critically ill patient could be neutralized by sera from several patients. Notably, we confirmed that 2019-nCoV uses the same cell entry receptor—angiotensin converting enzyme II (ACE2)—as SARS-CoV.
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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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              VMD: Visual molecular dynamics

              William Humphrey, Andrew Dalke, Klaus Schulten (1996)
              Article 0 comments Cited 5162 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (nlm-ta): J Proteome Res
                Journal ID (iso-abbrev): J Proteome Res
                Journal ID (publisher-id): pr
                Journal ID (coden): jprobs
                Title: Journal of Proteome Research
                Publisher: American Chemical Society
                ISSN (Print): 1535-3893
                ISSN (Electronic): 1535-3907
                Publication date (Electronic): 27 July 2020
                Publication date (Print): 06 November 2020
                Volume: 19
                Issue: 11 , Proteomics in Pandemic Disease
                Pages: 4609-4623
                Affiliations
                [1]Department of Biological Sciences, Institute for Advanced Studies in Basic Sciences (IASBS) , Zanjan, 45137-66731, Iran
                Author notes
                [* ]Email: hhadi@ 123456iasbs.ac.ir . Tel: +982433153316. Fax: +982433153342.
                Article
                DOI: 10.1021/acs.jproteome.0c00348
                PMC ID: 7640954
                PubMed ID: 32786692
                SO-VID: 228fe28e-fe3b-4594-858a-fd1421ddaf56
                Copyright ©
                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.

                History
                Date received : 23 May 2020
                Categories
                Subject: Article
                Custom metadata
                document-id-old-9 pr0c00348
                document-id-new-14 pr0c00348
                ccc-price

                ScienceOpen disciplines: Molecular biology
                Keywords: sars-cov-2,ace2 polymorphism,iranian ethnic groups,adaptive biasing force,ace2 closed state,binding affinity
                Data availability:
                ScienceOpen disciplines: Molecular biology
                Keywords: sars-cov-2, ace2 polymorphism, iranian ethnic groups, adaptive biasing force, ace2 closed state, binding affinity

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