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      How much energy is stored in SARS‐CoV‐2 and its structural elements?

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          Abstract

          Severe acute respiratory syndrome coronavirus 2 (SARS‐CoV‐2) is the virus causing the COVID‐19 disease. Data regarding the morphological properties of this virus are collected from the literature and then the energy stored in each structural element is calculated with Domalski and Hearing's group contribution method. Viruses, including the Corona viruses, derive all of their energy from the host cell and carry out all of their activities with this energy. SARS‐CoV‐2 construct a vehicle needed for the delivery of its mRNA to other hosts to inflict them with the disease. Upon transfer of the viral RNA to the new host, the remaining parts of the viral structure are discarded. Structural and molecular assessments showed that the chemical formula of SARS‐CoV‐2 virus is C 7,336,852H 12,384,463N 1,247,424O 1,915,357P 100,231S 25,084 and its enthalpy of formation is −8.70 × 10 −16 kJ. Comparison of SARS‐CoV‐2 with the other viruses shows that its elemental composition does not like any of the others. The results of this study are expected to improve our knowledge of the thermodynamic properties of this virus.

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          Coronavirus biology and replication: implications for SARS-CoV-2

          Philip V’kovski, Annika Kratzel, Silvio Steiner … (2020)
          The SARS-CoV-2 pandemic and its unprecedented global societal and economic disruptive impact has marked the third zoonotic introduction of a highly pathogenic coronavirus into the human population. Although the previous coronavirus SARS-CoV and MERS-CoV epidemics raised awareness of the need for clinically available therapeutic or preventive interventions, to date, no treatments with proven efficacy are available. The development of effective intervention strategies relies on the knowledge of molecular and cellular mechanisms of coronavirus infections, which highlights the significance of studying virus–host interactions at the molecular level to identify targets for antiviral intervention and to elucidate critical viral and host determinants that are decisive for the development of severe disease. In this Review, we summarize the first discoveries that shape our current understanding of SARS-CoV-2 infection throughout the intracellular viral life cycle and relate that to our knowledge of coronavirus biology. The elucidation of similarities and differences between SARS-CoV-2 and other coronaviruses will support future preparedness and strategies to combat coronavirus infections.
          Article 0 comments Cited 1207 times – based on 0 reviews     Review now
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            The spike protein of SARS-CoV — a target for vaccine and therapeutic development

            Lanying Du, Yuxian He, Yusen Zhou … (2009)
            Key Points This Review provides an overview on the spike (S) protein of severe acute respiratory syndrome-coronavirus (SARS-CoV) as a target for the development of vaccines and therapeutics for the prevention and treatment of SARS. SARS is a newly emerging infectious disease, caused by SARS-CoV, a novel coronavirus that caused a global outbreak of SARS. SARS-CoV S protein mediates binding of the virus with its receptor angiotensin-converting enzyme 2 and promotes the fusion between the viral and host cell membranes and virus entry into the host cell. SARS-CoV S protein induces humoral and cellular immune responses against SARS-CoV. SARS S protein is the target of new SARS vaccines. These vaccines are based on SARS-CoV full-length S protein and its receptor-binding domain, including DNA-, viral vector- and subunit-based vaccines Peptides, antibodies, organic compounds and short interfering RNAs are additional anti-SARS-CoV therapeutics that target the S protein. The work on SARS-CoV S protein-based vaccines and drugs will be useful as a model for the development of prophylactic strategies and therapies against other viruses with class I fusion proteins that can cause emerging infectious diseases.
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              Molecular architecture of the SARS-CoV-2 virus

              Hangping Yao, Yutong Song, Yong Chen … (2020)
              SARS-CoV-2 is an enveloped virus responsible for the COVID-19 pandemic. Despite recent advances in the structural elucidation of SARS-CoV-2 proteins, detailed architecture of the intact virus remains to be unveiled. Here we report the molecular assembly of the authentic SARS-CoV-2 virus using cryo-electron tomography (cryo-ET) and subtomogram averaging (STA). Native structures of the S proteins in both pre- and postfusion conformations were determined to average resolutions of 8.7-11 Å. Compositions of the N-linked glycans from the native spikes were analyzed by mass-spectrometry, which revealed highly similar overall processing states of the native glycans to that of the recombinant glycoprotein glycans. The native conformation of the ribonucleoproteins (RNP) and its higher-order assemblies were revealed. Overall, these characterizations have revealed the architecture of the SARS-CoV-2 virus in exceptional detail, and shed lights on how the virus packs its ∼30 kb long single-segmented RNA in the ∼80 nm diameter lumen.
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                Author and article information

                Contributors
                Mustafa Özilgen:
                ORCID: https://orcid.org/0000-0003-0522-3644
                mozilgen@yeditepe.edu.tr
                Journal
                Journal ID (doi): 10.1002/(ISSN)2578-4862
                Journal ID (publisher-id): EST2
                Title: Energy Storage
                Publisher: John Wiley & Sons, Ltd. (Chichester, UK )
                ISSN (Electronic): 2578-4862
                Publication date (Electronic): 09 November 2021
                Publication date PMC-release: 09 November 2021
                Electronic Location Identifier: e298
                Affiliations
                [ 1 ] Department of Biomedical Engineering Faculty of Engineering, Yeditepe University Istanbul Turkey
                [ 2 ] Department of Food Engineering Faculty of Engineering, Yeditepe University Istanbul Turkey
                Author notes
                [*] [* ] Correspondence

                Mustafa Özilgen, Yeditepe University, Faculty of Engineering, Department of Food Engineering, Kayisdagi Cad., Istanbul 34755, Turkey.

                Email: mozilgen@ 123456yeditepe.edu.tr

                Author information
                https://orcid.org/0000-0001-9524-7417
                https://orcid.org/0000-0003-0522-3644
                https://orcid.org/0000-0002-5143-3602
                Article
                Publisher ID: EST2298
                DOI: 10.1002/est2.298
                PMC ID: 8646435
                SO-VID: 21ee0985-4c48-46ef-9506-9ef1a6ad7b2b
                Copyright © © 2021 John Wiley & Sons Ltd.
                License:

                This article is being made freely available through PubMed Central as part of the COVID-19 public health emergency response. It can be used for unrestricted research re-use and analysis in any form or by any means with acknowledgement of the original source, for the duration of the public health emergency.

                History
                Date revision received : 17 October 2021
                Date received : 31 August 2021
                Date accepted : 24 October 2021
                Page count
                Figures: 6, Tables: 13, Pages: 16, Words: 9549
                Categories
                Subject: Research Article
                Subject: Research Articles
                Custom metadata
                source-schema-version-number 2.0
                edited-state corrected-proof
                details-of-publishers-convertor Converter:WILEY_ML3GV2_TO_JATSPMC version:6.0.9 mode:remove_FC converted:06.12.2021

                Keywords: disease spreading vehicle,covid‐19 disease,elemental composition,energy storage,enthalpy of formation,group contribution method,sars‐cov‐2,structural elements
                Data availability:
                Keywords: disease spreading vehicle, covid‐19 disease, elemental composition, energy storage, enthalpy of formation, group contribution method, sars‐cov‐2, structural elements

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