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Biochem Biophys Res Commun . The biogenesis of SARS-CoV-2 spike glycoprotein: multiple targets for host-directed antiviral therapy

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  • Biochem Biophys Res Commun . The biogenesis of SARS-CoV-2 spike glycoprotein: multiple targets for host-directed antiviral therapy


    Biochem Biophys Res Commun


    . 2020 Nov 28;S0006-291X(20)32009-X.
    doi: 10.1016/j.bbrc.2020.10.080. Online ahead of print.
    The biogenesis of SARS-CoV-2 spike glycoprotein: multiple targets for host-directed antiviral therapy


    Silvia Santopolo 1 , Anna Riccio 1 , M Gabriella Santoro 2



    AffiliationsFree PMC article

    Abstract

    Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of COVID-19 (coronavirus disease-19), represents a far more serious threat to public health than SARS and MERS coronaviruses, due to its ability to spread more efficiently than its predecessors. Currently, there is no worldwide-approved effective treatment for COVID-19, urging the scientific community to intense efforts to accelerate the discovery and development of prophylactic and therapeutic solutions against SARS-CoV-2 infection. In particular, effective antiviral drugs are urgently needed. With few exceptions, therapeutic approaches to combat viral infections have traditionally focused on targeting unique viral components or enzymes; however, it has now become evident that this strategy often fails due to the rapid emergence of drug-resistant viruses. Targeting host factors that are essential for the virus life cycle, but are dispensable for the host, has recently received increasing attention. The spike glycoprotein, a component of the viral envelope that decorates the virion surface as a distinctive crown ("corona") and is essential for SARS-CoV-2 entry into host cells, represents a key target for developing therapeutics capable of blocking virus invasion. This review highlights aspects of the SARS-CoV-2 spike biogenesis that may be amenable to host-directed antiviral targeting.

    Keywords: Antiviral; COVID-19; Coronavirus; ERp57; Furin; N-Glycosylation.

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