S-Palmitoylation cycles as Relevant Targets for Viral Infections

  • Funded by Swiss National Science Foundation (SNSF)
  • Total publications:3 publications

Grant number: 196651

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Key facts

  • Disease

    COVID-19
  • Start & end year

    2020
    2022
  • Known Financial Commitments (USD)

    $332,686.98
  • Funder

    Swiss National Science Foundation (SNSF)
  • Principal Investigator

    Gisou van der Goot, Francisco Mesquita
  • Research Location

    Switzerland
  • Lead Research Institution

    EPF Lausanne
  • Research Priority Alignment

    N/A
  • Research Category

    Pathogen: natural history, transmission and diagnostics

  • Research Subcategory

    Pathogen morphology, shedding & natural history

  • Special Interest Tags

    N/A

  • Study Type

    Non-Clinical

  • Clinical Trial Details

    N/A

  • Broad Policy Alignment

    Pending

  • Age Group

    Not Applicable

  • Vulnerable Population

    Not applicable

  • Occupations of Interest

    Not applicable

Abstract

The understanding of the novel coronavirus SARS-CoV-2 is greatly benefitted by past research on other viruses as well as bacterial toxins that need to enter mammalian cells. Our previous research on anthrax toxin entry has been instrumental to uncovering the involvement in S-palmitoylation in cellular processes. S-palmitoylation is a post-translational modification that is necessary for anthrax entry as well as for the life cycle of many envelop viruses. We have shown that both palmitoylation and depalmitoylation are essential for anthrax toxin entry. Preliminary experiments already indicate that inhibitors are depalmitoylation have a marked effect of SARS-CoV-2 viral entry, actually to similar extents as hydroxychloroquine. As one of the very few expert labs in S-palmitoyation worldwide, we propose to investigate how host S-palmitoylation cycles affects SARS-CoV-2 life cycle, from viral entry to virions release. Our contribution can further the development of pharmaceuticals that target SARS-CoV-2. Importantly, this approach can be extended to any virus, in anticipation of future epidemics.

Publicationslinked via Europe PMC

Mechanisms and functions of protein S-acylation.

SARS-CoV-2 hijacks a cell damage response, which induces transcription of a more efficient Spike S-acyltransferase.

SARS-CoV-2 shifts transcription of host gene to increase Spike acylation and boost infectivity