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Profiling Ubiquitin and Ubiquitin-like Dependent Post-translational Modifications and Identification of Significant Alterations
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Multiomics approach reveals the ubiquitination-specific processes hijacked by SARS-CoV-2

Gang Xu1, Yezi Wu1, Tongyang Xiao1

  • 1Institute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People's Hospital, The Second Affiliated Hospital, School of Medicine, Southern University of Science and Technology, 518112, Shenzhen, Guangdong Province, China.

Signal Transduction and Targeted Therapy
|September 7, 2022
PubMed

Insights

This study reveals how SARS-CoV-2 hijacks host ubiquitination processes to disrupt innate immunity and enhance viral infection. Identifying specific E3 ligases offers potential new antiviral and anti-inflammation targets for COVID-19 treatment.

Area of Science:

  • Virology
  • Immunology
  • Molecular Biology

Background:

  • COVID-19 pandemic caused by SARS-CoV-2 poses significant global health and socioeconomic challenges.
  • Existing antiviral drugs and vaccines are insufficient to fully control SARS-CoV-2 spread.
  • Understanding SARS-CoV-2 pathogenesis is crucial for identifying effective therapeutic targets.

Purpose of the Study:

  • To investigate the pathogenesis of SARS-CoV-2 in lung epithelial cells using a multiomics approach.
  • To elucidate the role of ubiquitination in SARS-CoV-2 infection and host immune response modulation.
  • To identify novel antiviral and anti-inflammation targets by screening E3 ligases and DUBs.

Main Methods:

  • Multiomics analysis including transcriptomics, proteomics, and ubiquitinomics of SARS-CoV-2-infected lung epithelial cells.
  • Investigation of ubiquitination of SARS-CoV-2 proteins, particularly the Spike protein.
  • High-throughput screening of E3 ubiquitin ligase and deubiquitinating enzyme libraries.

Main Results:

  • SARS-CoV-2 infection activates strong innate immune responses, including interferon and inflammatory pathways.
  • Ubiquitinomics revealed SARS-CoV-2 hijacks host ubiquitination processes to disrupt innate immunity.
  • Ubiquitination of the Spike protein enhances viral infection; four E3 ligases were identified as influencing SARS-CoV-2 infection.

Conclusions:

  • SARS-CoV-2 modulates host innate immunity and promotes viral infection by manipulating ubiquitination pathways.
  • Targeting specific ubiquitination processes and identified E3 ligases presents potential antiviral and anti-inflammatory strategies against COVID-19.

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