Ubiquitin-Modified Proteome of SARS-CoV-2-Infected Host Cells Reveals Insights into Virus-Host Interaction and

Huan Zhang1, Huanying Zheng2, Jinying Zhu1

  • 1Key Laboratory of Zoonotic of Liaoning Province, College of Animal Science and Veterinary Medicine, Shenyang Agricultural University, Shenyang 110866, Liaoning Province, P. R. China.

Insights

This study reveals how ubiquitination changes in host cells and SARS-CoV-2 proteins during COVID-19 infection. These findings offer new insights into virus-host interactions and potential therapeutic targets for COVID-19.

Area of Science:

  • Biochemistry
  • Virology
  • Immunology

Background:

  • The COVID-19 pandemic, caused by SARS-CoV-2, presents a significant global health challenge.
  • Understanding the pathogenesis and host immune response to SARS-CoV-2 is crucial but remains incomplete.

Purpose of the Study:

  • To investigate ubiquitination alterations in host cells and SARS-CoV-2 during infection.
  • To identify potential therapeutic targets for COVID-19 by examining virus-host interactions.

Main Methods:

  • Quantitative proteomic analysis using label-free liquid chromatography-tandem mass spectrometry.
  • Identification and quantification of lysine ubiquitination sites in host proteins and viral proteins.

Main Results:

  • Identified 8943 ubiquitination sites on 3086 proteins; 138 sites (104 proteins) upregulated and 828 sites (447 proteins) downregulated at 72h post-infection.
  • Bioinformatics analysis indicated SARS-CoV-2 modulates host immunity via ubiquitination of key proteins (USP5, IQGAP1, TRIM28, Hsp90).
  • Observed ubiquitination on 11 SARS-CoV-2 proteins involved in replication and immune evasion.

Conclusions:

  • SARS-CoV-2 infection significantly alters host cell ubiquitination patterns.
  • Ubiquitination of viral proteins suggests a role in virus replication and host immune response modulation.
  • This research provides novel insights into SARS-CoV-2-host interactions and potential therapeutic strategies for COVID-19.

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