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ISGylation by HERCs facilitates STING activation.

Ying Qin1, Min Wang2, Xintong Meng1

  • 1Key Laboratory for Experimental Teratology of the Chinese Ministry of Education and Key Laboratory of Infection and Immunity of Shandong Province, School of Basic Medical Science, Cheeloo College of Medicine, Shandong University, Jinan, Shandong, China.

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|April 23, 2024
PubMed
Summary

HECT domain- and RCC1-like domain-containing proteins (HERCs) regulate the stimulator of interferon genes (STING) protein

Keywords:
Antiviral innate immunityCP: ImmunologyHERCsISGylationSARS-CoV-2 protein PLproSTINGpost-translational modifications

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Area of Science:

  • Immunology
  • Molecular Biology
  • Virology

Background:

  • Stimulator of interferon genes (STING) protein activation is critical for innate immunity against pathogens.
  • Post-translational modifications, including ISGylation, modulate STING activity, but their specific roles remain incompletely understood.
  • Understanding STING regulation is key to developing host-directed antiviral therapies.

Purpose of the Study:

  • To elucidate the role of ISG15 modification (ISGylation) in controlling STING stability and activation.
  • To investigate the function of HECT domain- and RCC1-like domain-containing proteins (HERCs) in STING-mediated immune responses.
  • To explore the interplay between ISGylation and ubiquitination in STING regulation.

Main Methods:

  • Investigated STING protein stability and activation in the presence and absence of HERC proteins.
  • Utilized in vitro and in vivo models of herpes simplex virus 1 infection.
  • Analyzed the effect of severe acute respiratory syndrome coronavirus 2 papain-like protease on STING ISGylation.

Main Results:

  • HERC proteins (HERC5/HERC6) mediate ISGylation of STING at K150, preventing its ubiquitination and degradation.
  • Herc6 deficiency impairs type I interferon responses and enhances viral replication during herpes simplex virus 1 infection.
  • SARS-CoV-2 papain-like protease antagonizes host defense by cleaving HERC5-mediated STING ISGylation.

Conclusions:

  • HERC-mediated ISGylation is a key mechanism controlling STING stability and activation.
  • ISGylation and ubiquitination pathways are interconnected in regulating STING function.
  • This study reveals a novel antiviral mechanism and a target for therapeutic intervention against viral infections.