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Updated: Sep 10, 2025

An Ex Vivo Chicken Primary Bursal-cell Culture Model to Study Infectious Bursal Disease Virus Pathogenesis
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An Ex Vivo Chicken Primary Bursal-cell Culture Model to Study Infectious Bursal Disease Virus Pathogenesis

Published on: October 4, 2018

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CYLD suppresses infectious Bursal disease virus replication by deubiquitinating VP1

Qinghua Zeng1, Manzi Huang1, Boqian Zha1

  • 1Department of Veterinary Preventive Medicine, College of Animal Science and Technology, Jiangxi Agricultural University, Nanchang 330045, PR China; Jiangxi Provincial Key Laboratory for Animal Health, College of Animal Science and Technology, Jiangxi Agricultural University, Nanchang 330045, PR China.

Veterinary Microbiology
|August 27, 2025
PubMed

Insights

Cylindromatosis (CYLD) deubiquitinase inhibits infectious Bursal disease virus (IBDV) replication by targeting viral protein VP1. Viral protein VP3 disrupts this interaction, promoting IBDV replication, highlighting CYLD as a potential therapeutic target.

Area of Science:

  • Virology
  • Molecular Biology
  • Immunology

Background:

  • Cylindromatosis (CYLD) is a deubiquitinase (DUB) involved in regulating signaling pathways and has emerging roles in antiviral immunity.
  • The function of CYLD in infectious Bursal diseases virus (IBDV) infection is not well understood.

Purpose of the Study:

  • To investigate the role of CYLD in IBDV infection and elucidate the underlying molecular mechanisms.
  • To identify potential therapeutic targets for IBDV infection.

Main Methods:

  • Coimmunoprecipitation and mass spectrometry to identify CYLD-interacting proteins.
  • Overexpression and knockout/knockdown studies in DF-1 cells to assess CYLD's effect on IBDV replication.
  • In vivo and in vitro expression analysis of CYLD during IBDV infection.
  • Site-directed mutagenesis to identify critical residues in CYLD's enzymatic activity.

Main Results:

  • CYLD directly binds to IBDV protein VP1.
  • CYLD overexpression inhibits IBDV replication, while CYLD deficiency enhances it, independent of the interferon pathway.
  • IBDV infection upregulates CYLD expression.
  • CYLD deubiquitinates VP1, reducing its polymerase activity and inhibiting viral replication.
  • A specific catalytic residue (C602) in CYLD is crucial for its enzymatic activity and VP1 interaction.
  • Viral protein VP3 antagonizes CYLD's antiviral activity by disrupting the CYLD-VP1 interaction.

Conclusions:

  • CYLD plays a significant role in antiviral immunity against IBDV by targeting VP1 deubiquitination and activity.
  • The VP3-CYLD-VP1 axis is critical for regulating IBDV replication.
  • CYLD represents a potential therapeutic target for controlling IBDV infections.
Keywords:
CYLDDeubiquitinationIBDV VP1

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