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Updated: Mar 14, 2026

Monitoring Activation of the Antiviral Pattern Recognition Receptors RIG-I And PKR By Limited Protease Digestion and Native PAGE
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Foot-and-Mouth Disease Virus Viroporin 2B Antagonizes RIG-I-Mediated Antiviral Effects by Inhibition of Its Protein

Zixiang Zhu1, Guoqing Wang1, Fan Yang1

  • 1State Key Laboratory of Veterinary Etiological Biology, National Foot and Mouth Diseases Reference Laboratory, Key Laboratory of Animal Virology of Ministry of Agriculture, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, China.

Journal of Virology
|October 7, 2016
PubMed

Insights

Retinoic acid-inducible gene I (RIG-I) inhibits foot-and-mouth disease virus (FMDV) replication. FMDV's 2B protein uniquely reduces RIG-I levels, revealing a novel viral immune evasion strategy.

Area of Science:

  • Virology
  • Immunology
  • Molecular Biology

Background:

  • Foot-and-mouth disease virus (FMDV) poses a significant threat to livestock.
  • The innate immune sensor retinoic acid-inducible gene I (RIG-I) plays a crucial role in antiviral defense.
  • The interaction between RIG-I and FMDV has not been previously elucidated.

Purpose of the Study:

  • To investigate the role of RIG-I in FMDV-infected cells.
  • To determine the mechanism by which FMDV evades RIG-I-mediated immunity.
  • To identify specific viral factors involved in antagonizing RIG-I.

Main Methods:

  • Analysis of RIG-I transcription and protein expression in FMDV-infected cells.
  • Investigating the role of FMDV proteases (Lpro, 3Cpro) and the 2B protein in regulating RIG-I.
  • Co-immunoprecipitation assays to confirm direct interaction between RIG-I and FMDV 2B.
  • Site-directed mutagenesis of FMDV 2B to identify critical regions for RIG-I interaction and reduction.

Main Results:

  • FMDV infection upregulated RIG-I transcription but decreased its protein expression.
  • FMDV 2B protein, but not Lpro or 3Cpro, directly interacted with RIG-I and reduced its protein levels.
  • The reduction of RIG-I by 2B was specific to FMDV and independent of host cell apoptosis or major degradation pathways.
  • Specific regions within the C-terminus of FMDV 2B (aa 105-114 and 135-144) were essential for RIG-I reduction and interaction.

Conclusions:

  • RIG-I exhibits antiviral activity against FMDV.
  • FMDV employs a novel immune evasion mechanism involving the 2B protein to suppress RIG-I.
  • Understanding this interaction provides insights into FMDV pathogenesis and potential therapeutic targets.

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