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Heat Shock-Binding Protein 21 Regulates the Innate Immune Response to Viral Infection
Yan Xu1, Qiong Yang1, Binbin Xue1
1Institute of Pathogen Biology and Immunology of College of Biology, Hunan Provincial Key Laboratory of Medical Virology, State Key Laboratory of Chemo/Biosensing and Chemometrics, Hunan Universitygrid.67293.39, Changsha, China.
Journal of Virology
|March 7, 2022
Summary
Heat shock binding protein 21 (HBP21) promotes antiviral immunity by enhancing interferon production. HBP21 deficiency increases susceptibility to viral infections, highlighting its crucial role in the innate immune response.
Area of Science:
- Immunology
- Molecular Biology
- Virology
Background:
- Interferons (IFNs) are critical for pathogen elimination.
- Heat shock binding protein 21 (HBP21), a molecular chaperone, is known for its role in tumor development.
- The function of HBP21 in antimicrobial immunity was previously unknown.
Purpose of the Study:
- To investigate the role of HBP21 in innate antiviral immunity.
- To elucidate the mechanism by which HBP21 regulates interferon production.
Main Methods:
- Viral infection models (in vitro and in vivo).
- Co-immunoprecipitation assays to study protein interactions.
- Western blotting to assess protein phosphorylation and complex formation.
- Analysis of HBP21 protein structure.
Main Results:
- HBP21 deficiency impaired virus-induced IFN production and increased susceptibility to viral infection.
- HBP21 interacts with IRF3, promoting TBK1-IRF3 complex formation.
- HBP21 inhibits PP2A-mediated dephosphorylation of IRF3, enhancing IRF3 activation.
- Virus-induced phosphorylation of HBP21 at Ser85 and Ser153 is crucial for IRF3 activation.
Conclusions:
- HBP21 acts as a positive regulator of the innate antiviral response.
- HBP21 enhances IFN production through dual regulation of IRF3 activation.
- These findings reveal novel immunological functions of molecular chaperones and provide insights into innate immunity regulation.
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