HSPD1 interacts with IRF3 to facilitate interferon-beta induction

The production of IFN- I (IFN-α/β) is one of the earliest and most important host-protective responses. Interferon regulatory factor 3 (IRF3) is a critical transcriptional factor in the IFN-β signaling pathway. Although significant progress has been achieved in the regulation of IRF3, the process ma...

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Bibliographic Details
Published in:PloS one 2014-12, Vol.9 (12), p.e114874-e114874
Main Authors: Lin, Lan, Pan, Shan, Zhao, Jianqing, Liu, Cheng, Wang, Pingan, Fu, Lei, Xu, Xinlin, Jin, Meilin, Zhang, Anding
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Biological response modifiers
Biology and Life Sciences
Chaperonin 60 - analysis
Chaperonin 60 - immunology
Chaperonin 60 - metabolism
Dimerization
Health aspects
Heat shock proteins
HEK293 Cells
HeLa Cells
Hsp60 protein
Humans
Infection
Interferon
Interferon regulatory factor
Interferon regulatory factor 3
Interferon Regulatory Factor-3 - analysis
Interferon Regulatory Factor-3 - immunology
Interferon Regulatory Factor-3 - metabolism
Interferon-beta - analysis
Interferon-beta - immunology
Interferon-beta - metabolism
Kinases
Mitochondrial Proteins - analysis
Mitochondrial Proteins - immunology
Mitochondrial Proteins - metabolism
Molecular Sequence Data
Phosphorylation
Protein Interaction Maps
Signal transduction
Signaling
Veterinary colleges
Viral infections
α-Interferon
β-Interferon
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Summary:The production of IFN- I (IFN-α/β) is one of the earliest and most important host-protective responses. Interferon regulatory factor 3 (IRF3) is a critical transcriptional factor in the IFN-β signaling pathway. Although significant progress has been achieved in the regulation of IRF3, the process may be more complicated than previously considered. In the present study, heat shock protein 60 (HSP60, HSPD1) was identified as a novel IRF3-interacting protein. Overexpression of HSPD1 facilitated the phosphorylation and dimerization of IRF3 and enhanced IFN-β induction induced by SeV infection. In contrast, knockdown of endogenous HSPD1 significantly inhibited the signaling pathway. Furthermore, HSPD1 enhanced activation of the IFN-β promoter mediated by RIG-I, MDA-5, MAVS, TBK1 and IKKε but not IRF3/5D, a mock phosphorylated form of IRF3. The present study indicated that HSPD1 interacted with IRF3 and it contributed to the induction of IFN-β.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0114874