Cytoplasmic flagellin activates caspase-1 and secretion of interleukin 1beta via Ipaf - PubMed (original) (raw)
doi: 10.1038/ni1344. Epub 2006 Apr 30.
Affiliations
- PMID: 16648853
- DOI: 10.1038/ni1344
Cytoplasmic flagellin activates caspase-1 and secretion of interleukin 1beta via Ipaf
Edward A Miao et al. Nat Immunol. 2006 Jun.
Abstract
Macrophages respond to Salmonella typhimurium infection via Ipaf, a NACHT-leucine-rich repeat family member that activates caspase-1 and secretion of interleukin 1beta. However, the specific microbial salmonella-derived agonist responsible for activating Ipaf is unknown. We show here that cytosolic bacterial flagellin activated caspase-1 through Ipaf but was independent of Toll-like receptor 5, a known flagellin sensor. Stimulation of the Ipaf pathway in macrophages after infection required a functional salmonella pathogenicity island 1 type III secretion system but not the flagellar type III secretion system; furthermore, Ipaf activation could be recapitulated by the introduction of purified flagellin directly into the cytoplasm. These observations raise the possibility that the salmonella pathogenicity island 1 type III secretion system cannot completely exclude 'promiscuous' secretion of flagellin and that the host capitalizes on this 'error' by activating a potent host-defense pathway.
Comment in
- Cytosolic detection of flagellin: a deadly twist.
Roy CR, Zamboni DS. Roy CR, et al. Nat Immunol. 2006 Jun;7(6):549-51. doi: 10.1038/ni0606-549. Nat Immunol. 2006. PMID: 16715062 No abstract available.
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