Journal
JOURNAL OF LEUKOCYTE BIOLOGY
Volume 82, Issue 2, Pages 220-225Publisher
WILEY
DOI: 10.1189/jlb.1206756
Keywords
NLR; TLR; ASC; Ipaf; cryopyrin
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Funding
- NHLBI NIH HHS [5/T32/HL007517] Funding Source: Medline
- NIAID NIH HHS [AI063331] Funding Source: Medline
- PHS HHS [A/064748] Funding Source: Medline
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Nucleotide-binding and oligomerization domain-like receptors (NLRs) constitute a family of germline-encoded pattern-recognition receptors, which allow the host to respond rapidly to a wide variety of pathogenic microorganisms. Here, we discuss recent advances in the study of a subset of NLRs, which control the activation of caspase-1 through the assembly of large protein complexes, inflammasomes. The NALP1b inflammasome recognizes anthrax lethal toxin, and flagellin from Salmonella and Legionella induces assembly of the Ipaf inflammasome. Cryopyrin/NALP3 mediates caspase-1 activation in response to a wide variety of bacterial ligands, imidazoquinolines, dsRNA, and the endogenous danger signal uric acid. The importance of these cytosolic receptors in immune regulation is underscored by the identification of mutations in cryopyrin/NALP3, which are genetically linked to human autoinflammatory disorders.
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