Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0023241 (Legionella)
 6,990 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Nods are cytosolic proteins that contain a nucleotide-binding oligomerization domain (NOD). These proteins include key regulators of apoptosis and pathogen resistance in mammals and plants. A large number of Nods contain leucine-rich repeats (LRRs), hence referred to as NOD-LRR proteins. Genetic variation in several NOD-LRR proteins, including human Nod2, Cryopyrin, and CIITA, as well as mouse Naip5, is associated with inflammatory disease or increased susceptibility to microbial infections. Nod1, Nod2, Cryopyrin, and Ipaf have been implicated in protective immune responses against pathogens. Together with Toll-like receptors, Nod1 and Nod2 appear to play important roles in innate and acquired immunity as sensors of bacterial components. Specifically, Nod1 and Nod2 participate in the signaling events triggered by host recognition of specific motifs in bacterial peptidoglycan and, upon activation, induce the production of proinflammatory mediators. Naip5 is involved in host resistance to Legionella pneumophila through cell autonomous mechanisms, whereas CIITA plays a critical role in antigen presentation and development of antigen-specific T lymphocytes. Thus, NOD-LRR proteins appear to be involved in a diverse array of processes required for host immune reactions against pathogens.
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PMID:NOD-LRR proteins: role in host-microbial interactions and inflammatory disease. 1595 91

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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PMID:Caspase-1 inflammasomes in infection and inflammation. 1744 55