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GBP5 promotes NLRP3 inflammasome assembly and immunity in mammals.

Science (New York, N.Y.) | Apr 27, 2012

http://www.ncbi.nlm.nih.gov/pubmed/22461501

Inflammasomes are sensory complexes that alert the immune system to the presence of infection or tissue damage. These complexes assemble NLR (nucleotide binding and oligomerization, leucine-rich repeat) or ALR (absent in melanoma 2-like receptor) proteins to activate caspase-1 cleavage and interleukin (IL)-1β/IL-18 secretion. Here, we identified a non-NLR/ALR human protein that stimulates inflammasome assembly: guanylate binding protein 5 (GBP5). GBP5 promoted selective NLRP3 inflammasome responses to pathogenic bacteria and soluble but not crystalline inflammasome priming agents. Generation of Gbp5(-/-) mice revealed pronounced caspase-1 and IL-1β/IL-18 cleavage defects in vitro and impaired host defense and Nlrp3-dependent inflammatory responses in vivo. Thus, GBP5 serves as a unique rheostat for NLRP3 inflammasome activation and extends our understanding of the inflammasome complex beyond its core machinery.

Pubmed ID: 22461501 RIS Download

Mesh terms: Alum Compounds | Animals | Apoptosis Regulatory Proteins | Carrier Proteins | Caspase 1 | Cell Line | Cytoskeletal Proteins | GTP-Binding Proteins | Humans | Inflammasomes | Interferon-gamma | Interleukin-1beta | Lipopolysaccharides | Listeria monocytogenes | Listeriosis | Macrophages | Mice | Protein Multimerization | RNA Interference | Salmonella typhimurium | Uric Acid

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Associated grants

  • Agency: NIAID NIH HHS, Id: R01 AI068041-06
  • Agency: Howard Hughes Medical Institute, Id:

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