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Critical function for Naip5 in inflammasome activation by a conserved carboxy-terminal domain of flagellin.

Inflammasomes are cytosolic multiprotein complexes that sense microbial infection and trigger cytokine production and cell death. However, the molecular components of inflammasomes and what they sense remain poorly defined. Here we demonstrate that 35 amino acids of the carboxyl terminus of flagellin triggered inflammasome activation in the absence of bacterial contaminants or secretion systems. To further elucidate the host flagellin-sensing pathway, we generated mice deficient in the intracellular sensor Naip5. These mice failed to activate the inflammasome in response to the 35 amino acids of flagellin or in response to Legionella pneumophila infection. Our data clarify the molecular basis for the cytosolic response to flagellin.

Pubmed ID: 18724372


  • Lightfield KL
  • Persson J
  • Brubaker SW
  • Witte CE
  • von Moltke J
  • Dunipace EA
  • Henry T
  • Sun YH
  • Cado D
  • Dietrich WF
  • Monack DM
  • Tsolis RM
  • Vance RE


Nature immunology

Publication Data

October 18, 2008

Associated Grants

  • Agency: NIAID NIH HHS, Id: AI070739
  • Agency: NIAID NIH HHS, Id: AI075039
  • Agency: NIAID NIH HHS, Id: K22 AI070739
  • Agency: NIAID NIH HHS, Id: K22 AI070739-02
  • Agency: NIAID NIH HHS, Id: R01 AI075039
  • Agency: NIAID NIH HHS, Id: R01 AI075039-01A2

Mesh Terms

  • Amino Acid Motifs
  • Animals
  • Apoptosis Regulatory Proteins
  • Calcium-Binding Proteins
  • Cytosol
  • Enzyme-Linked Immunosorbent Assay
  • Flagellin
  • Immunoblotting
  • Legionella pneumophila
  • Legionnaires' Disease
  • Macrophages
  • Mice
  • Multiprotein Complexes
  • Neuronal Apoptosis-Inhibitory Protein
  • Toll-Like Receptor 5
  • Transduction, Genetic