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

Research output: Contribution to journalArticle


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.


  • Karla L Lightfield
  • Jenny Persson
  • Sky W Brubaker
  • Chelsea E Witte
  • Jakob von Moltke
  • Eric A Dunipace
  • Thomas Henry
  • Yao-Hui Sun
  • Dragana Cado
  • William F Dietrich
  • Denise M Monack
  • Renée M Tsolis
  • Russell E Vance
External organisations
  • University of California, Berkeley
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Immunology in the medical area


  • Amino Acid Motifs/immunology, Animals, Apoptosis Regulatory Proteins/immunology, Calcium-Binding Proteins/immunology, Cytosol, Enzyme-Linked Immunosorbent Assay, Flagellin/chemistry, Immunoblotting, Legionella pneumophila/immunology, Legionnaires' Disease/immunology, Macrophages/immunology, Mice, Multiprotein Complexes/immunology, Neuronal Apoptosis-Inhibitory Protein/genetics, Toll-Like Receptor 5/immunology, Transduction, Genetic
Original languageEnglish
Pages (from-to)1171-8
Number of pages8
JournalNature Immunology
Issue number10
Publication statusPublished - 2008 Oct
Publication categoryResearch
Externally publishedYes