Critical function for Naip5 in inflammasome activation by a conserved carboxy-terminal domain of 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, Renee M Tsolis, Russell E. Vance

Research output: Contribution to journalArticle

334 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)1171-1178
Number of pages8
JournalNature Immunology
Volume9
Issue number10
DOIs
StatePublished - 2008

ASJC Scopus subject areas

  • Immunology

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    Lightfield, K. L., Persson, J., Brubaker, S. W., Witte, C. E., von Moltke, J., Dunipace, E. A., Henry, T., Sun, Y. H., Cado, D., Dietrich, W. F., Monack, D. M., Tsolis, R. M., & Vance, R. E. (2008). Critical function for Naip5 in inflammasome activation by a conserved carboxy-terminal domain of flagellin. Nature Immunology, 9(10), 1171-1178. https://doi.org/10.1038/ni.1646