Critical function for Naip5 in inflammasome activation by a conserved carboxy-terminal domain of flagellin
(2008) In Nature Immunology 9(10). p.8-1171- 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.
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- author
- publishing date
- 2008-10
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- 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
- in
- Nature Immunology
- volume
- 9
- issue
- 10
- pages
- 8 pages
- publisher
- Nature Publishing Group
- external identifiers
-
- scopus:52549099416
- pmid:18724372
- ISSN
- 1529-2908
- DOI
- 10.1038/ni.1646
- language
- English
- LU publication?
- no
- id
- 5f8643d2-2a46-4f9d-baae-e587a0dbdab1
- date added to LUP
- 2019-05-21 09:01:21
- date last changed
- 2024-06-25 14:10:33
@article{5f8643d2-2a46-4f9d-baae-e587a0dbdab1,
abstract = {{<p>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.</p>}},
author = {{Lightfield, Karla L and Persson, Jenny and Brubaker, Sky W and Witte, Chelsea E and von Moltke, Jakob and Dunipace, Eric A and Henry, Thomas and Sun, Yao-Hui and Cado, Dragana and Dietrich, William F and Monack, Denise M and Tsolis, Renée M and Vance, Russell E}},
issn = {{1529-2908}},
keywords = {{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}},
language = {{eng}},
number = {{10}},
pages = {{8--1171}},
publisher = {{Nature Publishing Group}},
series = {{Nature Immunology}},
title = {{Critical function for Naip5 in inflammasome activation by a conserved carboxy-terminal domain of flagellin}},
url = {{http://dx.doi.org/10.1038/ni.1646}},
doi = {{10.1038/ni.1646}},
volume = {{9}},
year = {{2008}},
}