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Asc Modulates the Function of NLRC4 in Response to Infection of Macrophages by Legionella pneumophila

Authors
Journal
mBio
2150-7511
Publisher
American Society for Microbiology
Publication Date
Volume
2
Issue
4
Identifiers
DOI: 10.1128/mbio.00117-11
Keywords
  • Research Article
Disciplines
  • Biology

Abstract

IMPORTANCE Caspase-1 is a protease activated during infection that is central to the regulation of several innate immune pathways. Studies examining the macromolecular complexes containing this protein, known as inflammasomes, have provided insight into the regulation of this protease. This work demonstrates that the intracellular bacterium Legionella pneumophila induces formation of complexes containing caspase-1 by multiple mechanisms and illustrates that an adapter molecule called Asc integrates signals from multiple independent upstream caspase-1 activators in order to assemble a spatially distinct complex in the macrophage. There were caspase-1-associated activities such as cytokine processing and secretion that were controlled by Asc. Importantly, this work uncovered a new role for Asc in dampening a caspase-1-dependent cell death pathway called pyroptosis. These findings suggest that Asc plays a central role in controlling a distinct subset of caspase-1-dependent activities by both assembling complexes that are important for cytokine processing and suppressing processes that mediate pyroptosis.

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