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Infect Immun. 2011 Jul;79(7):2839-46. doi: 10.1128/IAI.01243-10. Epub 2011 Apr 11.

K+ efflux is required for histone H3 dephosphorylation by Listeria monocytogenes listeriolysin O and other pore-forming toxins.

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  • 1Institut Pasteur, Unité des Interactions Bactéries-Cellules, Paris F-75015, France.

Abstract

Chromatin modification triggered by bacteria is a newly described mechanism by which pathogens impact host transcription. Listeria monocytogenes dephosphorylates histone H3 through the action of listeriolysin O (LLO); however, the underlying mechanism is unknown. Here we show that an unrelated pore-forming toxin, Aeromonas aerolysin, also provokes H3 dephosphorylation (dePH3). As reported for aerolysin, we show that LLO and related toxins induce a pore-dependent K(+) efflux and that this efflux is the signal required for dePH3. In addition, LLO-induced K(+) efflux activates caspase-1. However, we demonstrate that dePH3 is unlinked to this activation. Therefore, our study unveils K(+) efflux as an important signal leading to two independent events critical for infection, inflammasome activation and histone modification.

PMID:
21482680
[PubMed - indexed for MEDLINE]
PMCID:
PMC3191964
Free PMC Article
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