Send to:

Choose Destination
See comment in PubMed Commons below
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.

Author information

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


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.

[PubMed - indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire Icon for PubMed Central
    Loading ...
    Write to the Help Desk