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K⁺ Efflux Is Required for Histone H3 Dephosphorylation by Listeria monocytogenes Listeriolysin O and Other Pore-Forming Toxins
- Hamon, Mélanie Anne, Cossart, Pascale
- Infection and immunity 2011 v.79 no.7 pp. 2839-2846
- Aeromonas, Listeria monocytogenes, bacteria, chromatin, dephosphorylation, histones, pathogens, potassium, toxins
- 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.