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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Toxins / genetics
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Bacterial Toxins / metabolism*
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Caspase 1 / metabolism
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Cell Line, Tumor
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Cholesterol / pharmacology
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Chromatin / metabolism
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Cytotoxins / metabolism
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HeLa Cells
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Heat-Shock Proteins / metabolism*
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Hemolysin Proteins / metabolism*
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Histones / metabolism*
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Humans
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Immunoblotting
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Inflammasomes / metabolism
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Listeria monocytogenes / genetics
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Listeria monocytogenes / metabolism*
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Listeria monocytogenes / pathogenicity
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Phosphorylation
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Pore Forming Cytotoxic Proteins / metabolism*
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Potassium / metabolism*
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Protein Processing, Post-Translational
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Signal Transduction
Substances
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Bacterial Toxins
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Chromatin
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Cytotoxins
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Heat-Shock Proteins
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Hemolysin Proteins
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Histones
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Inflammasomes
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Pore Forming Cytotoxic Proteins
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aerolysin
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Cholesterol
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Caspase 1
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hlyA protein, Listeria monocytogenes
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Potassium