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1:
Proc Natl Acad Sci U S A.
2007 Aug 14;104(33):13467-72. Epub 2007 Aug 3.
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Erratum in:
Proc Natl Acad Sci U S A. 2007 Oct 30;104(44):17555.
Histone modifications induced by a family of bacterial toxins.
Hamon MA
,
Batsché E
,
Régnault B
,
Tham TN
,
Seveau S
,
Muchardt C
,
Cossart P
.
Unité des Interactions Bactéries-Cellules, Unité de Régulation pigénétique, and Génopole, Plate-forme 2, Institut Pasteur, F-75015 Paris, France.
Upon infection, pathogens reprogram host gene expression. In eukaryotic cells, genetic reprogramming is induced by the concerted activation/repression of transcription factors and various histone modifications that control DNA accessibility in chromatin. We report here that the bacterial pathogen Listeria monocytogenes induces a dramatic dephosphorylation of histone H3 as well as a deacetylation of histone H4 during early phases of infection. This effect is mediated by the major listerial toxin listeriolysin O in a pore-forming-independent manner. Strikingly, a similar effect also is observed with other toxins of the same family, such as Clostridium perfringens perfringolysin and Streptococcus pneumoniae pneumolysin. The decreased levels of histone modifications correlate with a reduced transcriptional activity of a subset of host genes, including key immunity genes. Thus, control of epigenetic regulation emerges here as an unsuspected function shared by several bacterial toxins, highlighting a common strategy used by intracellular and extracellular pathogens to modulate the host response early during infection.
Publication Types:
Research Support, Non-U.S. Gov't
PMID: 17675409 [PubMed - indexed for MEDLINE]
PMCID: PMC1948930
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