Listeria monocytogenes impairs SUMOylation for efficient infection
David Ribet,
Mélanie Hamon,
Edith Gouin,
Marie-Anne Nahori,
Francis Impens,
Hélène Neyret-Kahn,
Kris Gevaert,
Joël Vandekerckhove,
Anne Dejean and
Pascale Cossart ()
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David Ribet: Institut Pasteur, Unité des Interactions Bactéries-Cellules
Mélanie Hamon: Institut Pasteur, Unité des Interactions Bactéries-Cellules
Edith Gouin: Institut Pasteur, Unité des Interactions Bactéries-Cellules
Marie-Anne Nahori: Institut Pasteur, Unité des Interactions Bactéries-Cellules
Francis Impens: VIB, B-9000 Ghent, Belgium
Hélène Neyret-Kahn: Institut Pasteur, Unité Organisation Nucléaire et Oncogenèse
Kris Gevaert: VIB, B-9000 Ghent, Belgium
Joël Vandekerckhove: VIB, B-9000 Ghent, Belgium
Anne Dejean: Institut Pasteur, Unité Organisation Nucléaire et Oncogenèse
Pascale Cossart: Institut Pasteur, Unité des Interactions Bactéries-Cellules
Nature, 2010, vol. 464, issue 7292, 1192-1195
Abstract:
Listeria takes on SUMO During infection the food-borne pathogen Listeria monocytogenes exploits a large number of the host cell's functions including post-translational modifications involving ubiquitinylation and phosphorylation, which specifically modify the activity of key proteins. The effects of pathogenic bacteria on the ubiquitin-like modification known as SUMOylation, an essential process in eukaryotic cells, remain largely unknown. Now a study in L. monocytogenes-infected human cells and in a mouse model shows that its virulence factor, listeriolysin O (LLO), induces a decrease in the levels of cellular SUMOylated proteins by triggering degradation of Ubc9, an essential enzyme of the SUMOylation machinery. This work suggests that Listeria — and probably other pathogens too — dampens the host response to infection by decreasing the SUMOylation level of key regulatory proteins.
Date: 2010
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DOI: 10.1038/nature08963
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