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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