title: Listeria monocytogenes transiently alters mitochondrial dynamics during infection.
abstract: Mitochondria are essential and highly dynamic organelles, constantly undergoing fusion and fission. We analyzed mitochondrial dynamics during infection with the human bacterial pathogen Listeria monocytogenes and show that this infection profoundly alters mitochondrial dynamics by causing transient mitochondrial network fragmentation. Mitochondrial fragmentation is specific to pathogenic Listeria monocytogenes, and it is not observed with the nonpathogenic Listeria innocua species or several other intracellular pathogens. Strikingly, the efficiency of Listeria infection is affected in cells where either mitochondrial fusion or fission has been altered by siRNA treatment, highlighting the relevance of mitochondrial dynamics for Listeria infection. We identified the secreted pore-forming toxin listeriolysin O as the bacterial factor mainly responsible for mitochondrial network disruption and mitochondrial function modulation. Together, our results suggest that the transient shutdown of mitochondrial function and dynamics represents a strategy used by Listeria at the onset of infection to interfere with cellular physiology.
authors.affiliation: Unité des Interactions Bactéries-Cellules, Institut Pasteur, U604, Institut National de la Santé et de la Recherche Médicale, Institut National de la Recherche Agronomique, 75015 Paris, France.
authors.forename: Fabrizia
authors.initials: F
authors.lastname: Stavru
authors.forename: Frédéric
authors.initials: F
authors.lastname: Bouillaud
authors.forename: Anna
authors.initials: A
authors.lastname: Sartori
authors.forename: Daniel
authors.initials: D
authors.lastname: Ricquier
authors.forename: Pascale
authors.initials: P
authors.lastname: Cossart
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D017209:Apoptosis / Q000187:drug effects; D001427:Bacterial Toxins / Q000378:metabolism / Q000494:pharmacology; D002118:Calcium / Q000378:metabolism; D019069:Cell Respiration / Q000187:drug effects; D006367:HeLa Cells; D006360:Heat-Shock Proteins / Q000378:metabolism / Q000494:pharmacology; D006460:Hemolysin Proteins / Q000378:metabolism / Q000494:pharmacology; D006801:Humans; D042541:Intracellular Space / Q000187:drug effects / Q000378:metabolism; D008089:Listeria monocytogenes / Q000187:drug effects / Q000502:physiology*; D008088:Listeriosis / Q000378:metabolism* / Q000382:microbiology*; D053078:Membrane Potential, Mitochondrial / Q000187:drug effects; D008928:Mitochondria / Q000187:drug effects / Q000378:metabolism* / Q000382:microbiology*; D011188:Potassium / Q000378:metabolism
chemical_list: D001427:Bacterial Toxins; D006360:Heat-Shock Proteins; D006460:Hemolysin Proteins; D000255:Adenosine Triphosphate; C038705:hlyA protein, Listeria monocytogenes; D011188:Potassium; D002118:Calcium