title: The Salmonella effector protein PipB2 is a linker for kinesin-1.
abstract: Understanding the mechanisms of Salmonella virulence is an important challenge. The capacity of this intracellular bacterial pathogen to cause diseases depends on the expression of virulence factors including the second type III secretion system (TTSS-2), which is used to translocate into the eukaryotic cytosol a set of effector proteins that divert the biology of the host cell and shape the bacterial replicative niche. Yet little is known about the eukaryotic functions affected by individual Salmonella effectors. Here we report that the TTSS-2 effector PipB2 interacts with the kinesin light chain, a subunit of the kinesin-1 motor complex that drives anterograde transport along microtubules. Translocation of PipB2 is both necessary and sufficient for the recruitment of kinesin-1 to the membrane of the Salmonella-containing vacuole. In vivo, PipB2 contributes to the attenuation of Salmonella mutant strains in mice. Taken together, our data indicate that the TTSS-2-mediated fine-tuning of kinesin-1 activity associated with the bacterial vacuole is crucial for the virulence of Salmonella.
authors.affiliation: Centre d'Immunologie de Marseille-Luminy, Centre National de la Recherche Scientifique, Institut National de la Santé et de la Recherche Médicale, Université de la Méditerranée, Parc Scientifique de Luminy, Marseille, France.
authors.forename: Thomas
authors.initials: T
authors.lastname: Henry
authors.forename: Carole
authors.initials: C
authors.lastname: Couillault
authors.forename: Patrick
authors.initials: P
authors.lastname: Rockenfeller
authors.forename: Emmanuel
authors.initials: E
authors.lastname: Boucrot
authors.forename: Audrey
authors.initials: A
authors.lastname: Dumont
authors.forename: Nina
authors.initials: N
authors.lastname: Schroeder
authors.forename: Aurélie
authors.initials: A
authors.lastname: Hermant
authors.forename: Leigh A
authors.initials: LA
authors.lastname: Knodler
authors.forename: Patrick
authors.initials: P
authors.lastname: Lecine
authors.forename: Olivia
authors.initials: O
authors.lastname: Steele-Mortimer
authors.forename: Jean-Paul
authors.initials: JP
authors.lastname: Borg
authors.forename: Jean-Pierre
authors.initials: JP
authors.lastname: Gorvel
authors.forename: Stéphane
authors.initials: S
authors.lastname: Méresse
mesh_terms: D000818:Animals; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D001854:Bone Marrow Cells / Q000166:cytology; D002454:Cell Differentiation; D002460:Cell Line; D002478:Cells, Cultured; D005260:Female; D005269:Femur / Q000166:cytology; D017353:Gene Deletion; D006367:HeLa Cells; D006801:Humans; D016547:Kinesins / Q000378:metabolism*; D008264:Macrophages / Q000378:metabolism / Q000382:microbiology; D051379:Mice; D008807:Mice, Inbred BALB C; D008810:Mice, Inbred C57BL; D012475:Salmonella / Q000145:classification / Q000235:genetics / Q000254:growth & development / Q000378:metabolism* / Q000472:pathogenicity*; D012481:Salmonella Infections, Animal / Q000382:microbiology; D014617:Vacuoles / Q000382:microbiology; D014774:Virulence
chemical_list: D001426:Bacterial Proteins; C478165:PipB2 protein, Salmonella enterica; D016547:Kinesins