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- W1569346092 abstract "The facultative intracellular bacterium Bartonella henselae enters humanendothelial cells either passively by conventional phagocytosis or actively by apathogen-triggered process known as invasome-mediated internalization. The latterinvolves the formation of a cell-surface-associated bacterial aggregate, which issubsequently engulfed by host cell membranes eventually resulting in its completeinternalization.Recent work indicated that invasome formation of B. henselae depends on itsVirB/VirD4 T4SS.This work describes that the VirB/VirD4 T4SS of B. henselae injects a cocktailof seven effector proteins into endothelial host cells to subvert cellular functions andthat one of these translocated effector proteins, BepG, mediates the sustainedcytoskeletal changes leading to invasome formation. Moreover, this work indicates theexistence of two non-redundant pathways to promote invasome formation, one ofwhich is governed by the action of BepG and another one, involving further Bepproteins, which is BepG-independent.On the host cell side, Rho-family small GTPases Cdc42 and Rac1, but not RhoAare shown to be required for invasome-mediated internalization. Furthermore, it isshown that invasome formation leads both to the rearrangement of pre-existing F-actinfibers and to localized actin polymerization enriched for Arp2/3, which occurs in aScar1/WAVE-dependent manner. Finally, this work provides evidence that aftercomplete internalization the invasome membranes do not fuse with Lamp-1 positivelysosomes, indicating that invasome-mediated invasion represents a novel mechanismallowing the uptake of bacteria without entering the endocytic-lysosomal pathway.Importantly, this is the first report, which attributes the orchestrated action ofmore than one effector protein of B. henselae to a known VirB/VirD4 T4SS-dependentphenotype, namely invasome formation, which represents a multifacetted example forthe complexity of host cell subversion by a bacterial pathogen." @default.
- W1569346092 created "2016-06-24" @default.
- W1569346092 creator A5017626635 @default.
- W1569346092 date "2007-01-01" @default.
- W1569346092 modified "2023-09-25" @default.
- W1569346092 title "Molecular and cellular basis of the internalization of Bartonella henselae by human endothelial cells" @default.
- W1569346092 doi "https://doi.org/10.5451/unibas-004112968" @default.
- W1569346092 hasPublicationYear "2007" @default.
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