title: Modulation of bacterial entry into epithelial cells by association between vinculin and the Shigella IpaA invasin.
abstract: Shigella flexneri is the causative agent of bacillary dysentery in humans. Shigella invasion of epithelial cells is characterized by cytoskeletal rearrangements and formation of cellular projections engulfing the bacterium in a macropinocytic process. We show here that vinculin, a protein involved in linking actin filaments to the plasma membrane, is a direct target of Shigella during cell invasion. IpaA, a Shigella protein secreted upon cell contact, rapidly associates with vinculin during bacterial invasion. Although defective for cell entry, an ipaA mutant is still able to induce foci of actin polymerization, but differs from wild-type Shigella in its ability to recruit vinculin and alpha-actinin. Presumably, IpaA-vinculin interaction initiates the formation of focal adhesion-like structures required for efficient invasion.
authors.affiliation: Unité de Pathogénie Microbienne Moléculaire, INSERM U389, Institut Pasteur, Paris, France.
authors.forename: G
authors.initials: G
authors.lastname: Tran Van Nhieu
authors.forename: A
authors.initials: A
authors.lastname: Ben-Ze'ev
authors.forename: P J
authors.initials: PJ
authors.lastname: Sansonetti
mesh_terms: D000185:Actinin / Q000378:metabolism; D000942:Antigens, Bacterial / Q000235:genetics / Q000378:metabolism*; D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D003599:Cytoskeleton / Q000378:metabolism; D004848:Epithelium / Q000382:microbiology; D006367:HeLa Cells; D006801:Humans; D007150:Immunohistochemistry; D008856:Microscopy, Fluorescence; D008954:Models, Biological; D010873:Pinocytosis; D011485:Protein Binding; D012763:Shigella flexneri / Q000472:pathogenicity*; D016596:Vinculin / Q000378:metabolism*
chemical_list: D000942:Antigens, Bacterial; D001426:Bacterial Proteins; C063664:IpaA protein, Shigella flexneri; D000185:Actinin; D016596:Vinculin