title: The meningococcal PilT protein is required for induction of intimate attachment to epithelial cells following pilus-mediated adhesion.
abstract: The ability of Neisseria meningitidis (MC) to interact with cellular barriers is essential to its pathogenesis. With epithelial cells, this process has been modeled in two steps. The initial stage of localized adherence is mediated by bacterial pili. After this phase, MC disperse and lose piliation, thus leading to a diffuse adherence. At this stage, microvilli have disappeared, and MC interact intimately with cells and are, in places, located on pedestals of actin, thus realizing attaching and effacing (AE) lesions. The bacterial attributes responsible for these latter phenotypes remain unidentified. Considering that bacteria are nonpiliated at this stage, pili cannot be directly responsible for this effect. However, the initial phase of pilus-mediated localized adherence is required for the occurrence of diffuse adherence, loss of microvilli, and intimate attachment, because nonpiliated bacteria are not capable of such a cellular interaction. In this work, we engineered a mutation in the cytoplasmic nucleotide-binding protein PilT and showed that this mutation increased piliation and abolished the dispersal phase of bacterial clumps as well as the loss of piliation. Furthermore, no intimate attachment nor AE lesions were observed. On the other hand, PilT- MC remained adherent as piliated clumps at all times. Taken together these data demonstrate that the induction of diffuse adherence, intimate attachment, and AE lesions after pilus-mediated adhesion requires the cytoplasmic PilT protein.
authors: Laboratoire de Microbiologie, Institut National de la Santé et de la Recherche Médicale Unité 411, Faculté de Médecine Necker-Enfants Malades, 156 rue de Vaugirard, 75730 Paris Cedex 15, France.
authors: C
authors: C
authors: Pujol
authors: E
authors: E
authors: Eugène
authors: M
authors: M
authors: Marceau
authors: X
authors: X
authors: Nassif
mesh_terms: D000251:Adenosine Triphosphatases; D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000235:genetics / Q000502:physiology*; D001483:Base Sequence; D004847:Epithelial Cells / Q000382:microbiology* / Q000648:ultrastructure; D010861:Fimbriae, Bacterial / Q000502:physiology* / Q000648:ultrastructure; D005798:Genes, Bacterial; D006801:Humans; D008854:Microscopy, Electron; D008855:Microscopy, Electron, Scanning; D008871:Microvilli / Q000648:ultrastructure; D020409:Molecular Motor Proteins; D008969:Molecular Sequence Data; D016254:Mutagenesis, Insertional; D009345:Neisseria meningitidis / Q000235:genetics / Q000472:pathogenicity / Q000502:physiology* / Q000648:ultrastructure; D010641:Phenotype; D016133:Polymerase Chain Reaction; D014407:Tumor Cells, Cultured
chemical_list: D001426:Bacterial Proteins; D020409:Molecular Motor Proteins; D000251:Adenosine Triphosphatases