title: Modulation of Neisseria porin (PorB) by cytosolic ATP/GTP of target cells: parallels between pathogen accommodation and mitochondrial endosymbiosis.
abstract: PorB of the pathogenic Neisseria species belongs to the large family of pore-forming proteins (porins) produced by gram-negative bacteria. PorB is exceptional in that it is capable of translocating vectorially into membranes of infected target cells and functions in the infection process. Here we report on an unexpected similarity between Neisserial PorB and mitochondrial porins. Both porin classes interact with purine nucleoside triphosphates, which down-regulate pore size and cause a shift in voltage dependence and ion selectivity. Patch-clamp analyses indicate that PorB channel activity is tightly regulated in intact epithelial cells. In light of recent findings on the pivotal role of PorB in virulence and the prevention of phagosome lysosome fusion, these data provide important mechanistic clues on the intracellular pathogen accommodation reminiscent of mitochondrial endosymbiosis.
authors.affiliation: Max-Planck-Institut für Biologie, Abteilung Infektionsbiologie, Tübingen, Federal Republic of Germany.
authors.forename: T
authors.initials: T
authors.lastname: Rudel
authors.forename: A
authors.initials: A
authors.lastname: Schmid
authors.forename: R
authors.initials: R
authors.lastname: Benz
authors.forename: H A
authors.initials: HA
authors.lastname: Kolb
authors.forename: F
authors.initials: F
authors.lastname: Lang
authors.forename: T F
authors.initials: TF
authors.lastname: Meyer
mesh_terms: D000255:Adenosine Triphosphate / Q000502:physiology*; D001425:Bacterial Outer Membrane Proteins / Q000032:analysis / Q000737:chemistry / Q000378:metabolism*; D001483:Base Sequence; D002462:Cell Membrane / Q000737:chemistry; D002478:Cells, Cultured / Q000166:cytology / Q000502:physiology / Q000648:ultrastructure; D003228:Conjunctiva / Q000166:cytology; D003600:Cytosol / Q000378:metabolism; D004553:Electric Conductivity; D004847:Epithelial Cells; D004848:Epithelium / Q000502:physiology / Q000648:ultrastructure; D006160:Guanosine Triphosphate / Q000502:physiology*; D006801:Humans; D015640:Ion Channel Gating / Q000502:physiology; D008928:Mitochondria / Q000378:metabolism*; D008969:Molecular Sequence Data; D009345:Neisseria meningitidis / Q000737:chemistry / Q000378:metabolism*; D018408:Patch-Clamp Techniques; D018272:Porins / Q000378:metabolism; D011485:Protein Binding / Q000502:physiology; D017386:Sequence Homology, Amino Acid; D013559:Symbiosis / Q000502:physiology*
chemical_list: D001425:Bacterial Outer Membrane Proteins; D018272:Porins; C057699:porin protein, Neisseria; D006160:Guanosine Triphosphate; D000255:Adenosine Triphosphate