Cytoskeleton and motor proteins are required for the transcytosis of Neisseria gonorrhoeae through polarized epithelial cells.
Neisseria gonorrhoeae interact with polarized T84 epithelial cells by engaging carcinoembryonic antigen-related cellular adhesion molecule (CEACAM) receptors. Adherent bacteria that are taken up by the cells are able to traverse the epithelial layer from the apical to the basal side. Herein, we demonstrate that the actin cytoskeleton of the cells is not required for the initial adherence of the bacteria, however, it is essential for invasion into and traversal through T84 cells. Furthermore, microtubule inhibitors blocked the traversal, but not the adherence and invasion of the bacteria. Inhibition of the motor activity of myosins reduced invasion and traversal, but not bacterial adherence. Immunofluorescence confocal laser scanning microscopy revealed the colocalization of the microtubule-based kinesin and dynein motors, and the actin-based motor myosin with adherent and intracellular gonococci. Transcytosis was reduced by blocking kinesin and myosin with specific antibodies. This underlines the importance of these motor proteins for the transcytosis of epithelial monolayers by N. gonorrhoeae.
Department of Molecular Biology, Max Planck Institute for Infection Biology, Charitéplatz 1, D-10117 Berlin, Germany.
Jun A
JA
Wang
Thomas F
TF
Meyer
Thomas
T
Rudel
D000199:Actins / Q000502:physiology; D001422:Bacterial Adhesion / Q000187:drug effects / Q000502:physiology*; D015815:Cell Adhesion Molecules / Q000502:physiology*; D003110:Colonic Neoplasms; D003598:Cytoskeletal Proteins / Q000502:physiology*; D004398:Dyneins / Q000502:physiology; D004847:Epithelial Cells / Q000382:microbiology* / Q000502:physiology*; D006069:Gonorrhea / Q000209:etiology; D006801:Humans; D016547:Kinesins / Q000502:physiology; D008870:Microtubules / Q000502:physiology; D020409:Molecular Motor Proteins / Q000276:immunology / Q000502:physiology*; D009218:Myosins / Q000502:physiology; D009344:Neisseria gonorrhoeae / Q000502:physiology*; D015739:Nocodazole / Q000494:pharmacology; D017239:Paclitaxel / Q000494:pharmacology; D014407:Tumor Cells, Cultured; D014747:Vinblastine / Q000494:pharmacology
D000199:Actins; D015815:Cell Adhesion Molecules; D003598:Cytoskeletal Proteins; D020409:Molecular Motor Proteins; D014747:Vinblastine; D009218:Myosins; D004398:Dyneins; D016547:Kinesins; D017239:Paclitaxel; D015739:Nocodazole