Gonococcal opacity protein promotes bacterial entry-associated rearrangements of the epithelial cell actin cytoskeleton.

Infection and Immunity
H U GrassméJ P van Putten

Abstract

Neisseria gonorrhoeae enters cultured human mucosal cells following binding of a distinct gonococcal opacity (Opa) outer membrane protein to cell surface proteoglycan receptors. We examined the route of internalization that is activated by Opa-expressing gonococci (strain VP1). Microscopy of infected Chang epithelial cells showed that gonococcal uptake was insensitive to monodansylcadaverine (150 microM), which interferes with clathrin-mediated endocytosis. Similarly, indirect immunofluorescence staining for clathrin in infected cells showed distribution of cellular clathrin unaltered from the distribution in noninfected cells. The microtubule inhibitors colchicine (50 microM) and nocodazole (20 microM) but not the microtubule-stabilizing agent taxol (10 microM) caused a moderate (30 to 50%) reduction in gonococcal entry without affecting bacterial adherence. The most dramatic effects were obtained with the microfilament-disrupting agent cytochalasin D (3 microM), which totally blocked bacterial entry into the cells. Double immunofluorescence staining of gonococci and actin filaments in infected cells demonstrated bacterium-associated accumulations of F-actin as an early signal of bacterial entry. The recruitment of F-actin was...Continue Reading

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Citations

Jun 23, 2006·Infection and Immunity·Christiane KühleweinThomas Rudel
Nov 5, 1997·The Pediatric Infectious Disease Journal·B C Herold
Oct 14, 2000·Annual Review of Cell and Developmental Biology·A J Merz, M So
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Apr 20, 2011·Cellular Microbiology·Karen V SwansonWenxia Song
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Jul 27, 2017·Cellular Microbiology·Hoan Van NgoKeith Ireton
Nov 7, 2000·FEMS Immunology and Medical Microbiology·D BiswasC Sasakawa

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