Effects of the immunoglobulin A1 protease on Neisseria gonorrhoeae trafficking across polarized T84 epithelial monolayers

We previously demonstrated that the Neisseria IgA1 protease cleaves LAMP1 ( lysosome-associated membrane protein 1), a major integral membrane glycopro tein of lysosomes, thereby accelerating its degradation rate in infected A4 31 human epidermoid carcinoma cells and resulting in the alteration of lyso somes in these cells. In this study, we determined whether the IgA1 proteas e also affects the trafficking of Neisseria gonorrhoeae across polarized T8 4 epithelial monolayers. We report that N. gonorrhoeae infection of T84 mon olayers, grown on a solid substrate or polarized on semiporous membranes, a lso results in IgA1 protease-mediated reduction of LAMP1. We demonstrate th at iga mutants in two genetic backgrounds exited polarized T83 monolayers i n fewer numbers than the corresponding wild-type strains. Finally, we prese nt evidence that these mutants have a statistically significant and reprodu cible defect in their ability to traverse T84 monolayers. These results add to our previous data by showing that the IgA1 protease alters lysosomal co ntent in polarized as well as unpolarized cells and by demonstrating a role for the protease in the traversal of epithelial barriers by N. gonorrhoeae .