S. Hopper et al., Effects of the immunoglobulin A1 protease on Neisseria gonorrhoeae trafficking across polarized T84 epithelial monolayers, INFEC IMMUN, 68(2), 2000, pp. 906-911
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
.