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Infection and Immunity, November 2002, p. 5965-5971, Vol. 70, No. 11
0019-9567/02/$04.00+0     DOI: 10.1128/IAI.70.11.5965-5971.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Neisseria gonorrhoeae Porin P1.B Induces Endosome Exocytosis and a Redistribution of Lamp1 to the Plasma Membrane

Department of Molecular Microbiology and Immunology, L220, Oregon Health and Science University, Portland, Oregon 97201,¹ Division of Infectious Diseases, Boston University School of Medicine and Evans Biomedical Research Center, Boston, Massachusetts 02118²

Received 12 April 2002/ Returned for modification 13 June 2002/ Accepted 6 August 2002

The immunoglobulin A (IgA) protease secreted by pathogenic Neisseria spp. cleaves Lamp1, thereby altering lysosomes in a cell and promoting bacterial intracellular survival. We sought to determine how the IgA protease gains access to cellular Lamp1 in order to better understand the role of this cleavage event in bacterial infection. In a previous report, we demonstrated that the pilus-induced Ca²⁺ transient triggers lysosome exocytosis in human epithelial cells. This, in turn, increases the level of Lamp1 at the plasma membrane, where it can be cleaved by IgA protease. Here, we show that porin also induces a Ca²⁺ flux in epithelial cells. This transient is similar in nature to that observed in phagocytes exposed to porin. In contrast to the pilus-induced Ca²⁺ transient, the porin-induced event does not trigger lysosome exocytosis. Instead, it stimulates exocytosis of early and late endosomes and increases Lamp1 on the cell surface. These results indicate that Neisseria pili and porin perturb Lamp1 trafficking in epithelial cells by triggering separate and distinct Ca²⁺-dependent exocytic events, bringing Lamp1 to the cell surface, where it can be cleaved by IgA protease.

Editor: E. I. Tuomanen

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