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Infection and Immunity, July 1999, p. 3207-3214, Vol. 67, No. 7
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Pili Binding to Asialo-GM1 on Epithelial Cells Can Mediate Cytotoxicity or Bacterial Internalization by Pseudomonas aeruginosa

James C. Comolli,1,dagger Leslie L. Waite,1,Dagger Keith E. Mostov,2,3,4 and Joanne N. Engel1,5,*

Departments of Medicine,1 Anatomy,2 Biochemistry3 and Microbiology and Immunology5 and Cardiovascular Research Institute,4 University of California, San Francisco, San Francisco, California 94143

Received 16 March 1999/Returned for modification 5 April 1999/Accepted 15 April 1999

The interaction of Pseudomonas aeruginosa type IV pili and the glycosphingolipid asialo-GM1 (aGM1) can mediate bacterial adherence to epithelial cells, but the steps subsequent to this adherence have not been elucidated. To investigate the result of the interaction of pili and aGM1, we used polarized epithelial monolayers of Madin-Darby canine kidney (MDCK) cells in culture, which contained little detectable aGM1 on their apical surface but were able to incorporate exogenous aGM1. Compared to an untreated monolayer, P. aeruginosa PA103 displayed an eightfold increase in association with and fivefold more cytotoxicity toward MDCK cells pretreated with aGM1. Cytotoxicity of either carrier-treated or aGM1-treated monolayers required the type III secreted protein ExoU. Asialo-GM1 pretreatment of MDCK monolayers likewise augmented bacterial internalization of an isogenic invasive strain approximately fourfold. These increases were not seen in monolayers treated with GM1, the sialyated form of the glycolipid, and were inhibited by treatment with an antibody to aGM1. Also, the aGM1-mediated adhesion, cytotoxicity, and internalization required intact type IV pili since nonpiliated PA103 mutants were unaffected by aGM1 pretreatment of MDCK cells. These results demonstrate that epithelial cell injury and bacterial internalization can proceed from the same adhesin-receptor interaction, and they indicate that P. aeruginosa exoproducts solely determine the steps subsequent to adhesion.

* Corresponding author. Mailing address: Division of Infectious Disease, Box 0654, University of California, San Francisco, CA 94143-0654. Phone: (415) 476-7355. Fax: (415) 476-9364. E-mail: Jengel{at}medicine.ucsf.edu.

dagger Present address: Department of Bacteriology, University of Wisconsin, Madison, Madison, WI 53706.

Dagger Present address: Department of Obstetrics and Gynecology, University of California, San Francisco, San Francisco, CA 04143.

Infection and Immunity, July 1999, p. 3207-3214, Vol. 67, No. 7
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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