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Infection and Immunity, February 2001, p. 719-729, Vol. 69, No. 2
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.2.719-729.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Lack of Adherence of Clinical Isolates of Pseudomonas aeruginosa to Asialo-GM1 on Epithelial Cells

Torsten H. Schroeder,dagger Tanweer Zaidi, and Gerald B. Pier*

Channing Laboratory, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115

Received 14 August 2000/Returned for modification 9 October 2000/Accepted 24 October 2000

Numerous studies have reported that asialo-GM1, gangliotetraosylceramide, or moieties serve as epithelial cell receptors for Pseudomonas aeruginosa. Usually this interaction is confirmed with antibodies to asialo-GM1. However, few, if any, of these reports have evaluated the binding of fresh clinical isolates of P. aeruginosa to asialo-GM1 or the specificity of the antibodies for the asialo-GM1 antigen. We confirmed that asialo-GM1 dissolved in dimethyl sulfoxide could be added to the apical membrane of Madin-Darby canine kidney cells growing as a polarized epithelium on Transwell membranes (J. C. Comolli, L. L. Waite, K. E. Mostov, and J. N. Engel, Infect. Immun. 67:3207-3214, 1999) and that such treatment enhanced the binding of P. aeruginosa strain PA103. However, no other P. aeruginosa strain, including eight different clinical isolates, exhibited enhanced binding to asialo-GM1-treated cells. Studies with commercially available antibodies to asialo-GM1 showed that these preparations had high titers of antibody to P. aeruginosa antigens, including whole cells, purified lipopolysaccharide (LPS), and pili. Inhibition studies showed that adsorption of an antiserum to asialo-GM1 with P. aeruginosa cells could remove the reactivity of antibodies to asialo-GM1, and adsorption of this serum with asialo-GM1 removed antibody binding to P. aeruginosa LPS. Antibodies in sera raised to asialo-GM1 were observed to bind to P. aeruginosa cells by immunoelectron microscopy. Antibodies to asialo-GM1 inhibited formation of a biofilm by P. aeruginosa in the absence of mammalian cells, indicating a direct inhibition of bacterial cell-cell interactions. These findings demonstrate that asialo-GM1 is not a major cellular receptor for clinical isolates of P. aeruginosa and that commercially available antibodies raised to this antigen contain high titers of antibody to multiple P. aeruginosa antigens, which do not interfere with the binding of P. aeruginosa to mammalian cells but possibly interfere with the binding of P. aeruginosa cells to each other.

* Corresponding author. Mailing address: Channing Laboratory, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115-5804. Phone: (617) 525-2269. Fax: (617) 731-1541. E-mail: gpier{at}channing.harvard.edu.

dagger Present address: Department of Anesthesiology, Tübingen University Hospital, 72076 Tübingen, Germany.

Infection and Immunity, February 2001, p. 719-729, Vol. 69, No. 2
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.2.719-729.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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