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Laboratory and clinical Pseudomonas aeruginosa strains do not bind glycosphingolipids in vitro or during type IV pili-mediated initial host cell attachment

Lori L. Burrows^2,3,

¹ Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, Ontario, Canada
² Research Institute, Hospital for Sick Children, Toronto, Ontario, Canada M5G 1X8
³ Department of Surgery, University of Toronto, Toronto, Ontario, Canada
⁴ Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada

Correspondence
Clifford A. Lingwood
cling{at}sickkids.ca

The glycosphingolipids (GSLs) gangliotriaosylceramide (Gg₃) and gangliotetraosylceramide (Gg₄) have been implicated as receptors for type IV pili (T4P)-mediated Pseudomonas aeruginosa epithelial cell attachment. Since P. aeruginosa T4P are divided into five groups, the authors determined whether GSLs in general, and Gg₃ and Gg₄ in particular, are specifically bound and required for host epithelial cell attachment of clinical and laboratory strains within these groups. An enterohaemorrhagic Escherichia coli strain, CL56, known to bind to both Gg₃ and Gg₄, provided a positive control. TLC overlay showed no binding of more than 12 P. aeruginosa strains to either Gg₃ or Gg₄ (or other GSLs), while CL56 Gg₃/Gg₄ binding was readily detectable. GSL ELISA similarly demonstrated no significant P. aeruginosa binding to Gg₃ or Gg₄, compared with CL56. Using a selective chemical inhibitor, epithelial cell GSL synthesis was abrogated, and Gg₃ and Gg₄ expression deleted, but P. aeruginosa attachment was not impaired. Target cell attachment was mediated by T4P, since non-piliated, but flagellated, mutants were unable to bind to the target cells. CFTR (cystic fibrosis transmembrane conductance regulator) has also been implicated as a receptor; however, in this work, overexpression of CFTR had no effect on P. aeruginosa binding. It is concluded that neither Gg₃ nor Gg₄ are specifically recognized by P. aeruginosa, and that endogenous GSLs do not have a role in the attachment of live intact P. aeruginosa to cultured lung epithelial cells. In contrast to whole piliated P. aeruginosa, T4P sheared from such bacteria showed significant Gg₃ and Gg₄ binding, which may explain the results of other studies.

Present address: Department of Biochemistry and Biomedical Sciences, McMaster University, Rm 4H18 Health Sciences Centre, 1200 Main StW., Hamilton, ON, Canada L8N 3Z5.

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