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Interaction of bacterial lectins with human lung epithelium
Vyhnalová, Kateřina ; Hodek, Petr (advisor) ; Bořek Dohalská, Lucie (referee)
Cystic fibrosis (CF) is an autosomal recessive disease caused by mutations in the CFTR (cystic fibrosis transmembrane conductance regulator) gene encoding the same named chloride channel, which is present on the apical membrane of epithelial cells. As a consequence of these mutations, the transepithelial transport of ions and the regulation of other ion channels are impaired. Cystic fibrosis affects primarily respiratory system, where, as a result of the dysfunction of the CFTR protein, is an accumulation of excessively viscous mucus and altered glycosylation of saccharide structures on the surface of the lung epithelium. This pathological condition predisposes CF patients to bacterial lung infections, the leading cause of death in CF patients. The most common pathogen colonizing the respiratory system of CF patients is Pseudomonas aeruginosa (PA). For adhesion to host tissue, PA uses several virulence factors, including lectin PA-IIL, which exhibits an unusually high affinity for L-fucose. In this work the influence of selected monosaccharides and multivalent fucose-based inhibitors (glycoclusters) on PA-IIL binding to human lung epithelium was investigated. To assess the effect of these agens ex vivo, paraffin-embedded formalin-fixed human lung tissues (FFPE tissues) from a healthy individual and...
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