Journal of Laryngology & Otology

(RF) Otorhinolaryngology

Pseudomonas aeruginosa lectins I and II and their interaction with human airway cilia

Marco Mewe PhD a1, Denis Tielker MSc a2, Robert Schönberg MD a3, Melitta Schachner PhD a4, Karl-Erich Jaeger PhD a2 and Udo Schumacher PhD a1
a1 Institut für Anatomie II: Experimentelle Morphologie, Germany
a2 Institut für Molekulare Enzymtechnologie, Heinrich-Heine-Universität Düsseldorf, Jülich, Germany
a3 ENT-Klinik, Universitätsklinikum Hamburg-Eppendorf, Hamburg, Germany
a4 Zentrum für Molekulare Neurobiologie, Universität Hamburg, Hamburg, Germany

Article author query
mewe m   [PubMed][Google Scholar] 
tielker d   [PubMed][Google Scholar] 
schönberg r   [PubMed][Google Scholar] 
schachner m   [PubMed][Google Scholar] 
jaeger ke   [PubMed][Google Scholar] 
schumacher u   [PubMed][Google Scholar] 


The bacterium Pseudomonas aeruginosa (PA) produces two carbohydrate binding lectins, designated PA lectin-I and lectin-II (PA-IL, PA-IIL). Both lectins are used by the bacterium to adhere to the glycocalyx of mammalian cells. In addition, the lectins immobilize ciliary beat. The kinetics of ciliary beat inhibition by each individual lectin have been analysed; however, their joint action on cilia has not been reported. Here we demonstrate that PA-IL and PA-IIL inhibit ciliary beat in a similar time-dependent manner. If applied simultaneously, ciliary beat inhibition after five hours of incubation was weaker than if each lectin was applied separately. Thus it can be hypothesized that the lectins compete for the same binding site(s) of the glycocalyx. Sugar inhibition experiments demonstrate that D-galactose and L-fucose inhibit both lectins, although clear preferences of D-galactose for PA-IL and of L-fucose for PA-IIL exist. These interactions have to be kept in mind when designing sugar-based therapies.

Key Words: Bacterial Adhesion; Cilia; Cystic Fibrosis; Lectins; Pseudomonas Aeruginosa; Respiratory Tract Infections.