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

Published online by Cambridge University Press:  08 March 2006

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

Abstract

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.

Type
Research Article
Copyright
© 2005 Royal Society of Medicine Press

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