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

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Pseudomonas aeruginosa lectins I and II and their interaction with human airway cilia. / Mewe, Marco; Tielker, Denis; Schönberg, Robert; Schachner, Melitta; Jaeger, Karl-Erich; Schumacher, Udo.

in: The Journal of laryngology and otology, Jahrgang 119, Nr. 8, 08.2005, S. 595-9.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Mewe, M, Tielker, D, Schönberg, R, Schachner, M, Jaeger, K-E & Schumacher, U 2005, 'Pseudomonas aeruginosa lectins I and II and their interaction with human airway cilia', The Journal of laryngology and otology, Jg. 119, Nr. 8, S. 595-9. https://doi.org/10.1258/0022215054516313

APA

Mewe, M., Tielker, D., Schönberg, R., Schachner, M., Jaeger, K-E., & Schumacher, U. (2005). Pseudomonas aeruginosa lectins I and II and their interaction with human airway cilia. The Journal of laryngology and otology, 119(8), 595-9. https://doi.org/10.1258/0022215054516313

Vancouver

Mewe M, Tielker D, Schönberg R, Schachner M, Jaeger K-E, Schumacher U. Pseudomonas aeruginosa lectins I and II and their interaction with human airway cilia. The Journal of laryngology and otology. 2005 Aug;119(8):595-9. https://doi.org/10.1258/0022215054516313

Bibtex

@article{5d8db9d1242b47ab9bbd557c3b83160f,
title = "Pseudomonas aeruginosa lectins I and II and their interaction with human airway cilia",
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.",
keywords = "Adhesins, Bacterial, Bacterial Adhesion, Binding Sites, Cilia, Fucose, Galactose, Histocytochemistry, Humans, Lectins, Microscopy, Phase-Contrast, Nasal Mucosa, Pseudomonas aeruginosa, Tissue Culture Techniques",
author = "Marco Mewe and Denis Tielker and Robert Sch{\"o}nberg and Melitta Schachner and Karl-Erich Jaeger and Udo Schumacher",
year = "2005",
month = aug,
doi = "10.1258/0022215054516313",
language = "English",
volume = "119",
pages = "595--9",
journal = "J LARYNGOL OTOL",
issn = "0022-2151",
publisher = "Cambridge University Press",
number = "8",

}

RIS

TY - JOUR

T1 - Pseudomonas aeruginosa lectins I and II and their interaction with human airway cilia

AU - Mewe, Marco

AU - Tielker, Denis

AU - Schönberg, Robert

AU - Schachner, Melitta

AU - Jaeger, Karl-Erich

AU - Schumacher, Udo

PY - 2005/8

Y1 - 2005/8

N2 - 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.

AB - 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.

KW - Adhesins, Bacterial

KW - Bacterial Adhesion

KW - Binding Sites

KW - Cilia

KW - Fucose

KW - Galactose

KW - Histocytochemistry

KW - Humans

KW - Lectins

KW - Microscopy, Phase-Contrast

KW - Nasal Mucosa

KW - Pseudomonas aeruginosa

KW - Tissue Culture Techniques

U2 - 10.1258/0022215054516313

DO - 10.1258/0022215054516313

M3 - SCORING: Journal article

C2 - 16102212

VL - 119

SP - 595

EP - 599

JO - J LARYNGOL OTOL

JF - J LARYNGOL OTOL

SN - 0022-2151

IS - 8

ER -