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Induction of neutrophil chemotaxis by the quorum-sensing molecule N-(3-oxododecanoyl)-L-homoserine lactone

Acyl homoserine lactones are synthesized by Pseudomonas aeruginosa as signaling molecules which control production of virulence factors and biofilm formation in a paracrine manner. We found that N-(3-oxododecanoyl)-L-homoserine lactone (3OC12-HSL), but not its 3-deoxo isomer or acyl-homoserine lacto...

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Main Authors: Zimmermann, Sabine (Author) , Wagner, Christof (Author) , Müller, Wencke Eike (Author) , Brenner-Weiss, Gerald (Author) , Hug, Friederike (Author) , Prior, Birgit (Author) , Obst, Ursula (Author) , Hänsch, Gertrud Maria (Author)
Format: Article (Journal)
Language:English
Published: 2006
In: Infection and immunity
Year: 2006, Volume: 74, Issue: 10, Pages: 5687-5692
ISSN:1098-5522
DOI:10.1128/IAI.01940-05
Online Access:Verlag, lizenzpflichtig, Volltext: https://dx.doi.org/10.1128/IAI.01940-05
Verlag, lizenzpflichtig, Volltext: https://journals.asm.org/doi/epub/10.1128/IAI.01940-05
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Author Notes:Sabine Zimmermann, Christof Wagner, Wencke Müller, Gerald Brenner-Weiss, Friederike Hug, Birgit Prior, Ursula Obst, and Gertrud Maria Hänsch
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Summary:Acyl homoserine lactones are synthesized by Pseudomonas aeruginosa as signaling molecules which control production of virulence factors and biofilm formation in a paracrine manner. We found that N-(3-oxododecanoyl)-L-homoserine lactone (3OC12-HSL), but not its 3-deoxo isomer or acyl-homoserine lactones with shorter fatty acids, induced the directed migration (chemotaxis) of human polymorphonuclear neutrophils (PMN) in vitro. By use of selective inhibitors a signaling pathway, comprising phosphotyrosine kinases, phospholipase C, protein kinase C, and mitogen-activated protein kinase C, could be delineated. In contrast to the well-studied chemokines complement C5a and interleukin 8, the chemotaxis did not depend on pertussis toxin-sensitive G proteins, indicating that 3OC12-HSL uses another signaling pathway. Strong evidence for the presence of a receptor for 3OC12-HSL on PMN was derived from uptake studies; by use of radiolabeled 3OC12-HSL, specific and saturable binding to PMN was seen. Taken together, our data provide evidence that PMN recognize and migrate toward a source of 3OC12-HSL (that is, to the site of a developing biofilm). We propose that this early attraction of PMN could contribute to prevention of biofilm formation.
Item Description:Gesehen am 30.06.2021
Physical Description:Online Resource
ISSN:1098-5522
DOI:10.1128/IAI.01940-05

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