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...
Gespeichert in:
| Hauptverfasser: | , , , , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
2006
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| In: |
Infection and immunity
Year: 2006, Jahrgang: 74, Heft: 10, Pages: 5687-5692 |
| ISSN: | 1098-5522 |
| DOI: | 10.1128/IAI.01940-05 |
| Online-Zugang: | 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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| Verfasserangaben: | Sabine Zimmermann, Christof Wagner, Wencke Müller, Gerald Brenner-Weiss, Friederike Hug, Birgit Prior, Ursula Obst, and Gertrud Maria Hänsch |
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| 245 | 1 | 0 | |a Induction of neutrophil chemotaxis by the quorum-sensing molecule N-(3-oxododecanoyl)-L-homoserine lactone |c Sabine Zimmermann, Christof Wagner, Wencke Müller, Gerald Brenner-Weiss, Friederike Hug, Birgit Prior, Ursula Obst, and Gertrud Maria Hänsch |
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| 520 | |a 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. | ||
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