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

• Verfasst von: Zimmermann, Sabine [VerfasserIn]
• Verfasst von: Wagner, Christof [VerfasserIn]
• Verfasst von: Müller, Wencke Eike [VerfasserIn]
• Verfasst von: Brenner-Weiss, Gerald [VerfasserIn]
• Verfasst von: Hug, Friederike [VerfasserIn]
• Verfasst von: Prior, Birgit [VerfasserIn]
• Verfasst von: Obst, Ursula [VerfasserIn]
• Verfasst von: Hänsch, Gertrud Maria [VerfasserIn]
• Titel: Induction of neutrophil chemotaxis by the quorum-sensing molecule N-(3-oxododecanoyl)-L-homoserine lactone
• Verf.angabe: Sabine Zimmermann, Christof Wagner, Wencke Müller, Gerald Brenner-Weiss, Friederike Hug, Birgit Prior, Ursula Obst, and Gertrud Maria Hänsch
• Jahr: 2006
• Umfang: 6 S.
• Teil: volume:74
• Teil: year:2006
• Teil: number:10
• Teil: pages:5687-5692
• Teil: extent:6
• Fussnoten: Gesehen am 30.06.2021
• Titel Quelle: Enthalten in: Infection and immunity
• Ort Quelle: Washington, DC : Soc., 1970
• Jahr Quelle: 2006
• Band/Heft Quelle: 74(2006), 10, Seite 5687-5692
• ISSN Quelle: 1098-5522
• DOI: doi:10.1128/IAI.01940-05
• Datenträger: Online-Ressource
• Sprache: eng
• Sach-SW: 4-Butyrolactone
• Sach-SW: Biofilms
• Sach-SW: Chemotaxis, Leukocyte
• Sach-SW: Homoserine
• Sach-SW: Humans
• Sach-SW: Neutrophils
• Sach-SW: Pseudomonas aeruginosa
• Sach-SW: Signal Transduction
• K10plus-PPN: 176161584X

Abstract

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.