Induction of neutrophil chemotaxis by the quorum-sensing molecule N-3-oxododecanyol homoserine lactone (3OC12-HSL)

  • chair: Zimmermann, S. / Wagner, C. / Müller, W. / Brenner-Weiß, G. / Hug, F. / Prior, B. / Obst, U. / Hänsch, G. M. (2006)

  • place:

    Inf. Immun. 74 (2006), 5687-5692
  • Date: 2006

  • Zimmermann, S. / Wagner, C. / Müller, W. / Brenner-Weiß, G. / Hug, F. / Prior, B. / Obst, U. / Hänsch, G. M. (2006): „Induction of neutrophil chemotaxis by the quorum-sensing molecule N-3-oxododecanyol homoserine lactone (3OC12-HSL)“. In: Inf. Immun. 74 (2006), 5687-5692

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.

 

 

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