Haloperoxidase mediated quorum quenching by Nitzschia cf pellucida: study of the metabolization of N-acyl homoserine lactones by a benthic diatom.
Diatoms are known to produce a variety of halogenated compounds, which were recently shown to have a role in allelopathic interactions between competing species. The production of these compounds is linked to haloperoxidase activity. This research, has shown that this system may also be involved in diatom-bacteria interactions via the H2O2 dependent inactivation of a type of quorum sensing (QS) molecule, i.e., N-β-ketoacylated homoserine lactones (AHLs), by a natural haloperoxidase system from the benthic diatom Nitzschia cf pellucida. The AHL degradation pathway towards corresponding halogenated derivatives was elucidated via HPLC-MS analysis and the synthesis of a broad series of novel halogenated AHL analogues as reference compounds. Furthermore, their biological activity as quorum sensing modulators was directly compared and evaluated against a series of naturally occurring β-keto-AHLs. It has been demonstrated that the loss of the QS activity results from the final cleavage of the halogenated N-acyl chain of the signal molecules.
Department of Sustainable Organic Chemistry and Technology, Faculty of Bioscience Engineering, Ghent University, Coupure Links 653, Ghent B-9000, Belgium. Michail.Syrpas@UGent.be.
Michail
M
Syrpas
Department of Sustainable Organic Chemistry and Technology, Faculty of Bioscience Engineering, Ghent University, Coupure Links 653, Ghent B-9000, Belgium. Ewout.Ruysbergh@UGent.be.
Ewout
E
Ruysbergh
Department of Sustainable Organic Chemistry and Technology, Faculty of Bioscience Engineering, Ghent University, Coupure Links 653, Ghent B-9000, Belgium. Lander.Blommaert@UGent.be.
Lander
L
Blommaert
Department of Sustainable Organic Chemistry and Technology, Faculty of Bioscience Engineering, Ghent University, Coupure Links 653, Ghent B-9000, Belgium. Bart.Vanelslander@gmail.com.
Bart
B
Vanelslander
Department of Sustainable Organic Chemistry and Technology, Faculty of Bioscience Engineering, Ghent University, Coupure Links 653, Ghent B-9000, Belgium. Koen.Sabbe@UGent.be.
Koen
K
Sabbe
Department of Sustainable Organic Chemistry and Technology, Faculty of Bioscience Engineering, Ghent University, Coupure Links 653, Ghent B-9000, Belgium. Wim.Vyverman@UGent.be.
Wim
W
Vyverman
Department of Sustainable Organic Chemistry and Technology, Faculty of Bioscience Engineering, Ghent University, Coupure Links 653, Ghent B-9000, Belgium. Norbert.DeKimpe@UGent.be.
Norbert
N
De Kimpe
Department of Sustainable Organic Chemistry and Technology, Faculty of Bioscience Engineering, Ghent University, Coupure Links 653, Ghent B-9000, Belgium. Sven.Mangelinckx@UGent.be.
Sven
S
Mangelinckx
D001681:Biological Assay; D002374:Catalase / Q000737:chemistry; D002851:Chromatography, High Pressure Liquid; D002861:Chromobacterium / Q000187:drug effects; D017377:Diatoms / Q000737:chemistry* / Q000378:metabolism*; D004926:Escherichia coli / Q000187:drug effects / Q000378:metabolism; D049452:Green Fluorescent Proteins; D006714:Homoserine / Q000378:metabolism*; D007783:Lactones / Q000138:chemical synthesis / Q000378:metabolism*; D059625:Liquid-Liquid Extraction; D013058:Mass Spectrometry; D010544:Peroxidases / Q000737:chemistry*; D010637:Phenolsulfonphthalein; D053038:Quorum Sensing / Q000187:drug effects*
D007783:Lactones; D049452:Green Fluorescent Proteins; D006714:Homoserine; D010544:Peroxidases; D002374:Catalase; D010637:Phenolsulfonphthalein