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Haloperoxidase mediated quorum quenching by Nitzschia cf pellucida: study of the metabolization of N-acyl homoserine lactones by a benthic diatom

Michail Syrpas (UGent) , Ewout Ruysbergh (UGent) , Lander Blommaert (UGent) , Bart Vanelslander (UGent) , Koen Sabbe (UGent) , Wim Vyverman (UGent) , Norbert De Kimpe (UGent) and Sven Mangelinckx (UGent)
(2014) MARINE DRUGS. 12(1). p.352-367
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Abstract
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-beta-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 beta-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.
Keywords
haloperoxidase, quorum sensing, degradation pathway, AHL, reference compounds, diatom-bacteria interactions, SPONGE LUFFARIELLA-VARIABILIS, MARINE NATURAL-PRODUCTS, ACYLHOMOSERINE LACTONES, BACTERIAL COMMUNICATION, PSEUDOMONAS-AERUGINOSA, HALOGENATED FURANONES, SENSING INHIBITORS, SIGNAL MOLECULES, BROMOPEROXIDASE, METABOLITES

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MLA
Syrpas, Michail, Ewout Ruysbergh, Lander Blommaert, et al. “Haloperoxidase Mediated Quorum Quenching by Nitzschia Cf Pellucida: Study of the Metabolization of N-acyl Homoserine Lactones by a Benthic Diatom.” Ed. Véronique Martin-Jézéquel. MARINE DRUGS 12.1 (2014): 352–367. Print.
APA
Syrpas, M., Ruysbergh, E., Blommaert, L., Vanelslander, B., Sabbe, K., Vyverman, W., De Kimpe, N., et al. (2014). Haloperoxidase mediated quorum quenching by Nitzschia cf pellucida: study of the metabolization of N-acyl homoserine lactones by a benthic diatom. (V. Martin-Jézéquel, Ed.)MARINE DRUGS, 12(1), 352–367.
Chicago author-date
Syrpas, Michail, Ewout Ruysbergh, Lander Blommaert, Bart Vanelslander, Koen Sabbe, Wim Vyverman, Norbert De Kimpe, and Sven Mangelinckx. 2014. “Haloperoxidase Mediated Quorum Quenching by Nitzschia Cf Pellucida: Study of the Metabolization of N-acyl Homoserine Lactones by a Benthic Diatom.” Ed. Véronique Martin-Jézéquel. Marine Drugs 12 (1): 352–367.
Chicago author-date (all authors)
Syrpas, Michail, Ewout Ruysbergh, Lander Blommaert, Bart Vanelslander, Koen Sabbe, Wim Vyverman, Norbert De Kimpe, and Sven Mangelinckx. 2014. “Haloperoxidase Mediated Quorum Quenching by Nitzschia Cf Pellucida: Study of the Metabolization of N-acyl Homoserine Lactones by a Benthic Diatom.” Ed. Véronique Martin-Jézéquel. Marine Drugs 12 (1): 352–367.
Vancouver
1.
Syrpas M, Ruysbergh E, Blommaert L, Vanelslander B, Sabbe K, Vyverman W, et al. Haloperoxidase mediated quorum quenching by Nitzschia cf pellucida: study of the metabolization of N-acyl homoserine lactones by a benthic diatom. Martin-Jézéquel V, editor. MARINE DRUGS. 2014;12(1):352–67.
IEEE
[1]
M. Syrpas et al., “Haloperoxidase mediated quorum quenching by Nitzschia cf pellucida: study of the metabolization of N-acyl homoserine lactones by a benthic diatom,” MARINE DRUGS, vol. 12, no. 1, pp. 352–367, 2014.
@article{4426928,
  abstract     = {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-beta-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 beta-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.},
  author       = {Syrpas, Michail and Ruysbergh, Ewout and Blommaert, Lander and Vanelslander, Bart and Sabbe, Koen and Vyverman, Wim and De Kimpe, Norbert and Mangelinckx, Sven},
  editor       = {Martin-Jézéquel, Véronique},
  issn         = {1660-3397},
  journal      = {MARINE DRUGS},
  keywords     = {haloperoxidase,quorum sensing,degradation pathway,AHL,reference compounds,diatom-bacteria interactions,SPONGE LUFFARIELLA-VARIABILIS,MARINE NATURAL-PRODUCTS,ACYLHOMOSERINE LACTONES,BACTERIAL COMMUNICATION,PSEUDOMONAS-AERUGINOSA,HALOGENATED FURANONES,SENSING INHIBITORS,SIGNAL MOLECULES,BROMOPEROXIDASE,METABOLITES},
  language     = {eng},
  number       = {1},
  pages        = {352--367},
  title        = {Haloperoxidase mediated quorum quenching by Nitzschia cf pellucida: study of the metabolization of N-acyl homoserine lactones by a benthic diatom},
  url          = {http://dx.doi.org/10.3390/md12010352},
  volume       = {12},
  year         = {2014},
}

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