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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
Syrpas, M.; Ruysbergh, E.; Blommaert, L.; Vanelslander, B.; Sabbe, K.; Vyverman, W.; De Kimpe, N.; Mangelinckx, S. (2014). Haloperoxidase mediated quorum quenching by Nitzschia cf pellucida: study of the metabolization of N-Acyl Homoserine Lactones by a benthic diatom. Mar. Drugs 12(1): 352-367. dx.doi.org/10.3390/md12010352
In: Marine Drugs. Molecular Diversity Preservation International (MDPI): Basel. ISSN 1660-3397; e-ISSN 1660-3397, meer
Peer reviewed article  

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Trefwoorden
    Nitzschia pellucida Grunow, 1880 [WoRMS]
    Marien
Author keywords
    quorum sensing; haloperoxidase; degradation pathway; AHL; referencecompounds; diatom-bacteria interactions

Auteurs  Top 
  • Syrpas, M., meer
  • Ruysbergh, E., meer
  • Blommaert, L., meer
  • Vanelslander, B., meer

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-ß-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 ß-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.

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