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  Unexpected bacterial origin of the antibiotic icosalide: Two-tailed depsipeptide assembly in multifarious Burkholderia symbionts

Dose, B., Niehs, S. P., Scherlach, K., Flórez, L. V., Kaltenpoth, M., & Hertweck, C. (2018). Unexpected bacterial origin of the antibiotic icosalide: Two-tailed depsipeptide assembly in multifarious Burkholderia symbionts. ACS Chemical Biology, 13(9), 2414-2420. doi:10.1021/acschembio.8b00600.

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 Urheber:
Dose, Benjamin, Autor
Niehs, Sarah P., Autor
Scherlach, Kirstin, Autor
Flórez, Laura V.1, Autor           
Kaltenpoth, Martin1, Autor           
Hertweck, Christian, Autor
Affiliations:
1External Organizations, ou_persistent22              

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Schlagwörter: FUNGUS RHIZOPUS-MICROSPORUS; GENE-CLUSTER; DEFENSIVE MUTUALISM; BIOSYNTHESIS; DIVERSITY; IDENTIFICATION; ENDOSYMBIONTS; LIPOPEPTIDES; PSEUDOMONAS; ENDOPHYTESBiochemistry & Molecular Biology;
 Zusammenfassung: Icosalide is an unusual two-tailed lipocyclopeptide antibiotic that was originally isolated from a fungal culture. Yet, its biosynthesis and ecological function have remained enigmatic. By genome mining and metabolic profiling of a bacterial endosymbiont (Burkholderia gladioli) of the pest beetle Lagria villosa, we unveiled a bacterial origin of icosalide. Functional analysis of the biosynthetic gene locus revealed an unprecedented nonribosomal peptide synthetase (NRPS) that incorporates two beta-hydroxy acids by means of two starter condensation domains in different modules. This unusual assembly line, which may inspire new synthetic biology approaches, is widespread among many symbiotic Burkholderia species from diverse habitats. Biological assays showed that icosalide is active against entomopathogenic bacteria, thus adding to the chemical armory protecting beetle offspring. By creating a null mutant, we found that icosalide is a swarming inhibitor, which may play a role in symbiotic interactions and bears the potential for therapeutic applications.

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Sprache(n): eng - English
 Datum: 2018
 Publikationsstatus: Erschienen
 Seiten: 7
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Identifikatoren: DOI: 10.1021/acschembio.8b00600
Anderer: KAL100
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Titel: ACS Chemical Biology
  Kurztitel : ACS Chem. Biol.
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Washington, D.C. : American Chemical Society
Seiten: - Band / Heft: 13 (9) Artikelnummer: - Start- / Endseite: 2414 - 2420 Identifikator: ISSN: 1554-8929
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000035040