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  Algal oxylipins mediate the resistance of diatoms against algicidal bacteria

Meyer, N., Rettner, J., Werner, M., Werz, O., & Pohnert, G. (2018). Algal oxylipins mediate the resistance of diatoms against algicidal bacteria. Marine Drugs, 16(12): 486. doi:10.3390/md16120486.

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http://dx.doi.org/10.3390/md16120486 (Publisher version)
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Meyer, Nils, Author
Rettner, Johanna, Author
Werner, Markus, Author
Werz, Oliver, Author
Pohnert, Georg1, Author           
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1External Organizations, ou_persistent22              

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Free keywords: POLYUNSATURATED ALDEHYDES; MARINE; DEFENSE; PHYTOPLANKTON; METABOLITES; DIVERSITY; FAMILY; LIPIDS; ROLES; ACIDPharmacology & Pharmacy; HEPE hydroxylated eicosapentaenoic acid; HETE hydroxylated eicosatetraenoic acid; oxylipins; diatoms; plankton; algicidal bacteria; induced chemical defense; resolvins;
 Abstract: Algicidal bacteria can lyse microalgal blooms and trigger shifts within plankton communities. Resistant algal species can escape lysis, and have the opportunity to dominate the phytoplankton after a bacterial infection. Despite their important function in ecosystem regulation, little is known about mechanisms of resistance. Here, we show that the diatom Chaetoceros didymus releases eicosanoid oxylipins into the medium, and that the lytic algicidal bacterium, Kordia algicida, induces the production of several wound-activated oxylipins in this resistant diatom. Neither releases nor an induction occurs in the susceptible diatom Skeletonema costatum that is lysed by the bacterium within a few days. Among the upregulated oxylipins, hydroxylated eicosapentaenoic acids (HEPEs) dominate. However, also, resolvins, known lipid mediators in mammals, increase upon exposure of the algae to the algicidal bacteria. The prevailing hydroxylated fatty acid, 15-HEPE, significantly inhibits growth of K. algicida at a concentration of approximately 1 mu M. The oxylipin production may represent an independent line of defense of the resistant alga, acting in addition to the previously reported upregulation of proteases.

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Language(s): eng - English
 Dates: 2018
 Publication Status: Published online
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.3390/md16120486
Other: EXT641
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Title: Marine Drugs
Source Genre: Journal
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Publ. Info: Basel, Switzerland : MDPI AG
Pages: - Volume / Issue: 16 (12) Sequence Number: 486 Start / End Page: - Identifier: ISSN: 1660-3397
CoNE: https://pure.mpg.de/cone/journals/resource/1660-3397