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Rhodococcus erythropolis MTHt3 biotransforms ergopeptines to lysergic acid
VerfasserThamhesl, Michaela ; Apfelthaler, Elisabeth ; Schwartz-Zimmermann, Heidi Elisabeth ; Kunz-Vekiru, Elisavet ; Krska, Rudolf ; Kneifel, Wolfgang ; Schatzmayr, Gerd ; Moll, Wulf-Dieter
Erschienen in
BMC Microbiology, 2015, Jg. 15, 73 S.
ErschienenBioMed Central (BMC), 2015
DokumenttypAufsatz in einer Zeitschrift
URNurn:nbn:at:at-ubbw:3-1179 Persistent Identifier (URN)
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Rhodococcus erythropolis MTHt3 biotransforms ergopeptines to lysergic acid [1.1 mb]
Zusammenfassung (Englisch)


Ergopeptines are a predominant class of ergot alkaloids produced by tall fescue grass endophyte Neotyphodium coenophialum or cereal pathogen Claviceps purpurea. The vasoconstrictive activity of ergopeptines makes them toxic for mammals, and they can be a problem in animal husbandry.


We isolated an ergopeptine degrading bacterial strain, MTHt3, and classified it, based on its 16S rDNA sequence, as a strain of Rhodococcus erythropolis (Nocardiaceae, Actinobacteria). For strain isolation, mixed microbial cultures were obtained from artificially ergot alkaloid-enriched soil, and provided with the ergopeptine ergotamine in mineral medium for enrichment. Individual colonies derived from such mixed cultures were screened for ergotamine degradation by high performance liquid chromatography and fluorescence detection. R. erythropolis MTHt3 converted ergotamine to ergine (lysergic acid amide) and further to lysergic acid, which accumulated as an end product. No other tested R. erythropolis strain degraded ergotamine. R. erythropolis MTHt3 degraded all ergopeptines found in an ergot extract, namely ergotamine, ergovaline, ergocristine, ergocryptine, ergocornine, and ergosine, but the simpler lysergic acid derivatives agroclavine, chanoclavine, and ergometrine were not degraded. Temperature and pH dependence of ergotamine and ergine bioconversion activity was different for the two reactions.


Degradation of ergopeptines to ergine is a previously unknown microbial reaction. The reaction end product, lysergic acid, has no or much lower vasoconstrictive activity than ergopeptines. If the genes encoding enzymes for ergopeptine catabolism can be cloned and expressed in recombinant hosts, application of ergopeptine and ergine degrading enzymes for reduction of toxicity of ergot alkaloid-contaminated animal feed may be feasible.