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Rhodococcus erythropolis MTHt3 biotransforms ergopeptines to lysergic acid

BACKGROUND: 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. RESU...

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Autores principales: Thamhesl, Michaela, Apfelthaler, Elisabeth, Schwartz-Zimmermann, Heidi Elisabeth, Kunz-Vekiru, Elisavet, Krska, Rudolf, Kneifel, Wolfgang, Schatzmayr, Gerd, Moll, Wulf-Dieter
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2015
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Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4411749/
https://www.ncbi.nlm.nih.gov/pubmed/25887091
http://dx.doi.org/10.1186/s12866-015-0407-7
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author Thamhesl, Michaela
Apfelthaler, Elisabeth
Schwartz-Zimmermann, Heidi Elisabeth
Kunz-Vekiru, Elisavet
Krska, Rudolf
Kneifel, Wolfgang
Schatzmayr, Gerd
Moll, Wulf-Dieter
author_facet Thamhesl, Michaela
Apfelthaler, Elisabeth
Schwartz-Zimmermann, Heidi Elisabeth
Kunz-Vekiru, Elisavet
Krska, Rudolf
Kneifel, Wolfgang
Schatzmayr, Gerd
Moll, Wulf-Dieter
author_sort Thamhesl, Michaela
collection PubMed
description BACKGROUND: 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. RESULTS: 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. CONCLUSIONS: 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.
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spelling pubmed-44117492015-04-29 Rhodococcus erythropolis MTHt3 biotransforms ergopeptines to lysergic acid Thamhesl, Michaela Apfelthaler, Elisabeth Schwartz-Zimmermann, Heidi Elisabeth Kunz-Vekiru, Elisavet Krska, Rudolf Kneifel, Wolfgang Schatzmayr, Gerd Moll, Wulf-Dieter BMC Microbiol Research Article BACKGROUND: 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. RESULTS: 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. CONCLUSIONS: 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. BioMed Central 2015-03-28 /pmc/articles/PMC4411749/ /pubmed/25887091 http://dx.doi.org/10.1186/s12866-015-0407-7 Text en © Thamhesl et al.; licensee BioMed Central . 2015 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Research Article
Thamhesl, Michaela
Apfelthaler, Elisabeth
Schwartz-Zimmermann, Heidi Elisabeth
Kunz-Vekiru, Elisavet
Krska, Rudolf
Kneifel, Wolfgang
Schatzmayr, Gerd
Moll, Wulf-Dieter
Rhodococcus erythropolis MTHt3 biotransforms ergopeptines to lysergic acid
title Rhodococcus erythropolis MTHt3 biotransforms ergopeptines to lysergic acid
title_full Rhodococcus erythropolis MTHt3 biotransforms ergopeptines to lysergic acid
title_fullStr Rhodococcus erythropolis MTHt3 biotransforms ergopeptines to lysergic acid
title_full_unstemmed Rhodococcus erythropolis MTHt3 biotransforms ergopeptines to lysergic acid
title_short Rhodococcus erythropolis MTHt3 biotransforms ergopeptines to lysergic acid
title_sort rhodococcus erythropolis mtht3 biotransforms ergopeptines to lysergic acid
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4411749/
https://www.ncbi.nlm.nih.gov/pubmed/25887091
http://dx.doi.org/10.1186/s12866-015-0407-7
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