ArticleJournal of agricultural and food chemistry2017
Ergot Alkaloid Biosynthesis in the Maize (Zea mays) Ergot Fungus Claviceps gigantea.
Article in Journal of agricultural and food chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Two Satellite Gene Clusters Enhance Ergot Alkaloid Biosynthesis Capacity of AspergillusApplied and environmental microbiology · 2023Article
- Ergot Alkaloids Contribute to the Pathogenic Potential of the FungusApplied and environmental microbiology · 2023Article
- Derivation of the multiply-branched ergot alkaloid pathway of fungi.Microbial biotechnology · 2023Review
- A Baeyer-Villiger Monooxygenase Gene Involved in the Synthesis of Lysergic Acid Amides Affects the Interaction of the Fungus Metarhizium brunneum with Insects.Applied and environmental microbiology · 2021Article
- Co-Occurrence of 35 Mycotoxins: A Seven-Year Survey of Corn Grain and Corn Silage in the United States.Toxins · 2021Article
- Genetic Reprogramming of the Ergot Alkaloid Pathway of Metarhizium brunneum.Applied and environmental microbiology · 2020Article
- Molecular mechanisms in grass-Epichloë interactions: towards endophyte driven farming to improve plant fitness and immunity.World journal of microbiology & biotechnology · 2020Review
- Biological activity of Claviceps gigantea in juvenile New Zealand rabbits.Mycotoxin research · 2018Article
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Authors and funding
3 authors.
Funding
Abstract
Biosynthesis of the dihydrogenated forms of ergot alkaloids is of interest because many of the ergot alkaloids used as pharmaceuticals may be derived from dihydrolysergic acid (DHLA) or its precursor dihydrolysergol. The maize (Zea mays) ergot pathogen Claviceps gigantea has been reported to produce dihydrolysergol, a hydroxylated derivative of the common ergot alkaloid festuclavine. We hypothesized expression of C. gigantea cloA in a festuclavine-accumulating mutant of the fungus Neosartorya fumigata would yield dihydrolysergol because the P450 monooxygenase CloA from other fungi performs similar oxidation reactions. We engineered such a strain, and high performance liquid chromatography and liquid chromatography-mass spectrometry analyses demonstrated the modified strain produced DHLA, the fully oxidized product of dihydrolysergol. Accumulation of high concentrations of DHLA in field-collected C. gigantea sclerotia and discovery of a mutation in the gene lpsA, downstream from DHLA formation, supported our finding that DHLA rather than dihydrolysergol is the end product of the C. gigantea pathway.
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