Detection of Zymoseptoria tritici SDHI-insensitive field isolates carrying the SdhC-H152R and SdhD-R47W substitutions

BACKGROUND Succinate dehydrogenase inhibitor (SDHI) fungicides are important in the management of Zymoseptoria tritici in wheat. New active ingredients from this group of fungicides have been introduced recently and are widely used. Because the fungicides act at a single enzyme site, resistance deve...

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Bibliographic Details
Published in:Pest management science 2016-12, Vol.72 (12), p.2203-2207
Main Authors: Dooley, Hilda, Shaw, Michael W, Mehenni-Ciz, Jeanne, Spink, John, Kildea, Steven
Format: Article
Language:English
Subjects:
amino acid mutation
Amino Acid Substitution
Ascomycota - drug effects
Ascomycota - genetics
Ascomycota - isolation & purification
Drug Resistance, Fungal - genetics
Enzyme Inhibitors - pharmacology
fungicide resistance
Fungicides, Industrial - pharmacology
Ireland
Mutation
Mycosphaerella graminicola
Pesticides
Plant Diseases - microbiology
Pyrazoles - pharmacology
septoria tritici blotch
Succinate Dehydrogenase - antagonists & inhibitors
Succinate Dehydrogenase - genetics
succinate dehydrogenase inhibitor
Thiophenes - pharmacology
Triticum - microbiology
Triticum aestivum
Wheat
Zymoseptoria tritici
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Summary:BACKGROUND Succinate dehydrogenase inhibitor (SDHI) fungicides are important in the management of Zymoseptoria tritici in wheat. New active ingredients from this group of fungicides have been introduced recently and are widely used. Because the fungicides act at a single enzyme site, resistance development in Z. tritici is classified as medium‐to‐high risk. RESULTS Isolates from Irish experimental plots in 2015 were tested against the SDHI penthiopyrad during routine monitoring. The median of the population was approximately 2 times less sensitive than the median of the baseline population. Two of the 93 isolates were much less sensitive to penthiopyrad than the least sensitive of the baseline isolates. These isolates were also insensitive to most commercially available SDHIs. Analysis of the succinate dehydrogenase coding genes confirmed the presence of the substitutions SdhC‐H152R and SdhD‐R47W in the very insensitive isolates. CONCLUSION This is the first report showing that the SdhC‐H152R mutation detected in laboratory mutagenesis studies also exists in the field. The function and relevance of this mutation, combined with SdhD‐R47W, still needs to be determined. © 2016 Society of Chemical Industry
ISSN:1526-498X
1526-4998
DOI:10.1002/ps.4269