Role of sterol 3-ketoreductase sensitivity in susceptibility to the fungicide fenhexamid in Botrytis cinerea and other phytopathogenic fungi
Autor: | Pierre Leroux, Danièle Debieu, Emeline Montesinos, Sabine Fillinger, Jocelyne Bach |
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Rok vydání: | 2012 |
Předmět: |
0106 biological sciences
chemistry.chemical_classification 0303 health sciences biology General Medicine biology.organism_classification 01 natural sciences Phenotype Sterol Amino acid Fungicide 03 medical and health sciences Transmembrane domain Biochemistry chemistry Insect Science Agronomy and Crop Science Gene 030304 developmental biology 010606 plant biology & botany Botrytis cinerea Demethylation |
Zdroj: | Pest Management Science. 69:642-651 |
ISSN: | 1526-498X |
DOI: | 10.1002/ps.3418 |
Popis: | BACKGROUND:Thenarrow-spectrumfungicidefenhexamidwasintroducedintoFrenchvineyardsin2000tocontrolgreymould caused by a complex of two cryptic species: Botrytis cinerea, the predominant species sensitive to fenhexamid, and Botrytis pseudocinerea, naturally resistant. Fenhexamid was suggested to inhibit the 3-ketoreductase involved at C-4 demethylation steps during ergosterol biosynthesis, as revealed by its effects on the B. cinerea sterol profile. Resistance monitoring studies have hitherto identified two B. cinerea fenhexamid-resistant phenotypes, both resulting from mutations in the erg27 gene encoding 3-ketoreductase. RESULTS: The role of 3-ketoreductase sensitivity in fungal susceptibility to fenhexamid was investigated by studying sterol profilesandmicrosomal3-ketoreductaseinvariousfungalstrains.FenhexamiddoesinhibitB.cinerea3-ketoreductaseactivity. Erg27 mutations causing amino acid substitutions in or near the transmembrane domain strongly decrease the affinity of fenhexamid for 3-ketoreductase. Fenhexamid has very low affinities for 3-ketoreductase in inherently resistant species, whether closely related to B.cinerea, like B.pseudocinerea, or more distantly related, like Nectriahaematococca. CONCLUSION: erg27 mutation and erg27 polymorphism may therefore contribute to the unfavourable binding of fenhexamid toitstarget,3-ketoreductase,explainingtheacquisitionoffenhexamidresistanceinB.cinereaandthenarrowspectrumofthis fungicide. c � 2012 Society of Chemical Industry Supporting information may be found in the online version of this article. |
Databáze: | OpenAIRE |
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