NDLI: Genetic Analysis of Fenhexamid-Resistant Field Isolates of the Phytopathogenic Fungus Botrytis cinerea ▿ †

Content Provider	PubMed Central
Author	Fillinger, Sabine Leroux, Pierre Auclair, Christiane Barreau, Christian Hajj, Charbel Al Debieu, Danièle
Abstract	The hydroxyanilide fenhexamid, one of the latest antibotrytis fungicides, active especially against leotiomycete plant-pathogenic fungi, inhibits 3-ketoreductase of the C-4-demethylation enzyme complex during ergosterol biosynthesis. We isolated Botrytis cinerea strains resistant to various levels of fenhexamid from French and German vineyards. The sequence of the gene encoding 3-ketoreductase, erg27, varied according to levels of resistance. Highly resistant isolates, termed HydR3+, all presented a modification of the phenylalanine at the C terminus of the putative transmembrane domain at position 412, either to serine (85% of the isolates), to isoleucine (11.5% of the isolates), or to valine (3.5% of the isolates). The introduction of the \documentclass[10pt]{article}\usepackage{amsmath}\usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy}\usepackage{mathrsfs}\usepackage{pmc}\usepackage[Euler]{upgreek}\pagestyle{empty}\oddsidemargin -1.0in\begin{document}\begin{equation}erg27^{HydR3^{+}}\end{equation}\end{document} allele into a fenhexamid-sensitive strain by means of a replicative plasmid conferred fenhexamid resistance on the resulting transformants, showing that the mutations at position 412 are responsible for fenhexamid resistance. Weakly to moderately resistant isolates, termed HydR3−, showed different point mutations between the strains in the sequenced regions of the erg27 gene, corresponding to amino acid changes between positions 195 and 400 of the protein. The \documentclass[10pt]{article}\usepackage{amsmath}\usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy}\usepackage{mathrsfs}\usepackage{pmc}\usepackage[Euler]{upgreek}\pagestyle{empty}\oddsidemargin -1.0in\begin{document}\begin{equation}erg27^{HydR3^{-}}\end{equation}\end{document} alleles on the replicative vector introduced into a sensitive strain did not confer resistance to fenhexamid. Genetic crosses between HydR3− and sensitive strains showed strict correlation between the sequenced mutation in the erg27 gene and the resistance phenotypes, suggesting that these mutations are linked to fenhexamid resistance. The HydR3 mutations possibly modify the affinity of the 3-ketoreductase enzyme for its specific inhibitor, fenhexamid.
Related Links	http://dx.doi.org/10.1128/aac.00615-08
Ending Page	3940
Page Count	8
Starting Page	3933
File Format	PDF
ISSN	00664804
e-ISSN	10986596
Journal	Antimicrobial Agents and Chemotherapy
Issue Number	11
Volume Number	52
Language	English
Publisher	American Society for Microbiology (ASM)
Publisher Date	2008-11-01
Access Restriction	Open
Rights Holder	American Society for Microbiology (ASM)
Subject Keyword	Pharmacology (medical) Pharmacology Infectious Diseases Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Infectious Diseases Pharmacology Pharmacology (medical)

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