Co-Occurrence of Two Allelic Variants of CYP51 in Erysiphe necator and Their Correlation with Over-Expression for DMI Resistance

PLoS One. 2016 Feb 3;11(2):e0148025. doi: 10.1371/journal.pone.0148025. eCollection 2016.

Abstract

Demethylation inhibitors (DMIs) have been an important tool in the management of grapevine powdery mildew caused by Erysiphe necator. Long-term, intensive use of DMIs has resulted in reduced sensitivity in field populations. To further characterize DMI resistance and understand resistance mechanisms in this pathogen, we investigated the cyp51 sequence of 24 single-spored isolates from Virginia and surrounding states and analyzed gene expression in isolates representing a wide range of sensitivity. Two cyp51 alleles were found with respect to the 136th codon of the predicted EnCYP51 sequence: the wild-type (TAT) and the mutant (TTT), which results in the known Y136F amino acid change. Some isolates possessed both alleles, demonstrating gene duplication or increased gene copy number and possibly a requirement for at least one mutant copy of CYP51 for resistance. Cyp51 was over-expressed 1.4- to 19-fold in Y136F-mutant isolates. However, the Y136F mutation was absent in one isolate with moderate to high resistance factor. Two additional synonymous mutations were detected as well, one of which, A1119C was present only in isolates with high cyp51 expression. Overall, our results indicate that at least two mechanisms, cyp51 over-expression and the known target-site mutation in CYP51, contribute to resistance in E. necator, and may be working in conjunction with each other.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 14-alpha Demethylase Inhibitors / pharmacology*
  • Alleles*
  • Ascomycota / enzymology*
  • Ascomycota / genetics
  • Drug Resistance*
  • Fungal Proteins / biosynthesis*
  • Fungal Proteins / genetics
  • Gene Expression Regulation, Enzymologic / drug effects*
  • Gene Expression Regulation, Fungal / drug effects*
  • Mutation
  • Sterol 14-Demethylase / biosynthesis*
  • Sterol 14-Demethylase / genetics

Substances

  • 14-alpha Demethylase Inhibitors
  • Fungal Proteins
  • Sterol 14-Demethylase

Grants and funding

This work was supported by Virginia Wine Board (http://www.virginiawine.org/industry/wine-board), Viticulture Consortium-East (http://portal.nifa.usda.gov/web/crisprojectpages/0218903-viticulture-consortium--east.html), and North Carolina Wine & Grape Council (no current website, referenced at http://www.ncagr.gov/markets/ncwine/about-us/nc-wine-history.html). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.