Physiological and biochemical characteristics of laboratory induced mutants of Botrytis cinerea with resistance to fluazinam

Pestic Biochem Physiol. 2015 Jan:117:19-23. doi: 10.1016/j.pestbp.2014.10.003. Epub 2014 Oct 16.

Abstract

Botrytis cinerea is a necrotrophic and filamentous fungus with a high risk of developing resistance to fungicides. The pyridinamine fungicide fluazinam has been reported to have excellent activity against B. cinerea and better effect on controlling gray mold. In this study, the physiological and biochemical characteristics of laboratory-induced mutants of B. cinerea with resistance to fluazinam has been investigated. Compared to the wild-type strains, the fluazinam-resistant mutants had a significant decrease in respiratory rate, glycerol, oxalate, and ATP contents, and an increase in ATPase activity and sensitivity to osmotic pressure, but did not differ in cell membrane permeability. Sequencing indicated that two parental strains and four resistant mutants were identical in the nucleotide sequence of F-ATPase gene. These results will enrich our understanding of the resistance mechanism of B. cinerea to fluazinam.

Keywords: Botrytis cinerea; Characteristics; Fluazinam; Resistance.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / genetics
  • Adenosine Triphosphate / metabolism
  • Aminopyridines*
  • Base Sequence
  • Botrytis* / genetics
  • Botrytis* / metabolism
  • Cell Membrane Permeability
  • DNA, Fungal / genetics
  • Drug Resistance, Fungal* / genetics
  • Drug Resistance, Fungal* / physiology
  • Fungal Proteins / genetics
  • Fungicides, Industrial*
  • Glucose / pharmacology
  • Glycerol / metabolism
  • Mutation
  • Oxalic Acid / metabolism
  • Sequence Analysis, DNA

Substances

  • Aminopyridines
  • DNA, Fungal
  • Fungal Proteins
  • Fungicides, Industrial
  • fluazinam
  • Adenosine Triphosphate
  • Oxalic Acid
  • Adenosine Triphosphatases
  • Glucose
  • Glycerol