Author/Authors :
-، - نويسنده Department of Biochemical Engineering, Faculty of Science and Technology, University of Debrecen, Egyetem tér 1., 4032 Debrecen, Hungary. Asadollahi, M. , -، - نويسنده Department of Biochemical Engineering, Faculty of Science and Technology, University of Debrecen, Egyetem tér 1., 4032 Debrecen, Hungary. Szojka, A. , -، - نويسنده Department of Biochemical Engineering, Faculty of Science and Technology, University of Debrecen, Egyetem tér 1., 4032 Debrecen, Hungary. Fekete, E. , -، - نويسنده Department of Biochemical Engineering, Faculty of Science and Technology, University of Debrecen, Egyetem tér 1., 4032 Debrecen, Hungary. Karaffa, L. , -، - نويسنده Research and Extension Centre for Fruit Growing, Vadastag 2, H-4244 ?jfehért?, Hungary. Tak?cs, F. , -، - نويسنده Department of Biochemical Engineering, Faculty of Science and Technology, University of Debrecen, Egyetem tér 1., 4032 Debrecen, Hungary. Flipphi, M. , -، - نويسنده Institute of Food Processing, Quality Assurance and Microbiology, Faculty of Agricultural and Food Sciences and Environmental Management, University of Debrecen, B?sz?rményi ?t 138., 4032 Debrecen, Hungary. S?ndor, E.
Abstract :
Quinol oxidation inhibitors (QoIs) are one of the most important classes of fungicides used in agriculture. They block electron transfer between cytochrome b and cytochrome c1, thereby impeding the production of ATP via oxidative phosphorylation. QoI fungicides are generally at high risk of provoking resistance in fungal phytopathogens. Resistance has been reported in more than thirty species, amongst others, in Botrytis cinerea. In various QoI-resistant monosporic B. cinerea isolates from Hungary, a G-to-C point mutation was identified in the mitochondrial gene that encodes the QoI target, cytochrome b, resulting in a glycine to alanine substitution at position 143 (G143A). Analysis of Hungarian group I and group II strains further indicated the frequent occurrence of an additional group I-type intron in the cytb gene directly downstream of the glycine-143 codon. Mutual presence of distinct mitochondrial DNAs specifying different cytb alleles (heteroplasmy) has also been detected in monosporic strains. Remarkably, a number of group II field isolates were found to be highly resistant to azoxystrobin although they did not appear to carry the G-to-C mutation (G143A) generally associated with fungal QoI-resistance.
