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פותח על ידי קלירמאש פתרונות בע"מ -
Mechanisms of resistance to an azole fungicide in the grapevine powdery mildew fungus, Erysiphe necator
Year:
2015
Source of publication :
Phytopathology
Authors :
פרנקל, עומר
;
.
Volume :
105
Co-Authors:
Frenkel, O., School of Integrative Plant Science, Section of Plant Pathology and Plant-Microbe Biology, Cornell University, Ithaca, NY, United States, Department of Plant Pathology and Weed Research, Institute of Plant Protection, The Volcani Center, Bet Dagan, Israel
Cadle-Davidson, L., United States Department of Agriculture, Agricultural Research Service Grape Genetics Research Unit, Geneva, NY, United States
Wilcox, W.F., School of Integrative Plant Science, Section of Plant Pathology and Plant-Microbe Biology, Cornell University, Geneva, NY, United States
Milgroom, M.G., School of Integrative Plant Science, Section of Plant Pathology and Plant-Microbe Biology, Cornell University, Ithaca, NY, United States
Facilitators :
From page:
370
To page:
377
(
Total pages:
8
)
Abstract:
We studied the mechanisms of azole resistance in Erysiphe necator by quantifying the sensitivity to myclobutanil (EC50) in 65 isolates from the eastern United States and 12 from Chile. From each isolate, we sequenced the gene for sterol 14α-demethylase (CYP51), and measured the expression of CYP51 and homologs of four putative efflux transporter genes, which we identified in the E. necator transcriptome. Sequence variation in CYP51 was relatively low, with sequences of 40 U.S. isolates identical to the reference sequence. Nine U.S. isolates and five from Chile carried a previously identified A to T nucleotide substitution in position 495 (A495T), which results in an amino acid substitution in codon 136 (Y136F) and correlates with high levels of azole resistance. We also found a nucleotide substitution in position 1119 (A1119C) in 15 U.S. isolates, whose mean EC50 value was equivalent to that for the Y136F isolates. Isolates carrying mutation A1119C had significantly greater CYP51 expression, even though A1119C does not affect the CYP51 amino acid sequence. Regression analysis showed no significant effects of the expression of efflux transporter genes on EC50. Both the Y136F mutation in CYP51 and increased CYP51 expression appear responsible for azole resistance in eastern U.S. populations of E. necator.
Note:
Related Files :
fungi
gene expression
Genetics
metabolism
Microbiology
Vitis
עוד תגיות
תוכן קשור
More details
DOI :
10.1094/PHYTO-07-14-0202-R
Article number:
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
28778
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:41
You may also be interested in
Scientific Publication
Mechanisms of resistance to an azole fungicide in the grapevine powdery mildew fungus, Erysiphe necator
105
Frenkel, O., School of Integrative Plant Science, Section of Plant Pathology and Plant-Microbe Biology, Cornell University, Ithaca, NY, United States, Department of Plant Pathology and Weed Research, Institute of Plant Protection, The Volcani Center, Bet Dagan, Israel
Cadle-Davidson, L., United States Department of Agriculture, Agricultural Research Service Grape Genetics Research Unit, Geneva, NY, United States
Wilcox, W.F., School of Integrative Plant Science, Section of Plant Pathology and Plant-Microbe Biology, Cornell University, Geneva, NY, United States
Milgroom, M.G., School of Integrative Plant Science, Section of Plant Pathology and Plant-Microbe Biology, Cornell University, Ithaca, NY, United States
Mechanisms of resistance to an azole fungicide in the grapevine powdery mildew fungus, Erysiphe necator
We studied the mechanisms of azole resistance in Erysiphe necator by quantifying the sensitivity to myclobutanil (EC50) in 65 isolates from the eastern United States and 12 from Chile. From each isolate, we sequenced the gene for sterol 14α-demethylase (CYP51), and measured the expression of CYP51 and homologs of four putative efflux transporter genes, which we identified in the E. necator transcriptome. Sequence variation in CYP51 was relatively low, with sequences of 40 U.S. isolates identical to the reference sequence. Nine U.S. isolates and five from Chile carried a previously identified A to T nucleotide substitution in position 495 (A495T), which results in an amino acid substitution in codon 136 (Y136F) and correlates with high levels of azole resistance. We also found a nucleotide substitution in position 1119 (A1119C) in 15 U.S. isolates, whose mean EC50 value was equivalent to that for the Y136F isolates. Isolates carrying mutation A1119C had significantly greater CYP51 expression, even though A1119C does not affect the CYP51 amino acid sequence. Regression analysis showed no significant effects of the expression of efflux transporter genes on EC50. Both the Y136F mutation in CYP51 and increased CYP51 expression appear responsible for azole resistance in eastern U.S. populations of E. necator.
Scientific Publication
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