Occurrence of Different Resistance Mechanisms to Acetolactate Synthase Inhibitors in European Sorghum halepense

Four Hungarian and two Italian Sorghum halepense populations harvested in maize fields were investigated to elucidate the levels and mechanisms underlying acetolactate synthase (ALS) inhibitors resistance. The two Italian populations were highly cross-resistant to all ALS inhibitors tested, and the...

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Bibliographic Details
Published in:Journal of agricultural and food chemistry 2017-08, Vol.65 (34), p.7320-7327
Main Authors: Panozzo, Silvia, Milani, Andrea, Scarabel, Laura, Balogh, Ákos, Dancza, Istvan, Sattin, Maurizio
Format: Article
Language:English
Subjects:
Acetolactate Synthase - antagonists & inhibitors
Acetolactate Synthase - genetics
Acetolactate Synthase - metabolism
Europe
Herbicide Resistance
Herbicides - pharmacology
Plant Proteins - antagonists & inhibitors
Plant Proteins - genetics
Plant Proteins - metabolism
Sorghum - drug effects
Sorghum - enzymology
Sorghum - genetics
Zea mays - growth & development
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Summary:Four Hungarian and two Italian Sorghum halepense populations harvested in maize fields were investigated to elucidate the levels and mechanisms underlying acetolactate synthase (ALS) inhibitors resistance. The two Italian populations were highly cross-resistant to all ALS inhibitors tested, and the variant ALS allele Leu574 was identified in most of the plants; no differences were observed when the plants were treated with herbicide plus malathion. This suggests that the main resistance mechanism is target-site mediated. The Hungarian populations proved to be controlled by imazamox, while they were resistant to sulfonylureas and bispyribac-Na. All Hungarian populations, but not all plants of population 12–49H, presented the variant allele Glu376. This is the first documented occurrence of the Asp-376-Glu substitution in S. halepense. ALS enzyme bioassay and treatment with malathion confirmed that at least in plants of two populations the resistance is very likely due to both target-site and enhanced metabolism of P450 enzymes.
ISSN:0021-8561
1520-5118
DOI:10.1021/acs.jafc.7b01243