Binding of the respiratory chain inhibitor ametoctradin to the mitochondrial<i>bc</i><sub>1</sub>complex

Fehr, Marcus; Wolf, Antje; Stammler, G.

doi:10.1002/ps.4031

Cited by 34 publications

(41 citation statements)

References 46 publications

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“…These two populations were excluded from the subsequent analyses of AOX‐related resistance because a target site resistance to amisulbrom could not be completely ruled out. All the other resistant to amisulbrom populations were sensitive in the presence of SHAM, which showed that the resistance mechanism involved AOX‐related resistance, presumably AOX overexpression . The percentage of populations displaying the AOX‐related resistance mechanism varied from year to year, ranging from 4% in 2012 to 54% in 2017.…”

Section: Resultsmentioning

confidence: 91%

“…In P. viticola , the role of AOX overexpression in resistance to QoIs has been established. A fitness study performed in vitro without selection pressure and with a combination of sporangia with and without AOX overexpression showed a strong reduction in AOX expression in sporangia after several multiplication cycles . The competitiveness of sporangia with AOX overexpression but without selection pressure seems to be weaker.…”

Section: Discussionmentioning

confidence: 99%

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Investigation of the sensitivity of Plasmopara viticola to amisulbrom and ametoctradin in French vineyards using bioassays and molecular tools

Fontaine

Remuson

Caddoux

et al. 2019

Pest Management Science

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BACKGROUND: Complex III inhibitors are key compounds in the control of Plasmopara viticola. They are prone to the development of resistance, as demonstrated by the emergence of resistance to quinone-outside inhibitors. By using a combination of bioassays and molecular methods, we monitored sensitivity to amisulbrom and ametoctradin in P. viticola populations in French vineyards from 2012 to 2017. RESULTS:We found that the alternative oxidase (AOX)-related resistance mechanism was common in French P. viticola populations. Target-site resistance to ametoctradin was first detected in 2015 and is likely caused by a single point mutation in the cytochrome b gene, leading to the S34L substitution. The role of this substitution in resistance to ametoctradin was corroborated by another study using an experimental model. A molecular biology method has been developed to detect the mutant allele. To date, the frequency of this mutation is low in French P. viticola populations and it is often co-detected with the wild-type allele. CONCLUSION: Populations of P. viticola displaying evidence of AOX-related resistance were detected for every surveyed year, and their occurrence in French vineyards seems to be increasing over time. This resistance mechanism is currently threatening the efficacy of complex III inhibitors in the field. The low frequency of the S34L allele conferring resistance to ametoctradin, and the instability of resistant phenotypes in some populations, suggest that a fitness cost may be associated with the mutation.

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Section: Resultsmentioning

confidence: 91%

Section: Discussionmentioning

confidence: 99%

Investigation of the sensitivity of Plasmopara viticola to amisulbrom and ametoctradin in French vineyards using bioassays and molecular tools

Fontaine

Remuson

Caddoux

et al. 2019

Pest Management Science

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“…QoI fungicides interact with one of these sites in such a way that a single mutation (Gly143Ala) causes resistance, whereas the recently introduced fungicide Ametoctradin (QoSI; FRAC code 45) binds to the second site, and does not show cross resistance with QoIs (Fehr et al 2015). Currently Ametoctradin is only registered for use against oomycete pathogens, but there seems no reason why this important target site could not be exploited to widen the disease control spectrum.…”

Section: Finding New Modes Of Actionmentioning

confidence: 99%

Fungicide resistance: facing the challenge - a review

Hollomon¹

2015

Plant Prot. Sci.

134

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Hollomon D.W. (2015): Fungicide resistance: facing the challenge. Plant Protect. Sci., Fungicide resistance continues to generate disease control problems in many crops. Experience amassed over the past fifty years has emphasised the importance of diversity in modes of action in anti-resistance strategies. Because of losses, not only from resistance, but increasingly from environmental and health concerns, the number of modes of action has become dangerously small. This paper considers three challenges facing crop protection in the search for durable disease control systems. Greater understanding of the biochemistry surrounding fungal development and pathogenicity provides opportunities for the discovery and development of novel modes of action, and some recent advances in this area are discussed. To ensure sufficient resources available to take a novel discovery forward to a commercial product, a second challenge facing manufacturers involves early assessment of resistance risk. A third challenge facing researchers, manufacturers and growers requires translation of resistance risk into effective and durable disease control strategies in actual crops. At the core of this challenge is using resistance risk evidence obtained in laboratory and glasshouse studies using individual isolates of target pathogens, to evaluate the fitness cost of resistance in pathogen populations in field crops. Increasingly, management of resistance is seen as the integration of fungicides with non-chemical disease control methods. But success of any Integrated Disease Management (IDM) strategy ultimately depends on the ability of growers to maintain production and profitability.

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“…The cytochrome bc 1 complex (respiratory complex III, Cyt bc 1 , EC: http://1.10.2.2) of eukaryotic mitochondrial and prokaryotic energy‐transducing membranes is a proven target for antimicrobial agents of medical and agricultural interest [1–7]. This enzyme, which is widespread in nature, functions as a protonmotive ubiquinol:cytochrome c oxidoreductase, conserving and converting the Gibbs energy obtained from the exergonic oxidation of ubiquinol by cytochrome c into a transmembrane proton gradient which may be harnessed for other endergonic processes, typically ATP synthesis by an F o F 1 ATP synthase [8,9].…”

Section: Introduction and General Enzymatic Mechanism Of The Cytochromentioning

confidence: 99%

The cytochrome bc₁ complex as an antipathogenic target

2020

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The cytochrome bc1 complex is a key component of the mitochondrial respiratory chains of many eukaryotic microorganisms that are pathogenic for plants or humans, such as fungi responsible for crop diseases and Plasmodium falciparum, which causes human malaria. Cytochrome bc1 is an enzyme that contains two (ubi)quinone/quinol‐binding sites, which can be exploited for the development of fungicidal and chemotherapeutic agents. Here, we review recent progress in determination of the structure and mechanism of action of cytochrome bc1, and the associated development of antimicrobial agents (and associated resistance mechanisms) targeting its activity.

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Binding of the respiratory chain inhibitor ametoctradin to the mitochondrialbc₁complex

Cited by 34 publications

References 46 publications

Investigation of the sensitivity of Plasmopara viticola to amisulbrom and ametoctradin in French vineyards using bioassays and molecular tools

Investigation of the sensitivity of Plasmopara viticola to amisulbrom and ametoctradin in French vineyards using bioassays and molecular tools

Fungicide resistance: facing the challenge - a review

The cytochrome bc₁ complex as an antipathogenic target

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Binding of the respiratory chain inhibitor ametoctradin to the mitochondrialbc1complex

Cited by 34 publications

References 46 publications

Investigation of the sensitivity of Plasmopara viticola to amisulbrom and ametoctradin in French vineyards using bioassays and molecular tools

Investigation of the sensitivity of Plasmopara viticola to amisulbrom and ametoctradin in French vineyards using bioassays and molecular tools

Fungicide resistance: facing the challenge - a review

The cytochrome bc1 complex as an antipathogenic target

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Product

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Binding of the respiratory chain inhibitor ametoctradin to the mitochondrialbc₁complex

The cytochrome bc₁ complex as an antipathogenic target