Cross-resistance Patterns to Acetyl-CoA Carboxylase Inhibitors Associated with Different Mutations in Japanese Foxtail (Alopecurus japonicus)

Weed Science ◽  
2017 ◽  
Vol 65 (4) ◽  
pp. 444-451 ◽  
Author(s):  
Guoqi Chen ◽  
Lingyue Wang ◽  
Hongle Xu ◽  
Xibao Wu ◽  
Lang Pan ◽  
...  
Keyword(s):  
Amino Acid ◽  
Eastern China ◽  
Cross Resistance ◽  
Amino Acid Substitutions ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Cleaved Amplified Polymorphic Sequence ◽  
Resistance Patterns ◽  
Grass Weed ◽  
Clodinafop Propargyl

Japanese foxtail is a grass weed in eastern China. This weed is controlled by fenoxaprop-P-ethyl, one of the most common acetyl-CoA carboxylase (ACCase)-inhibiting herbicides. Some Japanese foxtail populations have developed resistance to fenoxaprop-P-ethyl, owing to target-site mutations (amino acid substitutions) located within the carboxyl transferase domain of ACCase. In the present study, three mutations were detected in three fenoxaprop-P-ethyl–resistant Japanese foxtail populations: Ile-1781-Leu in JCJT-2, Ile-2041-Asn in JZJR-1, and Asp-2078-Gly in JCWJ-3. Two copies ofACCase(Acc1-1andAcc1-2) were identified, but mutations were detected only inAcc1-1. The derived cleaved amplified polymorphic sequence (dCAPS) method detected these mutations successfully in Japanese foxtail. The mutation frequencies in JCJT-2, JZJR-1, and JCWJ-3 were approximately 98%, 92%, and 87%, respectively. Different cross-resistance patterns to ACCase inhibitors were found in the three resistant populations. JCJT-2 (Ile-1781-Leu) and JZJR-1 (Ile-2041-Asn) showed cross-resistance to haloxyfop-R-methyl, clodinafop-propargyl, and pinoxaden, but were susceptible to clethodim. JCWJ-3 (Asp-2078-Gly) showed cross-resistance to all tested ACCase-inhibiting herbicides.

Characterization of cross-resistance patterns in acetyl-CoA carboxylase inhibitor resistant wild oat (Avena fatua)

Weed Science ◽  
1997 ◽  
Vol 45 (6) ◽  
pp. 750-755 ◽  
Author(s):  
Luc Bourgeois ◽  
Norm C. Kenkel ◽  
Ian N. Morrison
Keyword(s):  
Cluster Analysis ◽  
Principal Component ◽  
Petri Dish ◽  
Cross Resistance ◽  
Wild Oat ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Pairwise Correlation ◽  
Resistance Patterns

The purpose of this study was to determine cross-resistance patterns among wild oat lines resistant to acetyl-CoA carboxylase (ACCase) inhibitors and to determine which, if any, cross-resistant type was more common than another. Discriminatory concentrations of two aryloxyphenoxy-propionates (APP) and three cyclohexanediones (CHD) were determined using a petri-dish bioassay. These concentrations were then applied to 82 resistant wild oat lines identified in previous studies. In addition, two resistant standards (UM1 and UM33) and a susceptible standard (UM5) were included in the experiments. Coleoptile lengths expressed as percentages of untreated controls were used to assess the level of resistance to each herbicide. Large variations were observed among wild oat lines and herbicides. However, cluster analysis summarized the relationship between the five herbicides (variables) and the wild oat lines into three main cross-resistance types. Type A included wild oat lines with high resistance to APP herbicides and no or low resistance to CHD herbicides. Types B and C included those with low to moderate resistant and high levels of resistance to all five herbicides, respectively. Type C was the most common cross-resistance type. Relationships among herbicides were determined using pairwise correlation and principal component analysis (PCA). All correlations were high between APP herbicides and between CHD herbicides but not between APP and CHD herbicides. The first two axes of the PCA accounted for 88.4% of the total variance, with the first axis correlated to the CHD herbicides and the second axis correlated to the APP herbicides. In the PCA, wild oat lines were segregated into the three types identified in the cluster analysis. Although CHD and APP herbicides bind at the same region on the ACCase, resistant wild oat lines respond differently to them.

scholarly journals Biochemical and structural characterization of quizalofop-resistant wheat acetyl-CoA carboxylase

2022 ◽  
Vol 12 (1) ◽  
Author(s):  
Raven Bough ◽  
Franck E. Dayan
Keyword(s):  
Amino Acid ◽  
Winter Wheat ◽  
Amino Acid Substitution ◽  
Reference Sequence ◽  
Cross Resistance ◽  
Homozygous Mutation ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Nucleotide Mutation

AbstractA novel nucleotide mutation in ACC1 resulting in an alanine to valine amino acid substitution in acetyl-CoA carboxylase (ACCase) at position 2004 of the Alopecurus myosuroides reference sequence (A2004V) imparts quizalofop resistance in wheat. Genotypes endowed with the homozygous mutation in one or two ACC1 homoeologs are seven- and 68-fold more resistant to quizalofop than a wildtype winter wheat in greenhouse experiments, respectively. In vitro ACCase activities in soluble protein extracts from these varieties are 3.8- and 39.4-fold more resistant to quizalofop with the homozygous mutation in either one or two genomes, relative to the wildtype. The A2004V mutation does not alter the specific activity of wheat ACCase, suggesting that this resistance trait does not affect the catalytic functions of ACCase. Modeling of wildtype and quizalofop-resistant wheat ACCase demonstrates that the A2004V amino acid substitution causes a reduction in the volume of the binding pocket that hinders quizalofop’s interaction with ACCase. Docking studies confirm that the mutation reduces the binding affinity of quizalofop. Interestingly, the models suggest that the A2004V mutation does not affect haloxyfop binding. Follow up in vivo and in vitro experiments reveal that the mutation, in fact, imparts negative cross-resistance to haloxyfop, with quizalofop-resistant varieties exhibiting higher sensitivity to haloxyfop than the wildtype winter wheat line.

scholarly journals Biochemical and Structural Characterization of Quizalofop-Resistant Wheat Acetyl-Coa Carboxylase

2021 ◽  
Author(s):  
Raven Bough ◽  
Franck Dayan
Keyword(s):  
Amino Acid ◽  
Amino Acid Substitution ◽  
Specific Activity ◽  
Reference Sequence ◽  
Cross Resistance ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Nucleotide Mutation

Abstract A novel nucleotide mutation in ACC1 resulting in an alanine to valine amino acid substitution in acetyl-CoA carboxylase (ACCase) at position 2004 of the Alopecurus myosuroides reference sequence (A2004V) imparts quizalofop resistance in wheat. Genotypes endowed with one or two homozygous mutant ACC1 homoelogs are 7- and 68-fold more resistant to quizalofop than a wildtype variety in greenhouse experiments, respectively. In vitro assays of ACCase activities in protein extracts from these varieties reveal a 3.8- and 39.4-fold increase in resistance to quizalofop in the single and double-mutants relative to the wildtype. The A2004V mutation does not alter the specific activity of wheat ACCase, suggesting that ACCase mutants retain their normal catalytic functions. Modeling of wildtype and quizalofop-resistant wheat ACCase demonstrates that the A2004V amino acid substitution causes a reduction in the volume of the binding pocket that hinders quizalofop’s interaction with ACCase. Docking studies confirm that the mutation reduces the binding affinity of quizalofop. Interestingly, the models suggest that the A2004V mutation does not affect haloxyfop binding. Follow up in vivo and in vitro experiments reveal that the mutation, in fact, imparts negative cross-resistance to haloxyfop, with quizalofop-resistant varieties exhibiting more sensitivity to haloxyfop than the wildtype variety.

scholarly journals Prototypical Recombinant Multi-Protease-Inhibitor-Resistant Infectious Molecular Clones of Human Immunodeficiency Virus Type 1

2013 ◽  
Vol 57 (9) ◽  
pp. 4290-4299 ◽  
Author(s):  
Vici Varghese ◽  
Yumi Mitsuya ◽  
W. Jeffrey Fessel ◽  
Tommy F. Liu ◽  
George L. Melikian ◽  
...  
Keyword(s):  
Amino Acid ◽  
Protease Inhibitor ◽  
Cross Resistance ◽  
Amino Acid Substitutions ◽  
Phenotypic Properties ◽  
The Public ◽  
Immunodeficiency Virus ◽  
The Many ◽  
High Level ◽  
Infectious Molecular Clones

ABSTRACTThe many genetic manifestations of HIV-1 protease inhibitor (PI) resistance present challenges to research into the mechanisms of PI resistance and the assessment of new PIs. To address these challenges, we created a panel of recombinant multi-PI-resistant infectious molecular clones designed to represent the spectrum of clinically relevant multi-PI-resistant viruses. To assess the representativeness of this panel, we examined the sequences of the panel's viruses in the context of a correlation network of PI resistance amino acid substitutions in sequences from more than 10,000 patients. The panel of recombinant infectious molecular clones comprised 29 of 41 study-defined PI resistance amino acid substitutions and 23 of the 27 tightest amino acid substitution clusters. Based on their phenotypic properties, the clones were classified into four groups with increasing cross-resistance to the PIs most commonly used for salvage therapy: lopinavir (LPV), tipranavir (TPV), and darunavir (DRV). The panel of recombinant infectious molecular clones has been made available without restriction through the NIH AIDS Research and Reference Reagent Program. The public availability of the panel makes it possible to compare the inhibitory activities of different PIs with one another. The diversity of the panel and the high-level PI resistance of its clones suggest that investigational PIs active against the clones in this panel will retain antiviral activity against most if not all clinically relevant PI-resistant viruses.

Cross-resistance to acetyl-CoA carboxylase–inhibiting herbicides conferred by a target-site mutation in perennial ryegrass (Lolium perenne) from Argentina

Weed Science ◽  
2020 ◽  
Vol 68 (2) ◽  
pp. 116-124 ◽  
Author(s):  
Marcos Yanniccari ◽  
Ramón Gigón
Keyword(s):  
Seed Production ◽  
Lolium Perenne ◽  
Perennial Ryegrass ◽  
Cross Resistance ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Plant Survival ◽  
Winter Cereal ◽  
Susceptible Population ◽  
Resistant Population

AbstractIn Argentina, Lolium spp. occur in 40% of winter cereal crops from the Pampas. Several years ago, cases of glyphosate-resistant perennial ryegrass (Lolium perenne L.) were detected, and the use of acetyl-CoA carboxylase (ACCase)-inhibiting herbicides to eradicate these plants has been considered. The aim of this study was to evaluate the sensitivity of a putative pinoxaden-resistant L. perenne population to ACCase-inhibiting herbicides. Around 80% of plants from the putative resistant population survived at a recommended dose of pinoxaden, and they produced viable seeds. The resistance indices (RIs) to pinoxaden were 5.1 and 2.8 for plant survival and seed production, respectively. A single point mutation that conferred a Asp-2078-Gly substitution in ACCase was the source of the resistance. To match the plant control achieved in the susceptible population, the resistant population required 5.4- and 10.4-fold greater doses of clethodim and quizalofop, respectively. RIs for viable seed production when treated with clethodim and quizalofop were 3.3 and 6.6, respectively. The Asp-2078-Gly mutation endowed significant levels of resistance to pinoxaden, clethodim, and quizalofop. For three herbicides, the level of resistance of a pinoxaden-resistant L. perenne population to ACCase inhibitors was evaluated, based on an evaluation of dose response for plant survival and seed production. The RIs were higher for plant survival than for seed production. In Argentina, the selection pressure associated with clethodim and haloxifop preplant application and pinoxaden use on wheat (Triticum aestivum L.) and barley (Hordeum vulgare L.) crops, would have favored the propagation of the Asp-2078-Gly mutation with its associated resistance.

scholarly journals Target-Site Mutations Conferring Herbicide Resistance

Plants ◽  
2019 ◽  
Vol 8 (10) ◽  
pp. 382 ◽  
Author(s):  
Brent P. Murphy ◽  
Patrick J. Tranel
Keyword(s):  
Amino Acid ◽  
Herbicide Resistance ◽  
Target Site ◽  
Single Amino Acid ◽  
Cross Resistance ◽  
Target Sites ◽  
Resistance Patterns ◽  
Experimental Approaches ◽  
Sites Of Action ◽  
Multiple Amino Acid

Mutations conferring evolved herbicide resistance in weeds are known in nine different herbicide sites of action. This review summarizes recently reported resistance-conferring mutations for each of these nine target sites. One emerging trend is an increase in reports of multiple mutations, including multiple amino acid changes at the glyphosate target site, as well as mutations involving two nucleotide changes at a single amino acid codon. Standard reference sequences are suggested for target sites for which standards do not already exist. We also discuss experimental approaches for investigating cross-resistance patterns and for investigating fitness costs of specific target-site mutations.

scholarly journals CYP81A P450s are involved in concomitant cross‐resistance to acetolactate synthase and acetyl‐CoA carboxylase herbicides inEchinochloa phyllopogon

2018 ◽  
Vol 221 (4) ◽  
pp. 2112-2122 ◽  
Author(s):  
Satoshi Iwakami ◽  
Yoshitaka Kamidate ◽  
Takuya Yamaguchi ◽  
Masumi Ishizaka ◽  
Masaki Endo ◽  
...  
Keyword(s):  
Acetolactate Synthase ◽  
Cross Resistance ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa
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