Characterization and diagnostic tests of resistance to acetohydroxyacid synthase inhibitors due to an Asp376Glu substitution in Amaranthus powellii

Ashigh, Jamshid; Corbett, Cheryl-Ann L.; Smith, Peter; Laplante, Julie; Tardif, François J.

doi:10.1016/j.pestbp.2009.06.002

Cited by 40 publications

(26 citation statements)

References 27 publications

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“…To date, the AHAS single-nucleotide polymorphism Asp376Glu has been reported in eight different weed species: Amaranthus powellii [1], Schoenoplectus juncoides [20], Kochia scoparia [32], Monochoria vaginalis [13], Conyza Canadensis [41], Galium spurium [3] Raphanus raphanistrum [39] and Amaranthus hybridus [35]. All studies have shown that the Asp376Glu mutation endowed high levels of resistance against sulfonylurea and triazolpyrimidine herbicides, whereas variable resistance levels were found for imidazolinone herbicides depending on the weed species studied.…”

Section: Discussionmentioning

confidence: 99%

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Acetohydroxyacid synthase (AHAS) amino acid substitution Asp376Glu in Lolium perenne: effect on herbicide efficacy and plant growth

Menegat

Bailly

Aponte³

et al. 2016

J Plant Dis Prot

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Recently, the acetohydroxyacid synthase (AHAS) amino acid substitution Asp376Glu was detected in a Lolium perenne population originating in France. This is the first documented occurrence of the Asp376Glu single-nucleotide polymorphism in a Lolium species. The effects on herbicide efficacy and plant fitness are presented. Separation of the original population into different genetic subgroups allowed the comparison of different L. perenne AHAS genotypes according to their susceptibility to AHAS-inhibiting herbicides. Root and shoot biomass accumulation as well as tiller production was analysed for resistant and sensitive populations. Genotype-specific AHAS activity and inhibition were studied in vitro, using recombinant Arabidopsis thaliana DNA. Plants expressing the AHAS Asp376Glu genotype were resistant against mesosulfuron ? iodosulfuron, pyroxsulam and propoxycarbazone. To imazamox, reduced susceptibility for dosages below 140 g a.i. ha -1 was observed. In the absence of herbicide, no significant impact of the Asp376Glu genotype on shoot biomass and tiller accumulation could be observed, whereas root biomass of the Asp376Glu genotype was significantly reduced by 68 % compared to the AHAS genetic wild type. The AHAS enzyme study revealed reduced AHAS enzyme rate of 48 % for the Asp376Glu genotype compared to the AHAS genetic wild type. This study highlights the role of the amino acid exchange on resistance profile against the most relevant AHAS-inhibiting herbicides. First indications were found that fitness of the Asp376Glu genotype is hampered.

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Section: Discussionmentioning

confidence: 99%

“…Despite the impact on AHAS inhibitor efficacy, the Asp376Glu amino acid substitution is the fourth least reported globally with only eight reported species to date, whereof only one is a monocotyledonous species [1,3,13,20,32,39,41].…”

Section: Introductionmentioning

confidence: 99%

Acetohydroxyacid synthase (AHAS) amino acid substitution Asp376Glu in Lolium perenne: effect on herbicide efficacy and plant growth

Menegat

Bailly

Aponte³

et al. 2016

J Plant Dis Prot

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“…Nevertheless, in the closely related species A . powellii and C. canadensis , the Asp‐376‐Glu mutation confers resistance to some of the same AHAS inhibitor herbicides, albeit at lower levels (9–47‐fold based on GR 50 R/S ratios) (although it might be worth noting that GR 50 R/S ratios are more variable than LD 50 ratios dependent on the design, conditions and, in particular, the length of experiments). These results indicate that generalisations on the patterns and levels of cross‐resistance to AHAS inhibitor herbicides endowed by specific AHAS mutations cannot be based on response to one or two herbicides from a particular AHAS inhibitor chemical group.…”

Section: Target‐site Resistancementioning

confidence: 99%

Resistance to AHAS inhibitor herbicides: current understanding

Powles

2014

Pest Management Science

374

442

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Acetohydroxyacid synthase (AHAS) inhibitor herbicides currently comprise the largest site-of-action group (with 54 active ingredients across five chemical groups) and have been widely used in world agriculture since they were first introduced in 1982. Resistance evolution in weeds to AHAS inhibitors has been rapid and identified in populations of many weed species. Often, evolved resistance is associated with point mutations in the target AHAS gene; however non-target-site enhanced herbicide metabolism occurs as well. Many AHAS gene resistance mutations can occur and be rapidly enriched owing to a high initial resistance gene frequency, simple and dominant genetic inheritance and lack of major fitness cost of the resistance alleles. Major advances in the elucidation of the crystal structure of the AHAS (Arabidopsis thaliana) catalytic subunit in complex with various AHAS inhibitor herbicides have greatly improved current understanding of the detailed molecular interactions between AHAS, cofactors and herbicides. Compared with target-site resistance, non-target-site resistance to AHAS inhibitor herbicides is less studied and hence less understood. In a few well-studied cases, non-target-site resistance is due to enhanced rates of herbicide metabolism (metabolic resistance), mimicking that occurring in tolerant crop species and often involving cytochrome P450 monooxygenases. However, the specific herbicide-metabolising, resistance-endowing genes are yet to be identified in resistant weed species. The current state of mechanistic understanding of AHAS inhibitor herbicide resistance is reviewed, and outstanding research issues are outlined.

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“…As reported by many researchers, the amino acid substitutions at Pro 197 by Ser, His, Leu, Ala or Thr have been observed to result in resistance to SU herbicides (Heap 2017). Some of the mutations have a potential to confer broad-spectrum resistance to all five herbicide inhibitor classes SU, IMI, TP, PTB and SCT which are Asp-376-Glu, Ala-205-Val, and Trp-574-Leu (Ashigh et al 2009;Powles & Yu 2010).…”

Section: Discussionmentioning

confidence: 86%

Patterns of resistance to AHAS inhibitors in Limnocharis flava from Malaysia

Zkaria¹,

Ahmad-Hamdani²,

Juraimi³

2018

Plant Prot. Sci.

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Zakaria N., Ahmad-Hamdani M.S., Juraimi A.S. (2018): Patterns of resistance to AHAS inhibitors in Limnocharis flava from Malaysia. Plant Protect. Sci., 54: 48-59.Limnocharis flava (L.) Buchenau is among the most problematic rice weeds in Malaysia and is also reported to have developed multiple resistance to AHAS inhibitor bensulfuron-methyl and synthetic auxin 2,4-D. In this study, resistance across different AHAS inhibitors was characterised in a L. flava population infesting rice fields in Pulau Pinang, Malaysia. Dose-response experiments were conducted to determine the level of resistance to sulfonylureas, imidazolinone, triazolopyrimidine, and pyrimidinyl-thiobenzoate. Cross-resistance across different AHAS inhibitors was observed in the resistant L. flava population, exhibiting a high level of resistance to bensulfuron-methyl, while exhibiting a moderate level of resistance to metsulfuron-methyl and a low level of resistance to pyrazosulfuron-ethyl and pyribenzoxim. However, all resistant L. flava individuals were still sensitive to imazethapyr, penoxsulam, and bispyribac-sodium. Based on the results, it is likely that resistance to AHAS inhibitors in L. flava is conferred by target-site resistance mechanisms.

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Characterization and diagnostic tests of resistance to acetohydroxyacid synthase inhibitors due to an Asp376Glu substitution in Amaranthus powellii

Cited by 40 publications

References 27 publications

Acetohydroxyacid synthase (AHAS) amino acid substitution Asp376Glu in Lolium perenne: effect on herbicide efficacy and plant growth

Acetohydroxyacid synthase (AHAS) amino acid substitution Asp376Glu in Lolium perenne: effect on herbicide efficacy and plant growth

Resistance to AHAS inhibitor herbicides: current understanding

Patterns of resistance to AHAS inhibitors in Limnocharis flava from Malaysia

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