scholarly journals Point Mutations and Cytochrome P450 Can Contribute to Resistance to ACCase-Inhibiting Herbicides in Three Phalaris Species

Plants ◽  
2021 ◽  
Vol 10 (8) ◽  
pp. 1703
Author(s):  
José G. Vázquez-García ◽  
Joel Torra ◽  
Candelario Palma-Bautista ◽  
Ricardo Alcántara-de la Cruz ◽  
Rafael De Prado
Keyword(s):  
Point Mutations ◽  
Resistance Mechanisms ◽  
Target Site ◽  
In Vitro Assays ◽  
Cross Resistance ◽  
Northern Iran ◽  
Target Site Resistance ◽  
Acetyl Coenzyme A Carboxylase ◽  
Selection Of

Species of Phalaris have historically been controlled by acetyl-coenzyme A carboxylase (ACCase)-inhibiting herbicides; however, overreliance on herbicides with this mechanism of action has resulted in the selection of resistant biotypes. The resistance to ACCase-inhibiting herbicides was characterized in Phalaris brachystachys, Phalaris minor, and Phalaris paradoxa samples collected from winter wheat fields in northern Iran. Three resistant (R) biotypes, one of each Phalaris species, presented high cross-resistance levels to diclofop-methyl, cycloxydim, and pinoxaden, which belong to the chemical families of aryloxyphenoxypropionates (FOPs), cyclohexanediones (DIMs), and phenylpyrazolines (DENs), respectively. The metabolism of 14C-diclofop-methyl contributed to the resistance of the P. brachystachys R biotype, while no evidence of herbicide metabolism was found in P. minor or P. paradoxa. ACCase in vitro assays showed that the target sites were very sensitive to FOP, DIM, and DEN herbicides in the S biotypes of the three species, while the R Phalaris spp. biotypes presented different levels of resistance to these herbicides. ACCase gene sequencing confirmed that cross-resistance in Phalaris species was conferred by specific point mutations. Resistance in the P. brachystachys R biotype was due to target site and non-target-site resistance mechanisms, while in P. minor and P. paradoxa, only an altered target site was found.

Target and Non–target site Mechanisms Confer Resistance to Glyphosate in Canadian Accessions ofConyza canadensis

Weed Science ◽  
2017 ◽  
Vol 66 (2) ◽  
pp. 234-245 ◽  
Author(s):  
Eric R. Page ◽  
Christopher M. Grainger ◽  
Martin Laforest ◽  
Robert E. Nurse ◽  
Istvan Rajcan ◽  
...  
Keyword(s):  
Ssr Markers ◽  
Resistance Mechanisms ◽  
Target Site ◽  
Conyza Canadensis ◽  
Weed Species ◽  
Target Site Resistance ◽  
Selection For ◽  
Simple Sequence ◽  
Growing Region ◽  
Selection Of

Glyphosate-resistant populations ofConyza canadensishave been spreading at a rapid rate in Ontario, Canada, since first being documented in 2010. Determining the genetic relationship among existing Ontario populations is necessary to understand the spread and selection of the resistant biotypes. The objectives of this study were to: (1) characterize the genetic variation ofC. canadensisaccessions from the province of Ontario using simple sequence repeat (SSR) markers and (2) investigate the molecular mechanism (s) conferring resistance in these accessions. Ninety-eightC. canadensisaccessions were genotyped using 8 SSR markers. Germinable accessions were challenged with glyphosate to determine their dose response, and the sequences of 5-enolpyruvylshikimate-3-phosphate synthase genes 1 and 2 were obtained. Results indicate that a majority of glyphosate-resistant accessions from Ontario possessed a proline to serine substitution at position 106, which has previously been reported to confer glyphosate resistance in other crop and weed species. Accessions possessing this substitution demonstrated notably higher levels of resistance than non–target site resistant (NTSR) accessions from within or outside the growing region and were observed to form a subpopulation genetically distinct from geographically proximate glyphosate-susceptible and NTSR accessions. Although it is unclear whether other non–target site resistance mechanisms are contributing to the levels of resistance observed in target-site resistant accessions, these results indicate that, at a minimum, selection for Pro-106-Ser has occurred in addition to selection for non–target site resistance and has significantly enhanced the levels of resistance to glyphosate inC. canadensisaccessions from Ontario.

scholarly journals Resistance to ACCase inhibitors in Eleusine indica from Brazil involves a target site mutation

2012 ◽  
Vol 30 (3) ◽  
pp. 675-681 ◽  
Author(s):  
M.D. Osuna ◽  
I.C.G.R. Goulart ◽  
R.A. Vidal ◽  
A. Kalsing ◽  
J.P. Ruiz Santaella ◽  
...  
Keyword(s):  
Amino Acid Position ◽  
Target Site ◽  
In Vitro Assays ◽  
Site Mutation ◽  
Eleusine Indica ◽  
Herbicide Resistant ◽  
Frequent Use ◽  
Target Site Resistance ◽  
Grass Weed

Eleusine indica (goosegrass) is a diploid grass weed which has developed resistance to ACCase inhibitors during the last ten years due to the intensive and frequent use of sethoxydim to control grass weeds in soybean crops in Brazil. Plant dose-response assays confirmed the resistant behaviour of one biotype obtaining high resistance factor values: 143 (fenoxaprop), 126 (haloxyfop), 84 (sethoxydim) to 58 (fluazifop). ACCase in vitro assays indicated a target site resistance as the main cause of reduced susceptibility to ACCase inhibitors. PCR-generated fragments of the ACCase CT domain of the resistant and sensitive reference biotype were sequenced and compared. A point mutation was detected within the triplet of aspartate at the amino acid position 2078 (referred to EMBL accession no. AJ310767) and resulted in the triplet of glycine. These results constitute the first report on a target site mutation for a Brazilian herbicide resistant grass weed.

scholarly journals Point Mutations as Main Resistance Mechanism Together With P450-Based Metabolism Confer Broad Resistance to Different ALS-Inhibiting Herbicides in Glebionis coronaria From Tunisia

2021 ◽  
Vol 12 ◽  
Author(s):  
Zeineb Hada ◽  
Yosra Menchari ◽  
Antonia M. Rojano-Delgado ◽  
Joel Torra ◽  
Julio Menéndez ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Dose Response ◽  
Resistance Mechanism ◽  
Point Mutations ◽  
Acetolactate Synthase ◽  
Target Site ◽  
Cross Resistance ◽  
P450 Monooxygenase ◽  
Target Site Resistance ◽  
Sites Of Action

Resistance to acetolactate synthase (ALS) inhibiting herbicides has recently been reported in Glebionis coronaria from wheat fields in northern Tunisia, where the weed is widespread. However, potential resistance mechanisms conferring resistance in these populations are unknown. The aim of this research was to study target-site resistance (TSR) and non-target-site resistance (NTSR) mechanisms present in two putative resistant (R) populations. Dose–response experiments, ALS enzyme activity assays, ALS gene sequencing, absorption and translocation experiments with radiolabeled herbicides, and metabolism experiments were carried out for this purpose. Whole plant trials confirmed high resistance levels to tribenuron and cross-resistance to florasulam and imazamox. ALS enzyme activity further confirmed cross-resistance to these three herbicides and also to bispyribac, but not to flucarbazone. Sequence analysis revealed the presence of amino acid substitutions in positions 197, 376, and 574 of the target enzyme. Among the NTSR mechanisms investigated, absorption or translocation did not contribute to resistance, while evidences of the presence of enhanced metabolism were provided. A pretreatment with the cytochrome P450 monooxygenase (P450) inhibitor malathion partially synergized with imazamox in post-emergence but not with tribenuron in dose–response experiments. Additionally, an imazamox hydroxyl metabolite was detected in both R populations in metabolism experiments, which disappeared with the pretreatment with malathion. This study confirms the evolution of cross-resistance to ALS inhibiting herbicides in G. coronaria from Tunisia through TSR and NTSR mechanisms. The presence of enhanced metabolism involving P450 is threatening the chemical management of this weed in Tunisian wheat fields, since it might confer cross-resistance to other sites of action.

scholarly journals Non-Target-Site Resistance to Herbicides: Recent Developments

Plants ◽  
2019 ◽  
Vol 8 (10) ◽  
pp. 417 ◽  
Author(s):  
Jugulam ◽  
Shyam
Keyword(s):  
Weed Management ◽  
Management Strategies ◽  
Target Site ◽  
Cross Resistance ◽  
Weed Species ◽  
Physiological Processes ◽  
Recent Developments ◽  
Target Site Resistance ◽  
Resistance To Herbicides ◽  
Selection Of

Non-target-site resistance (NTSR) to herbicides in weeds can be conferred as a result of the alteration of one or more physiological processes, including herbicide absorption, translocation, sequestration, and metabolism. The mechanisms of NTSR are generally more complex to decipher than target-site resistance (TSR) and can impart cross-resistance to herbicides with different modes of action. Metabolism-based NTSR has been reported in many agriculturally important weeds, although reduced translocation and sequestration of herbicides has also been found in some weeds. This review focuses on summarizing the recent advances in our understanding of the physiological, biochemical, and molecular basis of NTSR mechanisms found in weed species. Further, the importance of examining the co-existence of TSR and NTSR for the same herbicide in the same weed species and influence of environmental conditions in the altering and selection of NTSR is also discussed. Knowledge of the prevalence of NTSR mechanisms and co-existing TSR and NTSR in weeds is crucial for designing sustainable weed management strategies to discourage the further evolution and selection of herbicide resistance in weeds.

Target-Site Resistance Mechanisms to Tribenuron-methyl and Cross-resistance Patterns to ALS-inhibiting Herbicides of Catchweed Bedstraw (Galium aparine) with Different ALS Mutations

Weed Science ◽  
2018 ◽  
Vol 67 (2) ◽  
pp. 183-188 ◽  
Author(s):  
Wei Deng ◽  
Yingjie Di ◽  
Jingxuan Cai ◽  
Yueyang Chen ◽  
Shuzhong Yuan
Keyword(s):  
Acetolactate Synthase ◽  
Resistance Mechanisms ◽  
Target Site ◽  
Cross Resistance ◽  
Susceptible Population ◽  
Resistance Evolution ◽  
Galium Aparine ◽  
Resistance Patterns ◽  
Target Site Resistance ◽  
Tribenuron Methyl

AbstractCatchweed bedstraw (Galium aparine L.) is a problematic dicot weed that occurs in major winter wheat (Triticum aestivum L.) fields in China. Tribenuron-methyl has been widely used to control broadleaf weeds since 1988 in China. However, overuse has led to the resistance evolution of G. aparine to tribenuron-methyl. In this study, 20 G. aparine populations collected from Shandong and Henan provinces were used to determine tribenuron-methyl resistance and target-site resistance mechanisms. In dose–response experiments, 12 G. aparine populations showed different resistance levels (2.92 to 842.41-fold) to tribenuron-methyl compared with the susceptible population. Five different acetolactate synthase (ALS) mutations (Pro-197-Leu, Pro-197-Ser, Pro-197-His, Asp-376-Glu, and Trp-574-Leu) were detected in different resistant populations. Individuals heterozygous for Pro-197-Ser and Trp-574-Leu mutations were also observed in a resistant population (HN6). In addition, pHB4 (Pro-197-Ser), pHB7 (Pro-197-His), pHB8 (Pro-197-Leu), pHB5 (Asp-376-Glu), and pHB3 (Trp-574-Leu) subpopulations individually homozygous for specific ALS mutations were generated to evaluate the cross-resistance to ALS-inhibiting herbicides. The pHB4, pHB7, pHB8, pHB5, and pHB3 subpopulations all were resistant to sulfonylurea, pyrazosulfuron-ethyl, triazolopyrimidine, flumetsulam, sulfonylamino-carbonyl-triazolinone, flucarbazone-sodium, pyrimidinyl thiobenzoate, pyribenzoxim, and the imidazolinone imazethapyr. These results indicated the diversity of the resistance-conferring ALS mutations in G. aparine, and all these mutations resulted in broad cross-resistance to five kinds of ALS-inhibiting herbicides.

Target-Site Point Mutations Conferring Resistance to ACCase-Inhibiting Herbicides in Smooth Barley (Hordeum glaucum) and Hare Barley (Hordeum leporinum)

Weed Science ◽  
2015 ◽  
Vol 63 (2) ◽  
pp. 408-415 ◽  
Author(s):  
Lovreet S. Shergill ◽  
Jenna Malone ◽  
Peter Boutsalis ◽  
Christopher Preston ◽  
Gurjeet Gill
Keyword(s):  
Fatty Acid Biosynthesis ◽  
Point Mutations ◽  
Target Site ◽  
Shoot Biomass ◽  
Acid Biosynthesis ◽  
Target Site Resistance ◽  
Hordeum Leporinum ◽  
Different Populations ◽  
Acetyl Coenzyme A Carboxylase ◽  
Experienced Difficulty

Acetyl coenzyme A carboxylase (ACCase)-inhibiting herbicides affect fatty acid biosynthesis in plants and are widely used to control smooth and hare barley in dicot crops in Australia. Recently, growers have experienced difficulty in controlling smooth and hare barley with herbicides from this mode of action. Dose–response experiments conducted on five suspected resistant populations confirmed varying levels of resistance to quizalofop and haloxyfop. The level of resistance in these populations was greater than 27-fold to quizalofop and greater than 15-fold to haloxyfop. The quizalofop dose required to reduce shoot biomass by 50% (GR50) for the resistant populations varied from 52.6 to 111.9 g ha−1, and for haloxyfop from 26.5 to 71.3 g ha−1. Sequencing the CT domain of the ACCase gene from resistant plants of different populations confirmed the presence of previously known mutations Ile1781Leu and Gly2096Ala. Amino acid substitution at the 2096 position conferred a greater level of resistance to haloxyfop than the substitution at the 1781 position. This study documents the first known case of field-evolved target-site resistance to ACCase-inhibiting herbicides in Australian populations of smooth barley.

scholarly journals Target-Site and Non-target-Site Resistance Mechanisms Confer Multiple and Cross- Resistance to ALS and ACCase Inhibiting Herbicides in Lolium rigidum From Spain

2021 ◽  
Vol 12 ◽  
Author(s):  
Joel Torra ◽  
José María Montull ◽  
Andreu Taberner ◽  
Nawaporn Onkokesung ◽  
Neil Boonham ◽  
...  
Keyword(s):  
Glutathione Transferase ◽  
Point Mutations ◽  
Acetolactate Synthase ◽  
Target Site ◽  
Cross Resistance ◽  
Lolium Rigidum ◽  
P450 Monooxygenase ◽  
Winter Cereals ◽  
Target Site Resistance ◽  
Sites Of Action

Lolium rigidum is one the worst herbicide resistant (HR) weeds worldwide due to its proneness to evolve multiple and cross resistance to several sites of action (SoA). In winter cereals crops in Spain, resistance to acetolactate synthase (ALS)- and acetyl-CoA carboxylase (ACCase)-inhibiting herbicides has become widespread, with farmers having to rely on pre-emergence herbicides over the last two decades to maintain weed control. Recently, lack of control with very long-chain fatty acid synthesis (VLCFAS)-inhibiting herbicides has been reported in HR populations that are difficult to manage by chemical means. In this study, three Spanish populations of L. rigidum from winter cereals were confirmed as being resistant to ALS- and ACCase-inhibiting herbicides, with broad-ranging resistance toward the different chemistries tested. In addition, reduced sensitivity to photosystem II-, VLCFAS-, and phytoene desaturase-inhibiting herbicides were confirmed across the three populations. Resistance to ACCase-inhibiting herbicides was associated with point mutations in positions Trp-2027 and Asp-2078 of the enzyme conferring target site resistance (TSR), while none were detected in the ALS enzyme. Additionally, HR populations contained enhanced amounts of an ortholog of the glutathione transferase phi (F) class 1 (GSTF1) protein, a functional biomarker of non-target-site resistance (NTSR), as confirmed by enzyme-linked immunosorbent assays. Further evidence of NTSR was obtained in dose-response experiments with prosulfocarb applied post-emergence, following pre-treatment with the cytochrome P450 monooxygenase inhibitor malathion, which partially reversed resistance. This study confirms the evolution of multiple and cross resistance to ALS- and ACCase inhibiting herbicides in L. rigidum from Spain by mechanisms consistent with the presence of both TSR and NTSR. Moreover, the results suggest that NTSR, probably by means of enhanced metabolism involving more than one detoxifying enzyme family, confers cross resistance to other SoA. The study further demonstrates the urgent need to monitor and prevent the further evolution of herbicide resistance in L. rigidum in Mediterranean areas.

Target site–based resistance to penoxsulam in late watergrass (Echinochloa phyllopogon) from China

Weed Science ◽  
2019 ◽  
Vol 67 (4) ◽  
pp. 380-388 ◽  
Author(s):  
Jian Liu ◽  
Jiapeng Fang ◽  
Zongzhe He ◽  
Jun Li ◽  
Liyao Dong
Keyword(s):  
Binding Affinity ◽  
Acetolactate Synthase ◽  
Resistance Mechanisms ◽  
Target Site ◽  
Future Research ◽  
Target Site Resistance ◽  
Target Gene Sequence ◽  
Als Inhibitors ◽  
Echinochloa Phyllopogon

AbstractLate watergrass [Echinochloa phyllopogon (Stapf) Koso-Pol.] is one of the most persistent weeds in rice fields and shows resistance to some acetolactate synthase (ALS)-inhibiting herbicides, such as penoxsulam. Previous studies of E. phyllopogon’s herbicide resistance have focused on non–target site resistance mechanisms. In this study, E. phyllopogon populations from Heilong Jiang Province, China, that were possibly resistant to penoxsulam were used to identify the target site–based mechanisms of resistance. Population HSRH-520 showed a 25.4-fold higher resistance to penoxsulam than the sensitive population, HSRH-538. HSRH-520 was resistant to other ALS inhibitors, with resistance indexes ranging from 17.1 to 166. Target-gene sequence analysis revealed two different ALS genes in E. phyllopogon; a Pro-197-Ser substitution occurred in the ALS-2 gene of HSRH-520. In vitro activity assays revealed that the penoxsulam concentrations required to inhibit 50% of the ALS activity were 13.7 times higher in HSRH-520 than in HSRH-538. Molecular-docking tests showed that the Pro-197-Ser mutation reduced the binding affinity between ALS and ALS inhibitors belonging to the triazolopyrimidine, sulfonylaminocarbonyltriazolinone, and sulfonylurea families, and there were almost no effects on binding affinity when the ALS inhibitors were of the pyrimidinylthiobenzoate and imidazolinone families. Overall, the results indicated and verified that the Pro-197-Ser mutation leads to increased ALS activity by reducing the binding affinity of the inhibitor and ALS. This is the first report on the Pro-197-Ser mutation in the complete ALS gene of E. phyllopogon and will aid future research of target site–based resistance mechanisms of E. phyllopogon to ALS inhibitors.

scholarly journals Substantiation inEnterococcus faecalisof Dose-Dependent Resistance and Cross-Resistance to Pore-Forming Antimicrobial Peptides by Use of a Polydiacetylene-Based Colorimetric Assay

2010 ◽  
Vol 77 (3) ◽  
pp. 786-793 ◽  
Author(s):  
Jitender Mehla ◽  
S. K. Sood
Keyword(s):  
Colorimetric Assay ◽  
Physiological Activity ◽  
Resistance Mechanisms ◽  
Cross Resistance ◽  
Common Mechanism ◽  
Membrane Phospholipids ◽  
Mechanism Of Resistance ◽  
Colorimetric Response ◽  
Dose Dependent

ABSTRACTA better understanding of the antimicrobial peptide (AMP) resistance mechanisms of bacteria will facilitate the design of effective and potent AMPs. Therefore, to understand resistance mechanisms and forin vitroassessment, variants ofEnterococcus faecalisthat are resistant to different doses of the fungal AMP alamethicin (Almr) were selected and characterized. The resistance developed was dose dependent, as both doses of alamethicin and degrees of resistance were colinear. The formation of bacterial cell aggregates observed in resistant cells may be the prime mechanism of resistance because overall, a smaller cell surface in aggregated cells is exposed to AMPs. Increased rigidity of the membranes of Almrvariants, because of their altered fatty acids, was correlated with limited membrane penetration by alamethicin. Thus, resistance developed against alamethicin was an adaptation of the bacterial cells through changes in their morphological features and physiological activity and the composition of membrane phospholipids. The Almrvariants showed cross-resistance to pediocin, which indicated that resistance developed against both AMPs may share a mechanism, i.e., an alteration in the cell membrane. High percentages of colorimetric response by both AMPs against polydiacetylene/lipid biomimetic membranes of Almrvariants confirmed that altered phospholipid and fatty acid compositions were responsible for acquisition of resistance. So far, this is the only report of quantification of resistance and cross-resistance using anin vitrocolorimetric approach. Our results imply that a single AMP or AMP analog may be effective against bacterial strains having a common mechanism of resistance. Therefore, an understanding of resistance would contribute to the development of a single efficient, potent AMP against resistant strains that share a mechanism of resistance.

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