In southern Europe, the intensive use of 2,4-D (2,4-dichlorophenoxyacetic acid) and tribenuron-methyl in cereal crop systems has resulted in the evolution of resistant (R) corn poppy (Papaver rhoeas L.) biotypes. Experiments were conducted to elucidate (1) the resistance response to these two herbicides, (2) the cross-resistant pattern to other synthetic auxins and (3) the physiological basis of the auxin resistance in two R (F-R213 and D-R703) populations. R plants were resistant to both 2,4-D and tribenuron-methyl (F-R213) or just to 2,4-D (D-R703) and both R populations were also resistant to dicamba and aminopyralid. Results from absorption and translocation experiment revealed that R plants translocated less [14C]-2,4-D than S plants at all evaluation times. There was between four and eight-fold greater ethylene production in S plants treated with 2,4-D, than in R plants. Overall, these results suggest that reduced 2,4-D translocation is the resistance mechanism in synthetic auxins R corn poppy populations and this likely leads to less ethylene production and greater survival in R plants.

Target-site and non-target-site resistance mechanisms to ALS inhibitors were investigated in multiple resistant (tribenuron-methyl and 2,4-D) and only 2,4-D resistant, Spanish corn poppy populations. Six amino-acid replacements at the Pro197 position (Ala197, Arg197, His197, Leu197, Thr197 and Ser197) were found in three multiple resistant populations. These replacements were responsible for the high tribenuron-methyl resistance response, and some of them, especially Thr197 and Ser197, elucidated the cross-resistant pattern for imazamox and florasulam, respectively. Mutations outside of the conserved regions of the ALS gene (Gly427 and Leu648) were identified, but not related to resistance response. Higher mobility of labeled tribenuron-methyl in plants with multiple resistance was, however, similar to plants with only 2,4-D resistance, indicating the presence of non-target-site resistance mechanisms (NTSR). Metabolism studies confirmed the presence of a hydroxy imazamox metabolite in one of the populations. Lack of correlation between phenotype and genotype in plants treated with florasulam or imazamox, non-mutated plants surviving imazamox, tribenuron-methyl translocation patterns and the presence of enhanced metabolism revealed signs of the presence of NTSR mechanisms to ALS inhibitors in this species. On this basis, selection pressure with ALS non-SU inhibitors bears the risk of promoting the evolution of NTSR mechanisms in corn poppy.

No abstract

Glyphosate is a broad-spectrum systemic herbicide used to kill weeds, especially annual broadleaf weeds and grasses known to compete with commercial crops grown around the globe. However, weeds evolve and develop resistance to glyphosate. Until recently, no case of glyphosate resistance had been detected in France. Glyphosate resistance was indeed recently recorded in a Lolium rigidum weed population from a vineyard in the South of France. Here, we studied the mechanisms of this resistance case. Seed samples of L. rigidum were collected from the vineyard where resistance had been detected, as well as from a nearby area that had no known history of exposure to glyphosate. We studied the effect of retention of glyphosate spray, shikimic acid accumulation, glyphosate absorption and translocation, glyphosate metabolism, and the sequence of the enzyme that glyphosate targets in plants, 5-enolpyruvylshikimate-3-phosphate synthase. Our results show that glyphosate absorption decreased by 30 % in the resistant L. rigidum weed. In addition, glyphosate translocation out of the treated leaves was reduced by 52 %. Finally, the resistant biotype had a serine amino acid substitution at position 106 of the predicted protein, instead of the proline amino acid present in the susceptible population. Our results suggest that the resistant population of L. rigidum presents three different mechanisms of resistance to glyphosate, namely reduced absorption, reduced mobility in the plants, and a mutation in the gene coding for the enzyme targeted by glyphosate.

A Lolium multiflorum Lam. biotype resistant to diclofop-methyl was found in a Triticum aestivum field in France (Normandy) that had been treated for several years with diclofop-methyl. Based on plant survival evaluated 21 d after herbicide application, the biotype exhibited a high level of resistance to diclofop-methyl and moderate resistance to CGA-184927-propargil and PP-604. The resistant biotype exhibited a small increase in tolerance to haloxyfop-methyl, quizalofop-ethyl, sethoxydim, and BAS-517-H, but was controlled by recommended field rates for these herbicides. The mechanism of resistance was investigated for diclofop-methyl. There was little or no difference in diclofop-methyl absorption by leaves of resistant and susceptible biotypes measured 48 h after treatment. For both biotypes, less than 1% of absorbed radiolabel was translocated during 48 h following foliar application of 14C-diclofop-methyl. Metabolism of diclofop-methyl was not significantly altered in the resistant biotype. In both biotypes, diclofop-methyl was rapidly metabolized to diclofop acid followed by a slow rate of formation of a polar conjugate. Two multifunctional acetyl coenzyme A carboxylase isoforms (ACCase I and ACCase II) were isolated from leaf tissue of resistant and susceptible biotypes. Both isoforms exhibited a subunit molecular mass of 203 kDa. For both resistant and susceptible biotypes, ACCase I constituted approximately 80% of total ACCase activity. Graminicide concentrations required to inhibit ACCase activity by 50% (I50 values) were determined for both ACCase isoforms from resistant and susceptible biotypes. The ACCase II isoform was highly resistant to graminicides in both biotypes. In contrast, the I50 value for diclofop inhibition of ACCase I was 19-fold greater for the enzyme isolated from the resistant biotype compared with the susceptible biotype. It is concluded that diclofop resistance in the L. multiflorum biotype from Normandy is caused by the presence of a resistant form of the ACCase I isoform.