Mechanism of Fenoxaprop-P-ethyl Resistance in Italian Ryegrass (Lolium perennessp.multiflorum) from China

Weed Science ◽  
2017 ◽  
Vol 65 (6) ◽  
pp. 710-717 ◽  
Author(s):  
Pei Zhang ◽  
Han Wu ◽  
Hongle Xu ◽  
Yuan Gao ◽  
Wei Zhang ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Target Site ◽  
Italian Ryegrass ◽  
Mechanisms Of Resistance ◽  
Acetyl Coenzyme A ◽  
Resistant Population ◽  
Chinese Wheat ◽  
Moderately Resistant ◽  
Acetyl Coenzyme A Carboxylase ◽  
Clodinafop Propargyl

Italian ryegrass has invaded wheat fields in China and is becoming a predominant, troublesome weed. Fenoxaprop-P-ethyl has been widely used for weed control on Chinese farms since the 1990s. However, overuse has led to fenoxaprop-P-ethyl resistance in Italian ryegrass in Chinese wheat fields. In this study, we identified a putative fenoxaprop-P-ethyl–resistant population of Italian ryegrass, HZYC-6, from Henan province, China. Mutations involving Asp-2078-Gly and Ile-1781-Leu substitutions were identified in the carboxyl-transferase domain of acetyl-coenzyme A carboxylase in this population, and these mutations are the likely cause of the target site–based resistance to fenoxaprop-P-ethyl. In addition, we identified cytochrome P450–mediated metabolism of herbicides (non–target site based resistance) in the HZYC-6 population, indicating that multiple mechanisms of resistance may be segregating in this population. Furthermore, HZYC-6 was also highly resistant to haloxyfop-R-methyl and quizalofop-P-ethyl, moderately resistant to clodinafop-propargyl and sethoxydim, and had low resistance to clethodim and pinoxaden.

Characterization of Fenoxaprop-P-Ethyl–Resistant Junglerice (Echinochloa colona) from Mississippi

Weed Science ◽  
2016 ◽  
Vol 64 (4) ◽  
pp. 588-595 ◽  
Author(s):  
Alice A. Wright ◽  
Vijay K. Nandula ◽  
Logan Grier ◽  
Kurt C. Showmaker ◽  
Jason A. Bond ◽  
...  
Keyword(s):  
Coenzyme A ◽  
Point Mutations ◽  
Target Site ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme ◽  
Resistant Population ◽  
Sunflower County ◽  
Acetyl Coenzyme A Carboxylase ◽  
P450 Inhibitors

A population of junglerice from Sunflower County, MS, exhibited resistance to fenoxaprop-P-ethyl. An 11-fold difference in ED50 (the effective dose needed to reduce growth by 50%) values was observed when comparing the resistant population (249 g ae ha–1) with susceptible plants (20 g ae ha–1) collected from a different field. The resistant population was controlled by clethodim and sethoxydim at the field rate. Sequencing of the acetyl coenzyme A carboxylase, which encodes the enzyme targeted by fenoxaprop-P-ethyl, did not reveal the presence of any known resistance-conferring point mutations. An enzyme assay confirmed that the acetyl coenzyme A carboxylase in the resistant population is herbicide sensitive. Further investigations with two cytochrome P450 inhibitors, malathion and piperonyl butoxide, and a glutathione-S-transferase inhibitor, 4-chloro-7-nitrobenzofurazan, did not indicate involvement of any metabolic enzymes inhibited by these compounds. The absence of a known target-site point mutation and the sensitivity of the ACCase enzyme to herbicide show that fenoxaprop-P-ethyl resistance in this population is due to a non–target-site mechanism or mechanisms.

Identification of Japanese Foxtail (Alopecurus Japonicus) Resistant to Haloxyfop Using Three Different Assay Techniques

Weed Science ◽  
2007 ◽  
Vol 55 (6) ◽  
pp. 537-540 ◽  
Author(s):  
Caihong Yang ◽  
Liyao Dong ◽  
Jun Li ◽  
Stephen R. Moss
Keyword(s):  
Oilseed Rape ◽  
Coenzyme A ◽  
Resistance Index ◽  
Target Site ◽  
The Other ◽  
Resistance Level ◽  
Acetyl Coenzyme A ◽  
Whole Plant ◽  
Low Degrees ◽  
Acetyl Coenzyme A Carboxylase

The objective of this study was to investigate the resistance level of Japanese foxtail to haloxyfop, an acetyl coenzyme A carboxylase (ACCase; EC 6.4.1.2)–inhibiting herbicide. Eleven biotypes were collected from oilseed rape fields in different areas in Jiangsu and Anhui provinces where haloxyfop had been continuously applied for various periods. Biotypes were assessed by two different methods, a seed bioassay and whole-plant assay, to identify the most resistant and susceptible biotypes for further studies on the activity of the target enzyme ACCase. A good correlation was obtained between the two different bioassay methods. The Jurong and Chuzhou biotypes were the most resistant and susceptible biotypes, respectively, whereas the other nine biotypes showed variable and relatively low degrees of haloxyfop resistance. Furthermore, target-site enzyme sensitivity results confirmed that the Jurong biotype was resistant to haloxyfop with a concentration of herbicide causing 50% inhibition of ACCase activity (IC50) of 9.19 µM, whereas the IC50 of the susceptible biotype (Chuzhou) was 0.76 µM, giving a resistance index of 12.

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