Hostname: page-component-586b7cd67f-t7czq Total loading time: 0 Render date: 2024-11-24T05:41:08.186Z Has data issue: false hasContentIssue false
  • English
  • Français

Confirmation and characterization of cyhalofop-butyl–resistant Chinese sprangletop (Leptochloa chinensis) populations from China

Published online by Cambridge University Press:  14 February 2020

Yajun Peng ,
Lang Pan ,
Ducai Liu ,
Xiaomei Cheng ,
Guolan Ma ,
Sifu Li ,
Xueyuan Liu ,
Lifeng Wang Open the ORCID record for Lifeng Wang [Opens in a new window]  and
Lianyang Bai
Yajun Peng
Affiliation:
Graduate Student, College of Plant Protection, Hunan Agricultural University, Changsha, China Research Associate, Plant Protection Institute, Hunan Academy of Agricultural Sciences, Changsha, China
Lang Pan
Affiliation:
Associate Professor, College of Plant Protection, Hunan Agricultural University, Changsha, China
Ducai Liu
Affiliation:
Professor, Plant Protection Institute, Hunan Academy of Agricultural Sciences, Changsha, China
Xiaomei Cheng
Affiliation:
Research Associate, Institute of Horticulture, Hunan Academy of Agricultural Sciences, Changsha, China
Guolan Ma
Affiliation:
Associate Professor, Plant Protection Institute, Hunan Academy of Agricultural Sciences, Changsha, China
Sifu Li
Affiliation:
Research Associate, Plant Protection Institute, Hunan Academy of Agricultural Sciences, Changsha, China
Xueyuan Liu
Affiliation:
Professor, Plant Protection Institute, Hunan Academy of Agricultural Sciences, Changsha, China
Lifeng Wang*
Affiliation:
Associate Professor, Agricultural Biotechnology Research Institute, Hunan Academy of Agricultural Sciences, Changsha, China
Lianyang Bai*
Affiliation:
Professor, Hunan Academy of Agricultural Sciences, Changsha, China
*
Authors for correspondence: Lifeng Wang, Agricultural Biotechnology Research Institute, Hunan Academy of Agricultural Sciences, No. 2, Yuanda Road, Furong District, Changsha, China Email: [email protected]; Lianyang Bai, Hunan Academy of Agricultural Sciences, No. 2, Yuanda Road, Furong District, Changsha, China. Email: [email protected]
Authors for correspondence: Lifeng Wang, Agricultural Biotechnology Research Institute, Hunan Academy of Agricultural Sciences, No. 2, Yuanda Road, Furong District, Changsha, China Email: [email protected]; Lianyang Bai, Hunan Academy of Agricultural Sciences, No. 2, Yuanda Road, Furong District, Changsha, China. Email: [email protected]
Get access Rights & Permissions [Opens in a new window]

Abstract

Chinese sprangletop [Leptochloa chinensis (L.) Nees] is one grass weed severely affecting rice (Oryza sativa L.) growth in paddies in China. Cyhalofop-butyl is the main herbicide used to control grass weeds in Chinese paddy fields, especially for controlling L. chinensis; however, L. chinensis has evolved resistance to cyhalofop-butyl due to continuous and extensive application. To investigate cyhalofop-butyl resistance levels and mechanisms in L. chinensis in some of the Chinese rice areas, 66 field populations were collected and treated with cyhalofop-butyl. Of these tested populations, 10 showed a high level of resistance to cyhalofop-butyl; the 50% effective dose ranged within 108.4 to 1,443.5 g ai ha−1 with resistance index values of 9.1 to 121.8 when compared with the susceptible population. Acetyl-coenzyme A carboxylase genes (ACCase) of susceptible and all 10 resistant populations were amplified and sequenced. Among them, Ile-1781-Leu, Trp-2027-Cys, Trp-2027-Ser, and Ile-2041-Asn mutations were found in five resistant populations. No known resistance-related mutations were found in the other five resistant populations, indicating that resistance to cyhalofop-butyl in these populations was likely to be endowed by non–target site resistance mechanisms. Notably, the Ile-1781-Leu and Trp-2027-Cys substitutions have previously been reported, but this is the first report of Trp-2027-Ser and Ile-2041-Asn mutations in L. chinensis. Furthermore, three derived cleaved amplified polymorphic sequence methods were developed to rapidly detect these mutations in L. chinensis.

Keywords

ACCaseamino acid substitutiondCAPSresistance mechanism
Type
Research Article
Information
Weed Science , Volume 68 , Issue 3 , May 2020 , pp. 253 - 259
Copyright
© Weed Science Society of America, 2020

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

Footnotes

Associate Editor: Vijay Nandula, USDA–ARS

References

Beckie, HJ, Tardif, FJ (2012) Herbicide cross resistance in weeds. Crop Prot 35:15–2810.1016/j.cropro.2011.12.018CrossRefGoogle Scholar
Cheng, QH, Feng, Q, Lu, ZJ, Jin, ZH (2011) Occurrence causes of Leptochloa chinensis and its control countermeasures in the direct seeding rice field in Haining City of Zhejiang Province. J Weed Sci 29:60–62. ChineseGoogle Scholar
Cruz-Hipolito, H, Domínguez-Valenzuela, JA, Osuna, MD, De Prado, R (2012) Resistance mechanism to acetyl coenzyme A carboxylase inhibiting herbicides in Phalaris paradoxa collected in Mexican wheat fields. Plant Soil 355:121–13010.1007/s11104-011-1085-3CrossRefGoogle Scholar
Délye, C (2005) Weed resistance to acetyl coenzyme A carboxylase inhibitors: an update. Weed Sci 53:728–74610.1614/WS-04-203R.1CrossRefGoogle Scholar
Délye, C (2013) Unravelling the genetic bases of non-target-site-based resistance (NTSR) to herbicides: a major challenge for weed science in the forthcoming decade. Pest Manag Sci 69:176–18710.1002/ps.3318CrossRefGoogle Scholar
Délye, C, Wang, T, Darmency, H (2002) An isoleucine-leucine substitution in chloroplastic acetyl-CoA carboxylase from green foxtail (Setaria viridis L. Beauv.) is responsible for resistance to the cyclohexanedione herbicide sethoxydim. Planta 214:421–42710.1007/s004250100633CrossRefGoogle ScholarPubMed
Délye, C, Zhang, XQ, Chalopin, C, Michel, S, Powles, SB (2003) An isoleucine residue within the carboxyl-transferase domain of multidomain acetyl-coenzyme A carboxylase is a major determinant of sensitivity to aryloxyphenoxypropionate but not to cyclohexanedione inhibitors. Plant Physiol 132:1716–172310.1104/pp.103.021139CrossRefGoogle ScholarPubMed
Délye, C, Zhang, XQ, Michel, S, Matéjicek, A, Powles, SB (2005) Molecular bases for sensitivity to acetyl-coenzyme A carboxylase inhibitors in black-grass. Plant Physiol 137:794–80610.1104/pp.104.046144CrossRefGoogle ScholarPubMed
Deng, W, Cai, JX, Zhang, JY, Chen, YY, Chen, YR, Di, YJ, Yuan, SZ (2019) Molecular basis of resistance to ACCase-inhibiting herbicide cyhalofop-butyl in Chinese sprangletop (Leptochloa chinensis (L.) Nees) from China. Pestic Biochem Physiol 158:143–14810.1016/j.pestbp.2019.05.004CrossRefGoogle ScholarPubMed
Devine, MD (1997) Mechanisms of resistance to acetyl-coenzyme A carboxylase inhibitors: a review. Pestic Sci 51:259–26410.1002/(SICI)1096-9063(199711)51:3<259::AID-PS644>3.0.CO;2-S3.0.CO;2-S>CrossRefGoogle Scholar
Heap, I (2019) Weeds resistant to ACCase inhibitors. In The International Survey of Herbicide Resistant Weeds. http://www.weedscience.org/Summary/MOA.aspx. Accessed: December 25, 2019Google Scholar
Hochberg, O, Sibony, M, Rubin, B (2009) The response of ACCase-resistant Phalaris paradoxa populations involves two different target site mutations. Weed Res 49:37–4610.1111/j.1365-3180.2008.00677.xCrossRefGoogle Scholar
Jang, S, Marjanovic, J, Gornicki, P (2013) Resistance to herbicides caused by single amino acid mutations in acetyl-CoA carboxylase in resistant populations of grassy weeds. New Phytol 197:1110–111610.1111/nph.12117CrossRefGoogle ScholarPubMed
Kaundun, SS, Bailly, GC, Dale, RP, Hutchings, SJ, McIndoe, E (2013a) A novel W1999S mutation and non-target site resistance impact on acetyl-CoA carboxylase inhibiting herbicides to varying degrees in a UK Lolium multiflorum population. PLoS ONE 8:e5801210.1371/journal.pone.0058012CrossRefGoogle Scholar
Kaundun, SS, Hutchings, SJ, Dale, RP, McIndoe, E (2013b) Role of a novel I1781T mutation and other mechanisms in conferring resistance to acetyl-CoA carboxylase inhibiting herbicides in a black-grass population. PLoS ONE 8:e6956810.1371/journal.pone.0069568CrossRefGoogle Scholar
Kuenzer, C, Knauer, K (2013) Remote sensing of rice crop areas. Int J Remote Sens 34:2101–213910.1080/01431161.2012.738946CrossRefGoogle Scholar
Liu, W, Harrison, DK, Chalupska, D, Gornicki, P, O’Donnell, CC, Adkins, SW, Haselkorn, R, Williams, RR (2007) Single-site mutations in the carboxyltransferase domain of plastid acetyl-CoA carboxylase confer resistance to grass-specific herbicides. Proc Natl Acad Sci USA 104:3627–363210.1073/pnas.0611572104CrossRefGoogle ScholarPubMed
[NBSC] National Bureau of Statistics of China (2019) Output of Major Farm Products. http://data.stats.gov.cn/english/easyquery.htm?cn=C01. Accessed: December 25, 2019Google Scholar
Oerke, EC, Dehne, HW (2004) Safeguarding production—losses in major crops and the role of crop protection. Crop Prot 23:275–28510.1016/j.cropro.2003.10.001CrossRefGoogle Scholar
Pan, L, Li, J, Xia, WW, Zhang, D, Dong, LY (2015) An effective method, composed of LAMP and dCAPS, to detect different mutations in fenoxaprop-P-ethylresistant American sloughgrass (Beckmannia syzigachne Steud.) populations. Pestic Biochem Physiol 117:1–810.1016/j.pestbp.2014.10.008CrossRefGoogle ScholarPubMed
Powles, SB, Yu, Q (2010) Evolution in action: plants resistant to herbicides. Annu Rev Plant Biol 61:317–34710.1146/annurev-arplant-042809-112119CrossRefGoogle ScholarPubMed
Warwick, SI, Sauder, CA, Beckie, HJ (2010) Acetolactate synthase (ALS) target-site mutations in ALS inhibitor-resistant Russian thistle (Salsola tragus). Weed Sci 58:244–25110.1614/WS-D-09-00083.1CrossRefGoogle Scholar
Xu, HL, Li, J, Zhang, D, Cheng, Y, Jiang, Y, Dong, LY (2014) Mutations at codon position 1999 of acetyl-CoA carboxylase confer resistance to ACCase-inhibiting herbicides in Japanese foxtail (Alopecurus japonicus). Pest Manag Sci 70:1894–190110.1002/ps.3753CrossRefGoogle Scholar
Xu, HL, Zhu, XD, Wang, HC, Li, J, Dong, LY (2013) Mechanism of resistance to fenoxaprop in Japanese foxtail (Alopecurus japonicus) from China. Pestic Biochem Physiol 107:25–3110.1016/j.pestbp.2013.04.008CrossRefGoogle ScholarPubMed
Yu, JX, Gao, HT, Pan, L, Yao, ZW, Dong, LY (2017) Mechanism of resistance to cyhalofop-butyl in Chinese sprangletop (Leptochloa chinensis (L.) Nees). Pestic Biochem Physiol 143:306–31110.1016/j.pestbp.2016.11.001CrossRefGoogle Scholar
Yu, LP, Kim, YS, Tong, L (2010) Mechanism for the inhibition of the carboxyltransferase domain of acetyl-coenzyme A carboxylase by pinoxaden. Proc Natl Acad Sci USA 107:22072–2207710.1073/pnas.1012039107CrossRefGoogle ScholarPubMed
Yu, Q, Ahmad-Hamdani, MS, Han, H, Christoffers, MJ, Powles, SB (2013) Herbicide resistance-endowing ACCase gene mutations in hexaploid wild oat (Avena fatua): insights into resistance evolution in a hexaploid species. Heredity 110:220–23110.1038/hdy.2012.69CrossRefGoogle Scholar
Yu, Q, Collavo, A, Zheng, MQ, Owen, M, Sattin, M, Powles, SB (2007) Diversity of acetyl-coenzyme A carboxylase mutations in resistant Lolium populations: evaluation using clethodim. Plant Physiol 145:547–55810.1104/pp.107.105262CrossRefGoogle ScholarPubMed
Yuan, JS, Tranel, PJ, Stewart, CN (2007) Non-target-site herbicide resistance: a family business. Trends Plant Sci 12:6–1310.1016/j.tplants.2006.11.001CrossRefGoogle ScholarPubMed
Supplementary material: File

Peng et al. supplementary material

Table S1

Download Peng et al. supplementary material(File)
File 25 KB