Hostname: page-component-cd9895bd7-hc48f Total loading time: 0 Render date: 2024-12-21T12:43:51.843Z Has data issue: false hasContentIssue false
  • English
  • Français

First report of molecular basis of resistance to imazethapyr in common lambsquarters (Chenopodium album)

Published online by Cambridge University Press:  29 October 2019

Zhaofeng Huang Open the ORCID record for Zhaofeng Huang [Opens in a new window] ,
Xinxin Zhou ,
Chaoxian Zhang ,
Cuilan Jiang ,
Hongjuan Huang  and
Shouhui Wei
Zhaofeng Huang
Affiliation:
Associate Professor, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China
Xinxin Zhou
Affiliation:
Associate Professor, Institute for the Control of Agrochemicals, Ministry of Agriculture and Rural Affairs, Beijing, China
Chaoxian Zhang
Affiliation:
Professor, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China
Cuilan Jiang
Affiliation:
Assistant Professor, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China
Hongjuan Huang*
Affiliation:
Associate Professor, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China
Shouhui Wei*
Affiliation:
Associate Professor, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, China
*
Authors for correspondence: Shouhui Wei and Hongjuan Huang, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, 100193, China. (Emails: shwei@ippcaas.cn, hjhuang@ippcaas.cn)
Authors for correspondence: Shouhui Wei and Hongjuan Huang, Institute of Plant Protection, Chinese Academy of Agricultural Sciences, Beijing, 100193, China. (Emails: shwei@ippcaas.cn, hjhuang@ippcaas.cn)
Get access Rights & Permissions [Opens in a new window]

Abstract

Common lambsquarters (Chenopodium album L.) is one of the most troublesome weeds in soybean [Glycine max (L.) Merr.] and corn (Zea mays L.) fields in northeast China. In 2017, a C. album population that survived imazethapyr at the recommended field rate was collected from a soybean field in Heilongjiang Province in China. Experiments were conducted to determine the basis of resistance to imazethapyr and investigate the herbicide-resistance pattern in C. album. Dose–response tests showed that the resistant population (R) displayed high resistance to imazethapyr (20-fold) compared with the susceptible population (S). An in vitro acetolactate synthase (ALS) activity assay indicated that the ALS of the R population was resistant to imazethapyr compared with the ALS of the S population. Sequence analysis of the ALS gene revealed that the GCA was replaced by ACA at amino acid position 122, which resulted in an alanine to threonine substitution (Ala-122-Thr) in the R population. The R population displayed cross-resistance to thifensulfuron-methyl and flumetsulam but susceptibility to bispyribac-sodium, flucarbazone, glyphosate, mesotrione, and fomesafen. These results confirmed that the basis of imazethapyr resistance in C. album was conferred by the Ala-122-Thr substitution in the ALS enzyme. This is the first report of the target-site basis of ALS-inhibiting herbicide resistance in C. album.

Keywords

ALS enzymeherbicideherbicide resistancetarget sitemutation
Type
Research Article
Information
Weed Science , Volume 68 , Issue 1 , January 2020 , pp. 63 - 68
Copyright
© Weed Science Society of America, 2019

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: Franck E. Dayan, Colorado State University

References

Baio, FHR, Pires, LF, Tomquelski, G (2013) Mapping hairy beggarticks resistant to ALS herbicide in the Mato Grosso do Sul region. Biosci J 29:59–64Google Scholar
Bernasconi, P, Woodworth, AR, Rosen, BA, Subramanian, MV, Siehl, DL (1995) A naturally occurring point mutation confers broad range tolerance to herbicides that target acetolactate synthase. J Biol Chem 270:17381–17385CrossRefGoogle ScholarPubMed
Chaleff, RS, Mauvais, CJ (1984) Acetolactate synthase is the site of action of two sulfonylurea herbicides in higher plants. Science 224:1443–1445CrossRefGoogle ScholarPubMed
Devine, MD, Shukla, A (2000) Altered target sites as a mechanism of herbicide resistance. Crop Prot 19:881–889CrossRefGoogle Scholar
Duggleby, R, McCourt, JA, Guddat, LW (2008) Structure and mechanism of inhibition of plant acetohydroxy acid synthase. Plant Physiol Biochem 46:309–324CrossRefGoogle Scholar
Durner, J, Gailus, V, Boger, P (1990) New aspects on inhibition of plant acetolactate synthase by chlorsulfuron and imazaquin. Plant Physiol 95:1144–1149CrossRefGoogle Scholar
Ferguson, GM, Hamill, AS, Tardif, FJ (2001) ALS-inhibitor resistance in populations of Amaranthus powellii and Amaranthus retroflexus. Weed Sci 49:448–454CrossRefGoogle Scholar
Gerwick, BC, Subramanian, MV, Loney-Gallant, VI, Chandler, DP (1990) Mechanism of action of the 1, 2, 4-triazolo [1,5-a] pyrimidines. Pestic Sci 29:357–364CrossRefGoogle Scholar
Han, HP, Yu, Q, Purba, E, Li, M, Walsh, M, Friesen, S, Powles, SB (2012) A novel amino acid substitution Ala-122-Tyr in ALS confers high-level and broad resistance across ALS-inhibiting herbicides. Pest Manag Sci 68:1164–1170CrossRefGoogle ScholarPubMed
Heap, I (2019) The International Survey of Herbicide Resistant Weeds. http://www.weedscience.org. Accessed: July 27, 2019Google Scholar
Holm, LG, Plucknett, DL, Pancho, JV, Herberger, JP (1977) The World’s Worst Weeds: Distribution and Biology. Honolulu: University Press of Hawaii. 609 pGoogle Scholar
Huang, ZF, Chen, JY, Zhang, CX, Huang, HJ, Wei, SH, Zhou, XX, Chen, JC, Wang, X (2016) Target-site basis for resistance to imazethapyr in redroot amaranth (Amaranthus retroflexus L.). Pestic Biochem Physiol 128:10–15CrossRefGoogle Scholar
Huang, ZF, Sui, BF, Zhang, CX, Huang, HJ, We, SH (2019) The basis of resistance mechanism to mesosulfuron-methyl in Tausch’s goatgrass (Aegilops tauschii Coss.). Pestic Biochem Physiol 155:126–131CrossRefGoogle Scholar
Kaloumenos, NS, Dordas, CA, Diamantidis, GC, Eleftherohorinos, IG (2009) Multiple Pro197 substitutions in the acetolactate synthase of corn poppy (Papaver rhoeas) confer resistance to tribenuron. Weed Sci 57:362–368CrossRefGoogle Scholar
Li, J, Li, M, Gao, XX, Fang, F (2017) A novel amino acid substitution Trp574Arg in acetolactate synthase (ALS) confers broad resistance to ALS-inhibiting herbicides in crabgrass (Digitaria sanguinalis). Pest Manag Sci 73:2538–2543CrossRefGoogle Scholar
Liu, WT, Bi, YL, Li, LX, Yuan, GH, Wang, JX (2013) Molecular basis of resistance to tribenuron in water starwort (Myosoton aquaticum) populations from China. Weed Sci 61:390–395CrossRefGoogle Scholar
Lonhienne, T, Garcia, MD, Pierens, G, Mobli, M, Nouwens, A, Guddat, LW (2018) Structural insights into the mechanism of inhibition of AHAS by herbicides. Proc Natl Acad Sci USA 115:1945–1954CrossRefGoogle ScholarPubMed
Mazur, BJ, Falco, SC (1989) The development of herbicide resistant crops. Annu Rev Plant Biol 40:441–470CrossRefGoogle Scholar
McCourt, JA, Pang, SS, King-Scott, J, Guddat, LW, Duggleby, R (2006) Herbicide-binding sites revealed in the structure of plant acetohydroxyacid synthase. Proc Natl Acad Sci USA 103:569–573CrossRefGoogle ScholarPubMed
McNaughton, KE, Letarte, J, Lee, EA, Tardif, FJ (2005) Mutations in ALS confer herbicide resistance in redroot pigweed (Amaranthus retroflexus) and Powell amaranth (Amaranthus powellii). Weed Sci 53:17–22Google Scholar
Milliman, LD, Riechers, DE, Wax, LM, Simmons, FW (2003) Characterization of two biotypes of imidazolinone-resistant eastern black nightshade (Solanum ptychanthum). Weed Sci 51:139–144CrossRefGoogle Scholar
Riar, DS, Norsworthy, JK, Srivastava, V, Nandula, V, Bond, JA, Scott, RC (2013) Physiological and molecular basis of acetolactate synthase-inhibiting herbicide resistance in barnyardgrass (Echinochloa crus-galli). J Agric Food Chem 61:278–289CrossRefGoogle Scholar
Santel, HJ, Bowden, BA, Sorensen, VM, Mueller, KH, Reynolds, J (1999) Flucarbazone-sodium: a new herbicide for grass control in wheat. Weed Sci Soc Am Abstr 39:7Google Scholar
Seefeldt, SS, Jensen, JE, Fuerst, EP (1995) Log-logistic analysis of herbicide dose-response relationships. Weed Technol 9:218–227CrossRefGoogle Scholar
Shaner, DL, Anderson, PC, Stidham, MA (1984) Imidazolinones: potential inhibitors of acetohydroxyacid synthase. Plant Physiol 76:545–546CrossRefGoogle Scholar
Singh, S, Singh, V, Salas-Perez, RA, Bagavathiannan, MV, Lawton-Rauh, A, Roma-Burgos, N (2019) Target-site mutation accumulation among ALS inhibitor-resistant Palmer amaranth. Pest Manag Sci 75:1131–1139Google ScholarPubMed
Stidham, MA (1991) Herbicides that inhibit acetohydroxyacid synthase. Weed Sci 39:428–434CrossRefGoogle Scholar
Thiel, H, Varrelmann, M (2014) Identification of a new PSII target site psbA mutation leading to D1 amino acid Leu218Val exchange in the Chenopodium album D1 protein and comparison to cross-resistance profiles of known modifications at positions 251 and 264. Pest Manag Sci 70:278–285CrossRefGoogle Scholar
Tranel, PJ, Wright, TR (2002) Resistance of weeds to ALS-inhibiting herbicides: what have we learned? Weed Sci 50:700–712CrossRefGoogle Scholar
Tranel, PJ, Wright, TR, Heap, IM (2019) Mutations in Herbicide-Resistant Weeds to ALS Inhibitors. http://www.weedscience.org. Accessed: July 27, 2019Google Scholar
Trucco, F, Tatum, T, Rayburn, AL, Tranel, PJ (2009) Out of the swamp: unidirectional hybridization with weedy species may explain the prevalence of Amaranthus tuberculatus as a weed. New Phytol 184:819–827CrossRefGoogle ScholarPubMed
Umbarger, HE (1978) Amino acid biosynthesis and its regulation. Annu Rev Biochem 47:533–606CrossRefGoogle ScholarPubMed
Yu, Q, Frisesen, LSS, Zhang, XQ, Powles, SB (2004) Tolerance to acetolactate synthase and acetyl-coenzyme A carboxylase inhibiting herbicides in Vulpia bromoidesis conferred by two co-existing resistance mechanisms. Pestic Biochem Physiol 78:21–30CrossRefGoogle Scholar
Yu, Q, Han, HP, Vila-Aiub, MM, Powles, SB (2010) AHAS herbicide resistance endowing mutations: effect on AHAS functionality and plant growth. J Exp Bot 61:3925–3934CrossRefGoogle ScholarPubMed
Yu, Q, Nelson, J, Zheng, MQ, Jackson, M, Powles, SB (2007) Molecular characterization of resistance to AHAS-inhibiting herbicides in Hordeum leporinum biotypes. Pest Manag Sci 63:918–928CrossRefGoogle Scholar
Yu, Q, Powles, SB (2014) Resistance to AHAS inhibitor herbicides: current understanding. Pest Manag Sci 70:1340–1350CrossRefGoogle ScholarPubMed