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Resistance to ACCase-inhibiting herbicides in sprangletop (Leptochloa chinensis)

Published online by Cambridge University Press:  20 January 2017

Somsak Samanwong
Affiliation:
BayerCropScience(Thailand) Co. Ltd., 130/1 North Sathorn Road, Silom, Bangrak, Bangkok 10500, Thailand
Xiao-Qi Zhang
Affiliation:
Western Australian Herbicide Resistance Initiative, School of Plant Biology, University of Western Australia, Crawley, WA 6009, Australia
Stephen B. Powles
Affiliation:
Western Australian Herbicide Resistance Initiative, School of Plant Biology, University of Western Australia, Crawley, WA 6009, Australia

Abstract

This study reports evolved resistance to fenoxaprop-P in a population of sprangletop from a rice field in Thailand (BLC1). After eight applications of fenoxaprop-P, the herbicide appeared no longer effective. To confirm herbicide resistance in the BLC1 population, three experiments were conducted. First, glasshouse experiments revealed that the BLC1 population survived 600 g ai ha−1 of fenoxaprop-P without visual injury. Second, the BLC1 population was treated with fenoxaprop-P and other acetyl coenzyme A carboxylase (ACCase)–inhibiting herbicides (quizalofop-P, cyhalofop-butyl, and profoxydim) under field conditions; BLC1 exhibited resistance to all of these herbicides. Third, seeds of susceptible SLC1 and resistant BLC1 were germinated on 0.6% (v/v) agar across a range of herbicide concentrations. The resistant BLC1 population exhibited 61-, 44-, 9- and 8-fold resistance to fenoxaprop-P, cyhalofop, quizalofop-P, and profoxydim, respectively, compared with a susceptible SLC1 population. At the enzyme level, ACCase from the resistant BLC1 exhibited 30, 24, 11, 4, and 5 times resistance to fenoxaprop, cyhalofop-butyl, haloxyfop, clethodim, and cycloxydim, respectively. The spectrum of resistance at the whole plant level correlated well with resistance at the ACCase level. Hence, the mechanism of resistance to ACCase-inhibiting herbicides in this biotype of sprangletop is a herbicide-resistant ACCase. The specific mutation(s) of the ACCase gene that endows resistance in this population remains to be investigated.

Type
Physiology, Chemistry, and Biochemistry
Copyright
Copyright © Weed Science Society of America 

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References

Literature Cited

Boutsalis, P. 2001. Syngenta-test: a rapid whole-plant test for herbicide resistance. Weed Technol 15:257263.CrossRefGoogle Scholar
Brown, A. C., Moss, S. R., Wilson, Z. A., and Field, L. M. 2002). An isoleucine to leucine substitution in the ACCase of Alopecurus myosuroides (black-grass) is associated with resistance to the herbicide sethoxydim. Pestic. Biochem. Physiol 72:160168.CrossRefGoogle Scholar
Christoffers, M. J., Berg, M. L., and Messersmith, C. G. 2002. An isoleucine to leucine mutation in acetyl-CoA carboxylase confers herbicide resistance in wild oat. Genome 45:10491056.CrossRefGoogle ScholarPubMed
Cocker, K. M., Moss, S. R., and Coleman, J. O. D. 1999. Multiple mechanisms of resistance to fenoxaprop-P in United Kingdom and other European populations of herbicide-resistant Alopercurus myosuroides (Black-grass). Pestic. Biochem. Physiol 65:169180.CrossRefGoogle Scholar
Cocker, K. M., Northcroft, D. S., Coleman, J. O. D., and Moss, S. R. 2001. Resistance to ACCase-inhibiting herbicides and isoproturon in UK populations of Lolium multiflorum: mechanisms of resistance and implications for control. Pest Manag. Sci 57:587597.CrossRefGoogle ScholarPubMed
Delye, C., Wang, T., and Darmency, H. 2002. An isoleucine-leucine substitution in chloroplastic acetyl-Coo A carboxylase from green foxtail (Setaria viridis L Beauv.) is responsible for resistance to the cyclohexanedione herbicide sethoxydim. Planta 214:421427.CrossRefGoogle Scholar
Delye, C., Zhang, X. Q., Chalopin, C., Michel, S., and Powles, S. B. 2003. An isoleucine residue within the carboxyl-transferase domain of multidomain acetyl-Coenzyme A carboxylase is a major determinant of sensitivity to aryloxyphenoxypropionate inhibitors but not to cyclohexanedione inhibitors. Plant Physiol 132:18.CrossRefGoogle Scholar
Devine, M. D. and Shimabukuro, R. H. 1994. Resistance to acetyl coenzyme A carboxylase inhibiting herbicides. Pages 141169 in Powles, S. B. and Holtum, J.A.M. eds. Herbicide Resistance in Plants: Biochemistry and Biology. Boca Raton, FL: CRC Press.Google Scholar
Gronwald, J. D. 1991. Lipid biosynthesis inhibitors. Weed Sci 39:435449.CrossRefGoogle Scholar
Gronwald, J. W., Eberlein, C. V., Betts, K. J., Baerg, R. J., Ehlke, N. J., and Wyse, D. L. 1992. Mechanism of diclofop resistance in an Italian ryegrass (Lolium multiforum Lam.) biotype. Pestic. Biochem. Physiol 44:126139.CrossRefGoogle Scholar
Hall, L. M., Moss, S. R., and Powles, S. B. 1997. Mechanisms of resistance to aryloxyphenoxypropionate herbicides in two resistant biotypes of Alopecurus myosuroides: herbicide metabolism as a cross-resistance mechanism. Pestic. Biochem. Physiol 57:8798.CrossRefGoogle Scholar
Hidayat, I. and Preston, C. 1997. Enhanced metabolism of fluazifop acid in a biotype of Digitaria sanguinalis resistant to the herbicide fluazifop-P-butyl. Pestic. Biochem. Physiol 57:137146.CrossRefGoogle Scholar
Holtum, J. A. M., Matthews, J. M., Liljegren, D. R., and Powles, S. B. 1991. Cross-resistance to herbicides in annual ryegrass (Lolium rigidum). III. On the mechanism of resistance to diclofop-methyl. Plant Physiol 97:10261034.CrossRefGoogle ScholarPubMed
Ishikawa, H., Yamada, S., Hosaka, H., Kawana, T., Okunuki, S., and Kohara, K. 1985. Herbicidal properties of sethoxydim for the control of gramineous weeds. J. Pestic. Sci 10:187193.CrossRefGoogle Scholar
Kuk, Y., Wu, J., Derr, J. F., and Hatzois, K. K. 1999. Mechanism of fenoxaprop resistance in an accession of smooth crabgrass (Digitaria ischaemum). Pestic Biochem. Physiol 64:112123.CrossRefGoogle Scholar
Leach, G. E., Devine, M. D., Kirkwood, R. C., and Marshall, G. 1995. Target enzyme-based resistance to acetyl-coenzyme A carboxylase inhibitors in Eleusine indica . Pestic. Biochem. Physiol 51:129136.CrossRefGoogle Scholar
Maneechote, C., Holtum, J. A. M., Preston, C., and Powles, S. B. 1994. Resistant acteyl-CoA carboxylase is a mechanism of herbicide resistance in a biotype of Avena sterilis ssp. ludoviciana . Plant Cell Physiol 35:627635.CrossRefGoogle Scholar
Maneechote, C., Preston, C., and Powles, S. B. 1997. A diclofop-methyl-resistant Avena sterilis biotype with a herbicide–resistant acetyl-coenzyme A carboxylase and enhanced metabolism of diclofop-methyl. Pestic. Sci 28:105114.3.0.CO;2-3>CrossRefGoogle Scholar
Preston, C. and Powles, S. B. 1998. Amitrole inhibits diclofop metabolism and synergises diclofop-methyl in a diclofop-methyl-resistant biotype of Lolium rigidum . Pestic. Biochem. Physiol 62:179189.CrossRefGoogle Scholar
Seefeldt, S. S., Fuerst, E. P., Gealy, D. R., Shukla, A., Irzyk, G. P., and Devine, M. D. 1996. Mechanisms of resistance to diclofop of two wild oat (Avena fatua) biotypes from the Willamette Valley of Oregon. Weed Sci 44:776781.CrossRefGoogle Scholar
Shukla, A., Dupont, S., and Devine, M. D. 1997a. Resistance to ACCase-inhibitors herbicides in wild oat: evidence for target site-based resistance in two biotypes from Canada. Pestic. Biochem. Physiol 57:147155.CrossRefGoogle Scholar
Shukla, A., Leach, G. E., and Devine, M. D. 1997b. High level of resistance to sethoxydim conferred by an alteration in the target enzyme, acetyl CoA carboxylase, in Setaria faberi and Setaria viridis . Plant Physiol. Biochem 35:803807.Google Scholar
Swisher, B. A. and Corbin, F. T. 1982. Behavior of BAS-9052OH in soybean and johnsongrass plant and cell cultures. Weed Sci 30:640650.CrossRefGoogle Scholar
Tal, A., Zarka, S., and Rubin, B. 1996. Fenoxaprop-P resistance in Phalaris minor conferred by an insensitive acetyl-coenzyme A carboxylase. Pestic. Biochem. Physiol 56:134140.CrossRefGoogle Scholar
Tardif, F. J., Holtum, J. A. M., and Powles, S. B. 1993. Occurrence of a herbicide-resistant acetyl-coenzyme A carboxylase mutant in annual ryegrass (Lolium rigidum) selected by sethoxydim. Planta 190:176181.CrossRefGoogle Scholar
Yokohama, K., Kondo, K., Poolkumlung, P., and Zaprong, P. 2001. Herbicidal efficacy against Leptochloa chinensis of bis-pyribac-sodium in tank mixture with some rice herbicides. Pages 763769 in The Proceedings of 18th Asian-Pacific Weed Science Society Conference, Beijing, China: Beijing Grenadir Colour.Google Scholar
Zagnitko, O., Jelenska, J., Tevzadze, G., Haselkorn, R., and Gornicki, P. 2001. An isoleucine/leucine residue in the carboxyltransferase domain of acetyl-CoA carboxylase is critical for interaction with aryloxyphenoxypropionate and cyclohexanedion inhibitors. Proc. Natl. Acad. Sci. USA 98:66176622.CrossRefGoogle Scholar