Acetolactate Synthase-Inhibitor Resistance in Monochoria vaginalis (Burm. f.) C. Presl from Indonesia

• Published in: Plants (Basel) Vol. 11; no. 3; p. 400
• Main Authors: Widianto, Ryan, Kurniadie, Denny, Widayat, Dedi, Umiyati, Uum, Nasahi, Ceppy, Sari, Santika, Juraimi, Abdul Shukor, Kato-Noguchi, Hisashi
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 31.01.2022; MDPI
• Subjects: 2,4-D; Acetolactate synthase; Amino acids; Ammonium; Aquatic plants; Bensulfuron-methyl; Biosynthesis; Biotypes; Cell division; Crop production; DNA; Herbicide resistance; Herbicides; Inhibitors; Low resistance; Metabolism; Monochoria vaginalis; Mutation; Nucleotides; resistant spectrum; Rice fields; Sodium; Weeds; United States > US; China; Japan; Indonesia; resistant spectrum; herbicide resistance; Monochoria vaginalis; DNA; acetolactate synthase
• ISSN: 2223-7747; 2223-7747
• DOI: 10.3390/plants11030400

(Burm. f.) C. Presl, belonging to the family Pontederiaceae, is an aquatic herbaceous plant, native to temperate and tropical Asia. The species often occurs in paddy fields as a noxious weed in East Asia, and in the USA, and causes a significant reduction in rice production. The objective of the present research was the evaluation of the resistance levels of against three chemical groups of acetolactate synthase (ALS)-inhibitor herbicides and other two different groups of herbicides, and the investigation of the mutations in the gene of the resistant biotype of . Herbicide dose-response experiments showed that the resistant biotype of was highly resistant to bensulfuron-methyl, moderately resistant to bispyribac-sodium, had low resistance to penoxsulam and 2,4-D dimethyl ammonium, and was susceptible to sulfentrazone. The nucleotide sequences of the of resistant and susceptible biotypes showed 14 base substitutions, which caused two amino acid substitutions: Val-143-Ile and Val-148-Ile. It is the first report of the substitutions of amino acids Val-143-Ile and Val-148-Ile in ALS protein. Those mutations may give different resistance spectra against three ALS-inhibitor herbicides: bensulfuron-methyl, bispyribac-sodium, and penoxsulam. Further research is needed to elucidate the molecular basis of target-site resistance mechanisms such as the transformation of the gene of . It is also necessary to evaluate herbicide mixtures and/or the rotation of herbicide sites of action to control the resistant biotype of