Target‐site resistance to acetolactate synthase (ALS)‐inhibiting herbicides in Amaranthus palmeri from Argentina. Issue 12 (23rd August 2017)

• Record Type: Journal Article
• Authors: Larran, Alvaro S; Palmieri, Valeria E; Perotti, Valeria E; Lieber, Lucas; Tuesca, Daniel; Permingeat, Hugo R
• Is Part Of: Pest management science. Volume 73:Issue 12(2017)
• Page Start: 2578
• Page End: 2584
• Publication Date: 2017-08-23
• Subjects: weeds -- Amaranthus palmeri -- herbicide resistance -- acetolactate synthase -- acetolactate synthase inhibitors -- cross‐resistance; Pests -- Control -- Periodicals; Pesticides -- Periodicals; 632.9
• DOI: 10.1002/ps.4662
• Languages: English
• ISSNs: 1526-498X

Abstract

Abstract: BACKGROUND: Herbicide‐resistant weeds are a serious problem worldwide. Recently, two populations of Amaranthus palmeri with suspected cross‐resistance to acetolactate synthase (ALS)‐inhibiting herbicides (R1 and R2) were found by farmers in two locations in Argentina (Vicuña Mackenna and Totoras, respectively). We conducted studies to confirm and elucidate the mechanism of resistance. RESULTS: We performed in vivo dose–response assays, and confirmed that both populations had strong resistance to chlorimuron‐ethyl, diclosulam and imazethapyr when compared with a susceptible population (S). In vitro ALS activity inhibition tests only indicated considerable resistance to imazethapyr and chlorimuron‐ethyl, indicating that other non‐target mechanisms could be involved in diclosulam resistance. Subsequently, molecular analysis of als nucleotide sequences revealed three single base‐pair mutations producing substitutions in amino acids previously associated with resistance to ALS inhibitors, A122, W574, and S653. CONCLUSION: This is the first report of als resistance alleles in A. palmeri in Argentina. The data support the involvement of a target‐site mechanism of resistance to ALS‐inhibiting herbicides. © 2017 Society of Chemical Industry