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  • 1. Parrish, Jason Investigations into Multiple–Herbicide-Resistant Ambrosia artemisiifolia (Common Ragweed) in Ohio and Glyphosate-Resistance Mechanisms

    Doctor of Philosophy, The Ohio State University, 2015, Horticulture and Crop Science

    Common ragweed (Ambrosia artemisiifolia) is a weed problem in many places throughout the world. Though it seldom dominates the landscape, common ragweed seems to be able to exploit diverse habitats. Common ragweed is primarily outcrossing and has a high rate of gene polymorphisms, leading to high genetic diversity. This high level of genetic diversity likely plays a major role in the evolution of herbicide-resistant biotypes. Whole-plant bioassays of herbicide dose-response in the greenhouse were used to characterize resistance levels to glyphosate, cloransulam-methyl, and fomesafen herbicides. Additional studies were conducted to provide insight into potential mechanisms that may contribute to the development of resistance to glyphosate in an Ohio ragweed biotype, including 5 enolpyruvylshikimate-3-phosphate synthase (EPSPS) gene sequencing, quantitative PCR of the EPSPS gene, EPSPS enzyme immunoblot and activity/inhibition assays, 31P nuclear magnetic resonance (NMR) studies of glyphosate-treated tissues, and whole-plant absorption and translocation studies using 14C-labeled glyphosate. A single common ragweed population from Clinton County, Ohio exhibited multiple resistance to herbicides at dosages that exceeded the rate required to kill herbicide-sensitive common ragweed biotypes from 4- to 30 fold for glyphosate, > 1000 fold for cloransulam-methyl, and 14- to > 100 fold for fomesafen. This is the first report of a common ragweed biotype with multiple resistance to herbicides from three site-of-action (SOA) groups. Sequencing data indicated the gene coding for EPSPS has a high mutation rate in all studied common ragweed biotypes, but it typically does not code for an altered amino acid sequence in the glyphosate binding area. Additional studies identified alleles of EPSPS coding for proline-to-serine and proline-to-threonine substitutions at amino acid number 106 (based upon the mature maize EPSPS numbering scheme). Previous studies by other authors h (open full item for complete abstract)

    Committee: Mark Loux (Advisor); S. Kent Harrison (Committee Member); David Mackey (Committee Member); James Metzger (Committee Member); Anne Dorrance (Committee Member) Subjects: Agricultural Chemicals; Agriculture; Agronomy; Molecular Biology; Plant Biology