CROWN DAISY (Chrysanthemum coronarium) with GROUP B/2 resistance: (INHIBITION OF ACETOLACTATE SYNTHASE ) Inhibition of Acetolactate Synthase
MUTATION: PROLINE 197 to THREONINE
Crown daisy (Chrysanthemum coronarium) is a dicot plant in the asteraceae family. A single amino acid substitution from Proline 197 to Threonine has led to resistance to Inhibition of Acetolactate Synthase as indicated in the table below.		Crown daisy

Chemical Family	Example Herbicide	Resistance Level
Imidazolinones	Imazethapyr	Intermediate Resistance < 10 fold
Pyrimidinyl benzoates	Bispyribac-Na	Resistant > 10 fold
Sulfonylureas	Chlorsulfuron	Resistant > 10 fold
Triazolopyrimidine - Type 1	Chloransulam-methyl	Intermediate Resistance < 10 fold
Triazolinones	Flucarbazone-Na	Resistant > 10 fold

NOTE

Resistance to flumetsulam (a TP) was reported as ">4"

REFERENCES

Tal, A. ; Rubin, B.. 2004. Occurrence of resistant Chrysanthemum coronarium to ALS inhibiting herbicides in Israel. Resistant Pest Management Newsletter 13 : 31 - 33.

A greenhouse experiment was conducted on C. coronarium cultivars Gilat and Beeri to determine the resistance of C. coronarium, on both whole plant and enzyme levels, to herbicides, i.e. sulfonylureas (SU), imidazolinones, triazolopyrimidines, pyrimidinylthiobenzoates and sulfonylaminocarbonyltriazolinones. In a related experiment to identify the differences in the nucleotide and amino acid sequences of acetolactate synthase (ALS) between the resistant (R) and susceptible (S) biotypes. Dose-response experiments at the whole plant level have revealed that the R biotype from Gilat was highly resistant to tribenuron (>792-fold) relative to the susceptible wild-type. Other SU herbicides such as iodosulfuron, chlorsulfuron and sulfometuron have also exhibited R/S>100. However, moderate and variable resistance (4- to 48-fold) to herbicides from other ALS-inhibiting groups, i.e. imazethapyr, flumetsulam, pyrithiobac-Na and propoxycarbone-Na. The results confirm that resistance to ALS inhibiting herbicides in C. coronarium is due to an alteration in the target site (ALS) and associated with the substitutions in the proline197 to the ALS gene..

This case was entered by Patrick Tranel Email: tranel@illinois.edu

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