Cellular Membranes, the Sites for the Antifungal Activity of the Herbicide Sethoxydim

• Published in: Pakistan journal of biological sciences Vol. 10; no. 15; pp. 2480 - 2484
• Main Authors: Pakdaman, B.S., Mohammadi, E., Sepehrifa, R., Pouriesa, M., Rahimi Far, M., Moradi, F., Modarres, S.A.M.
• Format: Journal Article
• Language: English
• Published: Pakistan 01.08.2007
• Subjects: Antifungal Agents - pharmacology; Ascomycota - cytology; Ascomycota - drug effects; Ascomycota - metabolism; Brassica napus; Brassica napus - microbiology; Cell Membrane - drug effects; Cyclohexanones - pharmacology; Herbicides - pharmacology; Hydrogen Peroxide - metabolism; Iran; Malondialdehyde; Oxidants - metabolism; Random Allocation; Sclerotinia sclerotiorum; Trichoderma - cytology; Trichoderma - metabolism
• ISSN: 1028-8880
• DOI: 10.3923/pjbs.2007.2480.2484

The fungicidal effect of sethoxydim on the canola (Brassica napus var. Olifera) white stem rot pathogen (Sclerotinia sclerotiorum) encouraged us to conduct a series of studies on the mechanism of the antifungal activity of this herbicide commonly applied in Iranian fields under canola cultivation. Present preliminary studies on the changes in the level of Malondialdehyde (MDA) as the main product generated through peroxidation of polyunsaturated fatty acids indicated the disintegration of the fungal bilayer of plasma membrane as the result of the herbicidal treatment. Also, it was demonstrated that the amount of hydrogen peroxide in the treated samples was higher than the control samples with no herbicidal treatment. Therefore, our present results confirm the disintegration of the plasma membrane as one of the mechanism for the antifungal impact of sethoxydim. As with weed plants, the phytotoxic impact of this herbicide has been attributed to the inhibition of the first enzyme in the lipid biosynthesis pathway, acetyl-CoA carboxylase, therefore, it would be very interesting to study on this subject and the relations between the sensitivity of different fungi and their DNA and protein sequences of acetyl-CoA carboxylase.