An enzyme immunoassay of phaseolinone and its application in estimation of the amount of toxin in Macrophomina phaseolina-infected seeds

Article Abstract:

An enzyme immunoassay (ELISA) procedure for the detection and determination of phaseolinone levels was developed. Phaseolinone is an exotoxinproduced by Macrophomina phaseolina (Tassi) Gold which inhibits seed germination in a number of plants. The best results for ELISA was obtained at an antibody dilution of 1:2,000 in the coating buffer and an enzyme conjugate dilution of 1:1,000. The smallest amount of phaseolinone detected by the procedure was 5 picograms per well. Studies on seed germination inhibition showed a good correlation between the amount of phaseolinone detected and the degree of inhibition.

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Investigation of the sterol composition and azole resistance in field isolates of Septoria tritici

Article Abstract:

The S-27 field isolate of the fungal phytopathogen Septoria tritici has an azole-resistant phenotype due to reduced levels of azole. S-27 has isomers of ergosterol and ergosta-5,7-dienol. The response of S-27 to azole antifungal agent treatment is similar to that of other pathogenic fungi. The concentration of desmethyl sterols decreases and that of 14-alpha-methyl sterols increases after the treatment. This suggests that there is an inhibition of the P450-mediating sterol 14-alpha-demethylase. A decrease in ergosterol and an increase in nonutilizable sterols arrests the growth in S-27.

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A unique endoglucanase-encoding gene cloned from the phytopathogenic fungus Macrophomina phaseolina

Article Abstract:

The pathogenic fungus Macrophomina phaseolina contains a pathogen-specific gene (egl1) which produces an enzyme similar to its host plant's endoglucanase. This enzyme does not dissolve the host's cell wall but makes the cell wall loose so that the fungus can enter the cell. Egl1 is formed when the carbon source is carboxymethyl cellulose and is inhibited by the presence of glucose. The gene egl1 does not have a cellulose-binding domain and its nucleotide sequences and substrate specificity is different from that of other saprophytic enzymes.

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