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Molecular Features Affecting the Biological Activity of the Host-Selective Toxins from Cochliobolus victoriae
T J Wolpert1, V Macko, W Acklin
1Boyce Thompson Institute, Cornell University, Ithaca, New York 14853.
Abstract:
The structures of the toxins produced by Cochliobolus victoriae, victorin B, C, D, E, and victoricine, have recently been established. These toxins and modified forms of victorin C were tested for their effect on dark CO(2) fixation in susceptible oat (Avena sativa) leaf slices. Half-maximal inhibition of dark CO(2) fixation occurred with the native toxins in the range of 0.004 to 0.546 micromolar. An essential component for the inhibitory activity of victorin is the glyoxylic acid residue, particularly its hydrated aldehyde group. Removal of glyoxylic acid completely abolished the inhibitory activity of victorin, and the reduction of the aldehydo group transformed the toxin into a protectant. Conversion of victorin to its methyl ester resulted in diminution of inhibitory activity to 10% of the original activity of the toxin, whereas derivatization of the epsilon-amino group of the beta-hydroxylysine moiety resulted in a decrease of inhibitory activity to 1% of that of victorin C. However, the derivatized toxin retained its host selectivity. In addition, the opening of the macrocyclic ring of the toxin drastically reduced the inhibitory activity.
Insights
Victorin toxins from Cochliobolus victoriae inhibit CO2 fixation in oats. The glyoxylic acid residue is crucial for this activity, with modifications altering or abolishing the toxin's effect.
Area of Science:
- Plant Pathology
- Biochemistry
- Molecular Biology
Background:
- Cochliobolus victoriae produces victorin toxins that affect susceptible oat varieties.
- The precise molecular mechanisms underlying victorin's phytotoxicity are not fully understood.
Purpose of the Study:
- To elucidate the structure-activity relationship of victorin toxins.
- To identify key chemical moieties responsible for victorin's inhibitory effects on CO2 fixation.
Main Methods:
- Synthesis and modification of victorin toxins (B, C, D, E) and victoricine.
- Assaying the effect of native and modified toxins on dark CO2 fixation in susceptible oat (Avena sativa) leaf slices.
- Quantifying half-maximal inhibitory concentrations (IC50) for various toxin derivatives.
Main Results:
- Native victorins inhibited dark CO2 fixation at micromolar concentrations (0.004–0.546 μM).
- The glyoxylic acid residue, specifically its hydrated aldehyde group, is essential for inhibitory activity.
- Removal of glyoxylic acid abolished inhibition; reduction of the aldehyde group conferred a protective effect.
- Esterification or beta-hydroxylysine derivatization significantly reduced inhibitory activity (to 10% and 1%, respectively), but host selectivity was retained.
- Macrocyclic ring opening drastically reduced inhibitory activity.
Conclusions:
- The glyoxylic acid moiety and its aldehyde group are critical for victorin's phytotoxic activity.
- Specific chemical modifications can attenuate or abolish victorin's inhibitory effects while potentially retaining host selectivity.
- Understanding these structure-activity relationships provides insights into victorin's mode of action and potential for developing resistant crop varieties.
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