Cercospora beticola Toxins (X. Inhibition of Plasma Membrane H+-ATPase by Beticolin-1)

Simon-Plas, Françoise; Gomès, Éric; Milat, Marie‐Louise; Pugin, Alain; Blein, Jean‐Pierre

doi:10.1104/pp.111.3.773

Cited by 22 publications

(22 citation statements)

References 21 publications

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“…A similar interpretation was given for the fungal toxin beticolin-1, which displays two different types of H + -ATPase inhibition depending on the lipid environment of the enzyme (Simon-Plas et al 1996). This possible mechanism of action is supported by the following evidences: (i) In our conditions, FB 1 is able of interacting with the hydrophobic region of the membrane, as shown by the toxin-induced changes in membrane fluidity, and (ii) FB 1 can be inserted into liposome bilayers (Yin et al 1996b) and interacts with polar and non-polar regions of cholesterol and taurocholate in monomolecular films (Mahfoud et al 2002), thus one toxin molecule might also be inserted between two adjacent cholesterol molecules.…”

Section: Discussionmentioning

confidence: 56%

“…The DpH and Dw generated across the membrane are used to drive secondary transport of solutes and to facilitate cell elongation and stomata opening among other processes (Arango et al 2003). This enzyme is a target for several fungal toxins and elicitors, which either inhibit or stimulate its activity (Wevelsiep et al 1993;Marra et al 1996;Simon-Plas et al 1996;Xing et al 1996). In this work, we describe the effect of FB 1 on the plasma membrane H + -ATPase in vesicles isolated from maize embryos, an experimental system that precludes the action of the toxin on intracellular targets thus allowing to study its early effects on the plasma membrane.…”

Section: Introductionmentioning

confidence: 99%

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Fumonisin B1, a sphingoid toxin, is a potent inhibitor of the plasma membrane H+-ATPase

Gutiérrez-Nájera

Muñoz‐Clares

Palacios-Bahena

et al. 2005

Planta

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Fumonisin B(1) (FB(1)) is an amphipathic toxin produced by the pathogenic fungus Fusarium verticillioides which causes stem, root and ear rot in maize (Zea mays L.). In this work, we studied the action of FB(1) on the plasma membrane H(+)-ATPase (EC 3.6.1.34) from germinating maize embryos, and on the fluidity and lipid peroxidation of these membranes. In maize embryos the toxin at 40 microM inhibited root elongation by 50% and at 30 microM decreased medium acidification by about 80%. Irrespective of the presence and absence of FB(1), the H(+)-ATPase in plasma membrane vesicles exhibited non-hyperbolic saturation kinetics by ATPH-Mg, with Hill number of 0.67. Initial velocity studies revealed that FB(1) is a total uncompetitive inhibitor of this enzyme with an inhibition constant value of 17.5+/-1 microM. Thus FB(1) decreased V(max) and increased the apparent affinity of the enzyme for ATP-Mg to the same extent. Although FB(1) increased the fluidity at the hydrophobic region of the membrane, no correlation was found with its effect on enzyme activity, since both effects showed different FB(1)-concentration dependence. Peroxidation of membrane lipids was not affected by the toxin. Our results suggest that, under in vivo conditions, the plasma membrane H(+)-ATPase is a potentially important target of the toxin, as it is inhibited not only by FB(1) but also by its structural analogs, the sphingoid intermediates, which accumulate upon the inhibition of sphinganine N-acyltransferase by this toxin.

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Section: Discussionmentioning

confidence: 56%

Section: Introductionmentioning

confidence: 99%

Fumonisin B1, a sphingoid toxin, is a potent inhibitor of the plasma membrane H+-ATPase

Gutiérrez-Nájera

Muñoz‐Clares

Palacios-Bahena

et al. 2005

Planta

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“…In plant cells, beticolins have been found to induce loss of solutes, to depolarize transmembrane potential and to inhibit H ϩ extrusion and K ϩ uptake (Gapillout et al, 1996;Macri and Vianello, 1979). In plant microsomal vesicles and in purified plasma membranes, they have been shown to inhibit the ATP-dependent proton translocation (Macri et al, 1983;Simon-Plas et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

Magnesium ions promote assembly of channel‐like structures from beticolin 0, a non‐peptide fungal toxin purified from Cercospora beticola

et al. 1998

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SummaryBeticolins are toxins produced by the fungus Cercospora beticola. Using beticolin 0 (B0), we have produced a strong and Mg 2⍣ -dependent increase in the membrane conductance of Arabidopsis protoplasts and Xenopus oocytes. In protein-free artificial bilayers, discrete deflexions of current were observed (12 pS unitary conductance in symmetrical 100 mM KCl) in the presence of B0 (approximately 10 µM) and in the presence of nominal Mg 2⍣ . Addition of 50 µM Mg 2⍣ induced a macroscopic current which could be reversed to single channel current by chelating Mg 2⍣ with EDTA. Both unitary and macroscopic currents were ohmic. The increase in conductance of biological membranes triggered by B0 is therefore likely to originate from the ability of this toxin to organize itself into transmembrane pores in the presence of Mg 2⍣ . The pore is poorly selective, displaying permeability ratios P Cl /P K , P Na /P K and P Ca /P K close to 0.3, 0.65 and 0.4, respectively. Such channel-like activity could be involved in the deleterious biological activity of the toxin, by causing the collapse of ionic and electrical gradients through biological membranes together with Ca 2⍣ influx and scrambling of cellular signals.

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“…Cercosporin is a photosensitizing metabolite with host‐non‐specific toxicity (Daub & Ehrenshaft, 2000) that acts during pathogenesis (Shim & Dunkle, 2003; Choquer et al ., 2005): its toxic effects are the result of the production of active oxygen forms. Beticolins are also host‐non‐specific phytotoxins which have been associated with a broad range of cytotoxic effects (Simon‐Plas et al ., 1996; Goudet et al ., 2000).…”

Section: Introductionmentioning

confidence: 99%

Variability in aggressiveness, cultural characteristics, cercosporin production and fatty acid profile ofCercospora piaropi, a biocontrol agent of water hyacinth

2008

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The extent of variation in aggressiveness, growth and pigmentation in culture, phytotoxin production and fatty acid profile were determined in a population of 55 isolates of Cercospora piaropi , a fungus used as a biocontrol agent of the aquatic weed water hyacinth ( Eichhornia crassipes ). Besides differences in the colour of mycelium and diffusible pigments in culture, isolates of C. piaropi grown under standard conditions differed significantly in their ability to produce the phytotoxin cercosporin, as well as in aggressiveness and growth rate. A positive correlation existed between the ability of the isolates to produce cercosporin and their aggressiveness, and a negative correlation between growth rate and cercosporin production or growth rate and aggressiveness. Based on thin-layer chromatographic separation of extracts and comparison with beticolin-1, used as a standard, there was no evidence of production of beticolins. In discriminant analysis, fatty acid methyl ester (FAME) profiles had low resolution for differentiating populations among isolates of the fungus, and the level of resolution was influenced by the age of the colonies. Diffusible pigments in culture and cercosporin production are useful adjuncts to aggressiveness screening for choosing the most effective isolate of C. piaropi for biological control.

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Cercospora beticola Toxins (X. Inhibition of Plasma Membrane H+-ATPase by Beticolin-1)

Cited by 22 publications

References 21 publications

Fumonisin B1, a sphingoid toxin, is a potent inhibitor of the plasma membrane H+-ATPase

Fumonisin B1, a sphingoid toxin, is a potent inhibitor of the plasma membrane H+-ATPase

Magnesium ions promote assembly of channel‐like structures from beticolin 0, a non‐peptide fungal toxin purified from Cercospora beticola

Variability in aggressiveness, cultural characteristics, cercosporin production and fatty acid profile ofCercospora piaropi, a biocontrol agent of water hyacinth

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