The pectinolytic enzyme pectin methylesterase (PME) hydrolyses pectin in methanol and polygalacturonic acid. In the expressed sequence tag library of Botrytis cinerea T4, we identified a 1,041 bp Bcpme1 cDNA potentially encoding a 346-amino acid protein of 37 kDa showing 46.8% identity with Aspergillus sp. PMEs. Bcpme1 is a single copy gene and is similarly expressed in glucose and pectin containing media. To evaluate the role of Bcpme1 in Botrytis cinerea virulence, a mutant in Bcpme1 was generated by gene disruption. The Bcpme1 mutant showed similar growth on rich medium but reduced growth on pectin medium. Two isozymes of pI 7.4 and 7.1 were detected in pectin liquid-culture supernatants of wild-type strain Bd90 analyzed by isoelectric focusing-polyacrylamide gel electrophoresis, while those of Bcpme1 mutant possessed only the pI 7.1 isozyme. BCPME1, the pI 7.4 isozyme, is the major PME activity, as PME activity is 75% reduced in Bcpme1 mutant. Moreover, the Bcpme1 mutant was less virulent on apple fruits, grapevine, and Arabidopsis thaliana leaves. Those phenotypes were complemented by reintroducing a Bcpme1 copy in the Bcpme1 mutant. These results showed that B. cinerea possessed more than one PME-encoding gene and that BCPME1 is an important determinant of B. cinerea virulence.
Innovation toward ecofriendly plant protection products compatible with sustainable agriculture and healthy food is today strongly encouraged. Here, we assessed the biocontrol activity of three cyclic lipopeptides from Bacillus subtilis (mycosubtilin, M; surfactin, S; fengycin, F) and two mixtures (M + S and M + S + F) on wheat against Zymoseptoria tritici, the main pathogen on this crop. Foliar application of these biomolecules at a 100-mg L concentration on the wheat cultivars Dinosor and Alixan, 2 days before fungal inoculation, provided significant reductions of disease severity. The best protection levels were recorded with the M-containing formulations (up to 82% disease reduction with M + S on Dinosor), while S and F treatments resulted in lower but significant disease reductions. In vitro and in planta investigations revealed that M-based formulations inhibit fungal growth, with half-maximal inhibitory concentrations of 1.4 mg L for both M and M + S and 4.5 mg L for M + S + F, thus revealing that the observed efficacy of these products may rely mainly on antifungal property. By contrast, S and F had no direct activity on the pathogen, hence suggesting that these lipopeptides act on wheat against Z. tritici as resistance inducers rather than as biofungicides. This study highlighted the efficacy of several lipopeptides from B. subtilis to biocontrol Z. tritici through likely distinct and biomolecule-dependent modes of action.
Summary• Reduction in the degree of powdery mildew infection of wheat leaves is observed after treatments with trehalose, a nonreducing disaccharide commonly found in a wide variety of organisms, including fungi.• Wheat ( Triticum aestivum ) cv. Sideral plants grown in phytotrons were inoculated with Blumeria graminis f.sp. tritici . In addition to degree of infection, the effect of trehalose solution was further investigated using light and fluorescence microscopy and enzyme assays.• Infection in wheat leaves was reduced by 50 and 95% with trehalose solution (15 g l − 1 ) following a single spraying and three sprayings, respectively; in a detached leaf assay, trehalose was effective at concentrations as low as 0.01 g l − 1 . Trehalose did not inhibit conidial germination and differentiation of appressoria ( in vitro or on the leaf epidermis), but enhanced papilla deposition in epidermal cells. Trehalose also enhanced phenylalanine ammonia-lyase (PAL) and peroxidase (PO) activities; both markers of plant defence responses. However, the level of three cinnamyl alcohol dehydrogenase (CAD) activities (conyferyl, p -coumaryl and sinapyl alcohol dehydrogenase) was unchanged.• Trehalose treatment of wheat confers resistance to B. graminis infection by activating plant defence responses (e.g. papilla deposition, PAL and PO activities).
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