Variability in antifungal proteins in the grains of maize, sorghum and wheat

Darnetty,; Leslie, John F.; Muthukrishnan, Subbaratnam; Swegle, Mark; Vigers, Alison J.; Selitrennikoff, Claude P.

doi:10.1111/j.1399-3054.1993.tb05508.x

Cited by 28 publications

(29 citation statements)

References 31 publications

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“…The rationale includes evidence that glucan and chitin are structurally linked in the cell wall (5,9), so dual inhibition could produce an enhanced effect. Hydrolytic enzymes (e.g., chitinase and glucanase) inhibit fungi synergistically (2,11). Moreover, there is evidence that fungi may adapt to inhibition of synthesis of one wall component by compensatory production of another (19); this again leads to the theoretical expectation that hits on two targets could produce an enhanced effect.…”

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confidence: 99%

Drug Interaction Studies of a Glucan Synthase Inhibitor (LY 303366) and a Chitin Synthase Inhibitor (Nikkomycin Z) for Inhibition and Killing of Fungal Pathogens

Stevens

2000

Antimicrob Agents Chemother

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The interaction between inhibitors of components of the fungal cell wall, glucan and chitin, was studied in vitro with the respective synthase enzyme inhibitors LY 303366 and nikkomycin Z. With Aspergillus fumigatus synergy was noted for inhibition and killing, and synergistic activity was also noted for some isolates of other species presently regarded as difficult to treat.Because of the paucity of current antifungal drugs and targets (15), the development of new agents directed at novel targets is welcome. Particularly appealing are agents directed at fungus-specific targets, such as the cell wall. At present, two classes of cell wall inhibitors, glucan and chitin synthase inhibitors, are in development. Their spectra of activity have limitations; in particular, fungicidal activity against filamentous pathogens and agents of the endemic mycoses may be a gap for one or both of these classes. This is a preliminary survey of the interaction of these two classes against pathogens which represent problems in therapy, particularly Aspergillus spp. The rationale includes evidence that glucan and chitin are structurally linked in the cell wall (5, 9), so dual inhibition could produce an enhanced effect. Hydrolytic enzymes (e.g., chitinase and glucanase) inhibit fungi synergistically (2, 11). Moreover, there is evidence that fungi may adapt to inhibition of synthesis of one wall component by compensatory production of another (19); this again leads to the theoretical expectation that hits on two targets could produce an enhanced effect.(This study was presented in part at the International Conference on Chemotherapy, Sydney, Australia, 1997.) LY 303366 (LY) (D. A. Stevens, M. Martinez, and M. J. Devine, Abstr. 36th Intersci. Conf. Antimicrob. Agents Chemother., abstr. F46, 1996) was selected as a representative of the group of glucan synthase inhibitors, and nikkomycin Z (NZ) (6) was selected as the representative of chitin synthase inhibitors.Susceptibility testing was performed by broth macrodilution (twofold dilution) in a checkerboard design. The methodology has been extensively reported, providing the largest data set for Aspergillus tested by one method in one laboratory (3). The methods for inoculum preparation and for the determination of MIC and minimum fungicidal concentration (MFC) have been described in detail (16) for the organisms (randomly selected from our culture collection) studied here, with the exception of the Fusarium species, for which we employed the same methods as for other filamentous organisms. In brief, the end point for the MIC is the first clear tube and Ն96% killing is defined as the MFC end point. For Candida albicans, the National Committee for Clinical Laboratory Standards standard was used (12).Checkerboard drug interaction methodology, including the calculation of a fractional inhibitory concentration index (FICi) (4), has been detailed elsewhere (3, 17). In brief, an FICi of 1 represents an additive effect, an FICi of Ͼ2.0 demonstrates antagonism, and an FICi of Ͻ1.0 demonstrate...

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Drug Interaction Studies of a Glucan Synthase Inhibitor (LY 303366) and a Chitin Synthase Inhibitor (Nikkomycin Z) for Inhibition and Killing of Fungal Pathogens

Stevens

2000

Antimicrob Agents Chemother

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“…Again, all genotypes presented the same sequences. Previous reports of PR proteins in wheat, detected with different methods, included PWIR2 (REBMANN et al, 1991;CHEONG et al, 1997); Tal 18 (CRUZ-ORTEGA & OWNBY, 1993); one chitinase (PR3) and one β-glucanase (PR2) (DARNETTY et al, 1993); wheatwin1 and wheatwin2 (CARUSO et al, 1996); and TaPR1.1 and TaPR1.2 (MOLINA et al, 1999). Two wheat protein sequences at the Prosite data bank (http:// expasy.hcuge.ch/sprot/sprot-top.html), E13B (PR2) and IAAS (PR6) were also found.…”

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confidence: 99%

Pathogenesis-related proteins in Brazilian wheat genotypes: protein induction and partial gene sequencing

2003

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Leaves from 14 Brazilian genotypes of Triticum aestivum L. were treated with salicylic acid to induce pathogenesis-related (PR) proteins. Inter and intracellular extracts were then obtained and investigated through polyacrilamide gel electrophoresis. Seven bands were observed. Material related to two of them (of 40 and 24 kDa) occurred in intracellular spaces only. DNA from these same genotypes was then amplified through PCR using primers developed from three sequences encoding PR proteins, and compared with previously described sequences. The fragments presented homologies to PR groups 1, 3 (chitinases), and 5 (thaumatinlike). The PR3-like sequence also showed a site characteristic of PRs induced by ethylene and a portion without homology with previous sequences. No variation among genotypes were observed, either for protein extracts or DNA sequences.

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“…15 Sorghum seed antifungal proteins at 30 days after anthesis, including chitinase, were extracted, partially purified and eluted. The fractions containing chitinase were found to be inhibitory to spore germination of three fungi, ie Fusarium moniliforme.…”

Section: Discussionmentioning

confidence: 99%

Induction of chitinase in response to Aspergillus infection in sorghum (Sorghum bicolor (L) Moench)

Ratnavathi

Sashidhar

2004

J Sci Food Agric

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Chitinase is an antifungal protein which is induced in higher plants during infection and stress. In this paper the induction of chitinase activity in response to infection by Aspergillus parasiticus (NRRL 2999) in six sorghum (Sorghum bicolor (L) Moench) genotypes and its association with aflatoxin production were investigated. Chitinase was induced in all six genotypes (two each of red, yellow and white sorghum) when infected by A parasiticus (NRRL 2999). The induction of chitinase activity was highest in the white cultivars, followed by the yellow and red genotypes, compared with healthy grains. In the white cultivars the chitinase activity increased on the 6th and 9th days after infection and was fourto fivefold higher than in healthy grains. The total aflatoxin produced was lower in the red genotypes than in the yellow and white genotypes. The white genotypes showed maximum total aflatoxin production at 6 days after infection. The aflatoxins produced in the white genotypes were comparable to those in the red genotypes. There was a significant positive correlation between chitinase activity and aflatoxin production in red sorghum (r 2 = 0.600, p ≤ 0.001) and white sorghum (r 2 = 0.411, p ≤ 0.001). Maximum chitinase activity was observed on day 12 in all genotypes under healthy conditions.

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Variability in antifungal proteins in the grains of maize, sorghum and wheat

Cited by 28 publications

References 31 publications

Drug Interaction Studies of a Glucan Synthase Inhibitor (LY 303366) and a Chitin Synthase Inhibitor (Nikkomycin Z) for Inhibition and Killing of Fungal Pathogens

Drug Interaction Studies of a Glucan Synthase Inhibitor (LY 303366) and a Chitin Synthase Inhibitor (Nikkomycin Z) for Inhibition and Killing of Fungal Pathogens

Pathogenesis-related proteins in Brazilian wheat genotypes: protein induction and partial gene sequencing

Induction of chitinase in response to Aspergillus infection in sorghum (Sorghum bicolor (L) Moench)

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