Chitosan oligomers from Fusarium solani/pea interactions, chitinase/β-glucanase digestion of sporelings and from fungal wall chitin actively inhibit fungal growth and enhance disease resistance

Kendra, David F.; Christian, David A.; Hadwiger, Lee A.

doi:10.1016/0885-5765(89)90052-0

Cited by 158 publications

(79 citation statements)

References 26 publications

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“…lindemuthianum grown in culture markedly increases when the fungus develops in its host plant (unpublished results). This is in agreement with the reported involvement of chitosan fragments in plant defence (Kendra et al, 1989).…”

Section: Discussionsupporting

confidence: 83%

“…In some Zygomycetes, it has been demonstrated that chitosan derives from N-deacetylation of nascent chitin by chitin deacetylase (Araki & Ito, 1988;Trudel & Asselin, 1990). Exogenous chitosan and chitosan oligosaccharides from fungal cell walls can elicit various defence reactions in plants, including the synthesis and accumulation of callose (Kendra et al, 1989).…”

Section: Introductionmentioning

confidence: 99%

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Colloidal gold-complexed chitosanase: a new probe for ultrastructural localization of chitosan in fungi

Grenier

Benhamou

Asselin

1991

Journal of General Microbiology

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A chitosanase was purified from the intercellular fluid extract of chemically stressed barley (Hordeum vulgare) leaves. Purification was achieved by preparative PAGE involving separation under native conditions at pH 4.3 (Reisfeld system) followed by denaturing PAGE in the presence of SDS. One basic chitosanase with a molecular mass of 19 kDa could hydrolyse chitosan and glycol chitosan of crustacean origin in addition to fungal chitosan isolated after treatment of Mucor rnucedo cells with sodium hydroxide followed by extraction in acetic acid. This enzyme did not exhibit activity towards P-1,4-polymers such as chitin, cellulose or peptidoglycan (from Micrococcus luteus) after SDS-PAGE. The chitosanase was conjugated to colloidal gold at pH 9.5 and applied to fungal tissue sections or to isolated glycol chitosan, chitosan, cellulose or chitin. The chitosanase-gold complex reacted intensely with glycol chitosan and chitosan but did not bind to chitin or cellulose. The enzyme-gold complex also labelled chitosan isolated from M. rnucedo. However, it did not react with M. rnucedo cells in tissue sections. Labelling with the chitosanase-gold complex was easily detected over cell walls of Fusariurn oxysporurn f. sp. radicis-lycopersici spores and hyphae as well as over cell walls of Ophiostoma ulrni, Aspergillus niger and Colletotrichurn lindernuthianum. No binding was observed with Pythiurn ultirnum.

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Section: Discussionsupporting

confidence: 83%

Section: Introductionmentioning

confidence: 99%

Colloidal gold-complexed chitosanase: a new probe for ultrastructural localization of chitosan in fungi

Grenier

Benhamou

Asselin

1991

Journal of General Microbiology

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“…In the last two decades, applications of chitosan have been developed in many industries; chitosan has emerged as a new biomaterial for food, pharmaceutical, textile, and other industries, as well as for wastewater treatment (3,15,19). Recently, chitosan oligosaccharides have received growing attention because they perform a variety of biological activities, such as inhibiting the growth of bacteria and fungi (13,17,44,47), exerting antitumor activity (41,45), acting as immunopotentiating effectors (42,43), and eliciting pathogenesis-related proteins in higher plants (16). Chain length and DDA are considered the most important factors influencing the biological activities of chitosan oligosaccharides.…”

mentioning

confidence: 99%

Purification and Characterization of Chitosanase from Bacillus sp. Strain KCTC 0377BP and Its Application for the Production of Chitosan Oligosaccharides

Choi

Kim

Piao

et al. 2004

Appl Environ Microbiol

163

106

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For the enzymatic production of chitosan oligosaccharides from chitosan, a chitosanase-producing bacterium, Bacillus sp. strain KCTC 0377BP, was isolated from soil. The bacterium constitutively produced chitosanase in a culture medium without chitosan as an inducer. The production of chitosanase was increased from 1.2 U/ml in a minimal chitosan medium to 100 U/ml by optimizing the culture conditions. The chitosanase was purified from a culture supernatant by using CM-Toyopearl column chromatography and a Superose 12HR column for fast-performance liquid chromatography and was characterized according to its enzyme properties. The molecular mass of the enzyme was estimated to be 45 kDa by means of sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme demonstrated bifunctional chitosanase-glucanase activities, although it showed very low glucanase activity, with less than 3% of the chitosanase activity. Activity of the enzyme increased with an increase of the degrees of deacetylation (DDA) of the chitosan substrate. However, the enzyme still retained 72% of its relative activity toward the 39% DDA of chitosan, compared with the activity of the 94% DDA of chitosan. The enzyme produced chitosan oligosaccharides from chitosan, ranging mainly from chitotriose to chitooctaose. By controlling the reaction time and by monitoring the reaction products with gel filtration high-performance liquid chromatography, chitosan oligosaccharides with a desired oligosaccharide content and composition were obtained. In addition, the enzyme was efficiently used for the production of low-molecular-weight chitosan and highly acetylated chitosan oligosaccharides. A gene (csn45) encoding chitosanase was cloned, sequenced, and compared with other functionally related genes. The deduced amino acid sequence of csn45 was dissimilar to those of the classical chitosanase belonging to glycoside hydrolase family 46 but was similar to glucanases classified with glycoside hydrolase family 8.Chitosan is currently obtained by the deacetylation of chitin (poly-␤-1,4-D-N-acetylglucosamine) that has been extracted from an abundant source of shrimp or crab shells. Deacetylated chitosans are produced by treating chitin in a concentrated alkaline solution (50%, wt/vol) and boiling it for several hours (34). Chitosan is also found in nature; it is found in the cell walls of fungi of the class Zygomycetes, in the chlorophycean algae Chlorella sp. (26), and in insect cuticles (2). These natural chitosans are synthesized by the tandem action of chitin synthetase and chitin deacetylase, as shown for Mucor rouxii and Colletotrichum lindemuthianum (9). Both chemical and enzymatic procedures for chitosan production result in the incomplete deacetylation of chitin, which yields chitosans in the intermediate range of the degree of deacetylation (DDA). Consequently, chitosan can be considered as a partly deacetylated derivative of chitin; it must have diverse structures containing hetero-linkages of N-acetylglucosamine (GlcNAc)-glucosamine (GlcN) and Gl...

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“…The biotic elicitors in the pea system include intact spores of the bean pathogen, Fusarium solani f. sp. phaseoli (Fsph), as well as Fsph fungal components such as Chit (Kendra et al, 1989;Hadwiger et al, 1994;Hadwiger, 1999) and Fsph DNase, an endonuclease exuded from fungal mycelium (Gerhold et al, 1993;Hadwiger et al, 1995). Each of these biotic agents elicit disease resistance responses, including the activation of PR genes (Chang et al, 1992;Hadwiger et al, 1995).…”

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confidence: 99%

A Comparison of the Effects of DNA-Damaging Agents and Biotic Elicitors on the Induction of Plant Defense Genes, Nuclear Distortion, and Cell Death

2001

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Pea (Pisum sativum L. cv Alcan) endocarp tissue challenged with an incompatible fungal pathogen, Fusarium solani f. sp. phaseoli or fungal elicitors results in the induction of pathogenesis-related (PR) genes and the accumulation of pisatin, a phytoalexin. Essentially the same response occurs in pea tissue exposed to DNA-specific agents that crosslink or intercalate DNA. In this study, the effects of DNA-damaging agents were assessed relative to the inducible expression of several pea PR genes: phenylalanine ammonia lyase, chalcone synthase, and DRR206. Mitomycin C and actinomycin D mimicked the biotic elicitors in enhancing the expression of all three PR genes. The activities of these PR gene promoters, isolated from different plants, were evaluated heterologously in transgenic tobacco. It is remarkable that ␤-glucuronidase expression was induced when plants containing the heterologous phenylalanine ammonia lyase, chalcone synthase, and DRR206 promoter-␤-glucuronidase chimeric reporter genes were treated by DNA-damaging agents. Finally, cytological analyses indicated that many of these agents caused nuclear distortion and collapse of the treated pea cells. Yet we observed that cell death is not necessary for the induction of the PR gene promoters assessed in this study. Based on these observations and previously published results, we propose that DNA damage or the associated alteration of chromatin can signal the transcriptional activation of plant defense genes.

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Chitosan oligomers from Fusarium solani/pea interactions, chitinase/β-glucanase digestion of sporelings and from fungal wall chitin actively inhibit fungal growth and enhance disease resistance

Cited by 158 publications

References 26 publications

Colloidal gold-complexed chitosanase: a new probe for ultrastructural localization of chitosan in fungi

Colloidal gold-complexed chitosanase: a new probe for ultrastructural localization of chitosan in fungi

Purification and Characterization of Chitosanase from Bacillus sp. Strain KCTC 0377BP and Its Application for the Production of Chitosan Oligosaccharides

A Comparison of the Effects of DNA-Damaging Agents and Biotic Elicitors on the Induction of Plant Defense Genes, Nuclear Distortion, and Cell Death

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