What are the roles of chitinases in the growing fungus?

Gooday, Graham W.; Zhu, Wei-Yun; O'Donnell, Raymond W.

doi:10.1111/j.1574-6968.1992.tb05730.x

Cited by 72 publications

(8 citation statements)

References 29 publications

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“…Chitinases are digestive enzymes that break down glycosidic bonds in chitin. In fungi, chitinase has been to be shown to be involved in regulating degradation of cell walls, germination of spores, tip growth, branching of hyphae, detachment of spores, and autolysis of hyphae [28,29,30]. The present paper demonstrated the effect of citral on the chitinase activity of M. grisea (Figure 4).…”

Section: Resultssupporting

confidence: 50%

The Natural Product Citral Can Cause Significant Damage to the Hyphal Cell Walls of Magnaporthe grisea

Yin

et al. 2014

Molecules

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Abstract:In order to find a natural alternative to the synthetic fungicides currently used against the devastating rice blast fungus, Magnaporthe grisea, this study explored the antifungal potential of citral and its mechanism of action. It was found that citral not only inhibited hyphal growth of M. grisea, but also caused a series of marked hyphal morphological and structural alterations. Specifically, citral was tested for antifungal activity against M. grisea in vitro and was found to significantly inhibit colony development and mycelial growth with IC 50 and IC 90 values of 40.71 and 203.75 μg/mL, respectively. Furthermore, citral reduced spore germination and germ tube length in a concentration-dependent manner. Following exposure to citral, the hyphal cell surface became wrinkled with folds and cell breakage that were observed under scanning electron microscopy (SEM). There was damage to hyphal cell walls and membrane structures, loss of villous-like material outside of the cell wall, thinning of the cell wall, and discontinuities formed in the cell membrane following treatment based on transmission electron microscopy (TEM). This increase in chitinase activity both supports the morphological changes seen in the hyphae, and also suggests a mechanism of action. In conclusion, citral OPEN ACCESSMolecules 2014, 19 10280 has strong antifungal properties, and treatment with this compound is capable of causing significant damage to the hyphal cell walls of M. grisea.

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Section: Resultssupporting

confidence: 50%

The Natural Product Citral Can Cause Significant Damage to the Hyphal Cell Walls of Magnaporthe grisea

Yin

et al. 2014

Molecules

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“…Other extracellular proteins with different functionalities were also detected in glucose cultures. Some of them are probably involved in the metabolism of fungal carbohydrates, as an hexosaminidase [47]. For example, cellulase regulation in H. jecorina proceeds through deglycosylation catalyzed by glucosaminidases, which can modulate enzyme activity by this mechanism [48].…”

Section: Resultsmentioning

confidence: 99%

Differential β-glucosidase expression as a function of carbon source availability in Talaromyces amestolkiae: a genomic and proteomic approach

Eugenio

Méndez-Líter

Nieto-Domínguez

et al. 2017

Biotechnol Biofuels

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BackgroundGenomic and proteomic analysis are potent tools for metabolic characterization of microorganisms. Although cellulose usually triggers cellulase production in cellulolytic fungi, the secretion of the different enzymes involved in polymer conversion is subjected to different factors, depending on growth conditions. These enzymes are key factors in biomass exploitation for second generation bioethanol production. Although highly effective commercial cocktails are available, they are usually deficient for β-glucosidase activity, and genera like Penicillium and Talaromyces are being explored for its production.ResultsThis article presents the description of Talaromyces amestolkiae as a cellulase-producer fungus that secretes high levels of β-glucosidase. β-1,4-endoglucanase, exoglucanase, and β-glucosidase activities were quantified in the presence of different carbon sources. Although the two first activities were only induced with cellulosic substrates, β-glucosidase levels were similar in all carbon sources tested. Sequencing and analysis of the genome of this fungus revealed multiple genes encoding β-glucosidases. Extracellular proteome analysis showed different induction patterns. In all conditions assayed, glycosyl hydrolases were the most abundant proteins in the supernatants, albeit the ratio of the diverse enzymes from this family depended on the carbon source. At least two different β-glucosidases have been identified in this work: one is induced by cellulose and the other one is carbon source-independent. The crudes induced by Avicel and glucose were independently used as supplements for saccharification of slurry from acid-catalyzed steam-exploded wheat straw, obtaining the highest yields of fermentable glucose using crudes induced by cellulose.ConclusionsThe genome of T. amestolkiae contains several genes encoding β-glucosidases and the fungus secretes high levels of this activity, regardless of the carbon source availability, although its production is repressed by glucose. Two main different β-glucosidases have been identified from proteomic shotgun analysis. One of them is produced under different carbon sources, while the other is induced in cellulosic substrates and is a good supplement to Celluclast in saccharification of pretreated wheat straw.Electronic supplementary materialThe online version of this article (doi:10.1186/s13068-017-0844-7) contains supplementary material, which is available to authorized users.

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“…Such DNA fragments were not seen in the genomic DNA from the fungus. Indeed, chitinases constitute the main component of pathogenesis-related proteins involved in defense mechanisms against bacteria, fungi, and insects, widely spread throughout plant species [2,40].…”

Section: Evaluation Of Transgenic Tobacco For the Presence Of Transgementioning

confidence: 99%

Expression of a Chitinase Gene from Metarhizium anisopliae in Tobacco Plants Confers Resistance against Rhizoctonia solani

Kern

Maraschin

Endt

et al. 2009

Appl Biochem Biotechnol

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The chit1 gene from the entomopathogenic fungus Metarhizium anisopliae, encoding the endochitinase CHIT42, was placed under the control of the CaMV 35S promoter, and the resulting construct was transferred to tobacco. Seventeen kanamycin-resistant transgenic lines were recovered, and the presence of the transgene was confirmed by polymerase chain reactions and Southern blot hybridization. The number of chit1 copies was determined to be varying from one to four. Copy number had observable effects neither on plant growth nor development. Substantial heterogeneity concerning production of the recombinant chitinase, and both general and specific chitinolytic activities were detected in leaf extracts from primary transformants. The highest chitinase activities were found in plants harboring two copies of chit1 inserts at different loci. Progeny derived from self-pollination of the primary transgenics revealed a stable inheritance pattern, with transgene segregation following a mendelian dihybrid ratio. Two selected plants expressing high levels of CHIT42 were consistently resistant to the soilborne pathogen Rhizoctonia solani, suggesting a direct relationship between enzyme activity and reduction of foliar area affected by fungal lesions. To date, this is the first report of resistance to fungal attack in plants mediated by a recombinant chitinase from an entomopathogenic and acaricide fungus.

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What are the roles of chitinases in the growing fungus?

Cited by 72 publications

References 29 publications

The Natural Product Citral Can Cause Significant Damage to the Hyphal Cell Walls of Magnaporthe grisea

The Natural Product Citral Can Cause Significant Damage to the Hyphal Cell Walls of Magnaporthe grisea

Differential β-glucosidase expression as a function of carbon source availability in Talaromyces amestolkiae: a genomic and proteomic approach

Expression of a Chitinase Gene from Metarhizium anisopliae in Tobacco Plants Confers Resistance against Rhizoctonia solani

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