Co-operative action by endo- and exo-β-(1→3)-glucanases from parasitic fungi in the degradation of cell-wall glucans of <i>Sclerotinia sclerotiorum</i> (Lib.) de Bary

Jones, David W.; Gordon, Alex H.; Bacon, J. S. D.

doi:10.1042/bj1400047

Cited by 83 publications

(47 citation statements)

References 19 publications

(23 reference statements)

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“…Synergistic effects between fungal cell wall hydrolases have previously been reported; a cooperative action by several exo-and endo-␤-1,3-glucanases during the degradation of cell wall glucans of Sclerotinia sclerotiorum by T. viride has been suggested (21). In order to demonstrate this result in our system, combinations of the purified ␤-1,6-glucanase-II with other cell wall-degrading enzymes were made and the release of reducing sugars and the clearing activity on different fungal cell walls were assayed.…”

Section: Discussionmentioning

confidence: 95%

Purification and characterization of an endo-beta-1,6-glucanase from Trichoderma harzianum that is related to its mycoparasitism

et al. 1995

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The enzymes from Trichoderma species that degrade fungal cell walls have been suggested to play an important role in mycoparasitic action against fungal plant pathogens. The mycoparasite Trichoderma harzianum produces at least two extracellular ␤-1,6-glucanases, among other hydrolases, when it is grown on chitin as the sole carbon source. One of these extracellular enzymes was purified to homogeneity after adsorption to its substrate, pustulan, chromatofocusing, and, finally, gel filtration. The apparent molecular mass was 43,000, and the isoelectric point was 5.8. The first 15 amino acids from the N terminus of the purified protein have been sequenced. The enzyme was specific for ␤-1,6 linkages and showed an endolytic mode of action on pustulan. Further characterization indicated that the enzyme by itself releases soluble sugars and produces hydrolytic halli on yeast cell walls. When combined with other T. harzianum cell wall-degrading enzymes such as ␤-1,3-glucanases and chitinases, it hydrolyzes filamentous fungal cell walls. The enzyme acts cooperatively with the latter enzymes, inhibiting the growth of the fungi tested. Antibodies against the purified protein also indicated that the two identified ␤-1,6-glucanases are not immunologically related and are probably encoded by two different genes.

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Section: Discussionmentioning

confidence: 95%

Purification and characterization of an endo-beta-1,6-glucanase from Trichoderma harzianum that is related to its mycoparasitism

et al. 1995

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“…Their nutritional function is evident by the extracellular degradation of 1,3-/?-glucans serving as carbon sources (Bamforth, 1980;Stahmann et al, 1992). Parasitic fungi may use them for degradation of the host cell wall (Jones et al, 1973;Bodenmann et al, 1984). Their involvement in fungal cell wall formation during hyphal tip growth, as tightly balanced antagonists of glucan synthase, is controversial (Bartnicki-Garcia, 1968Wessels, 1988).…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of four extracellular 1,3- -glucanases of Botrytis cinerea

Stahmann

Schimz

Sahm

1993

Journal of General Microbiology

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~ ~~~The filamentous fungus Botvytis cinerea was found to produce four 1,3+glucanases (Glu I, II, 111, IV), These enzymes were visualized by activity-staining after separation by native polyacrylamide gel electrophoresis (PAGE). During growth on glucose as the single carbon source, only Glu III was detectable in the culture supernatant of B. cinerea. After glucose was exhausted from the medium, the extracellular (1,3)( 1,6)-/%~-glucan (cinerean) capsule of the fungus was degraded. In this phase the other three enzymes became detectable and the amount of all four enzymes increased. The enzyme with the greatest activity was Glu II, which was purified to homogeneity by SDS-PAGE. Its M, was 75000 and its isoelectric point (PI) was 5.2. Glycosylation of Glu I1 was shown by the periodic acid/Schiff reaction after SDS-PAGE. Glu I1 cleaved cinerean and laminarin. Both substrates were degraded in an exo-manner as shown by product characterization, and by studying the viscosity decrease in comparison with the liberation of reducing groups. The concentration of substrate that gave halfmaximal velocity (Se5) for Glu II was 580 pg ml-' for cinerean and 152 pg ml-' for laminarin. For Glu 111, also purified to homogeneity by SDS-PAGE, an M, of 84 000 and a PI of 3-6 were determined. Glu III cleaved laminarin (So.5 119 pg ml-') but not cinerean. Glu I and Glu IV were purified by activity-stained native PAGE. Both enzymes cleaved cinerean and laminarin in an exo-manner. Glu I focused at PI 4.9; its Se5 was 275 pg ml-' with cinerean and 138 pg ml-' with laminarin. The PI of Glu IV was 3.4; its So.5 was 171 pg ml-' for cinerean and 27 pg ml-' for lamina rin.

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“…However, information on the cell wall-degrading hydrolases of C. minitans is sparse. Although earlier studies (23) showed the presence of two synergistically interacting glucanases in the culture filtrate of this fungus, no data on the physicochemical properties, inducibility, and genetic background of these enzymes have been available.…”

Section: Discussionmentioning

confidence: 91%

“…According to Philips and Price (43), penetration is achieved merely by physical pressure exerted by the mycoparasite. However, other workers have claimed that penetration is facilitated by the production of cell wall-degrading enzymes by the fungus (21,23).…”

Section: Coniothyrium Minitansmentioning

confidence: 99%

Expression of cmg1 , an Exo-β-1,3-Glucanase Gene from Coniothyrium minitans , Increases during Sclerotial Parasitism

Giczey

Kerényi

Fülöp

et al. 2001

Appl Environ Microbiol

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During sclerotial infection of Sclerotinia sclerotiorum the mycoparasite Coniothyrium minitans penetrates through the host cell wall, which contains ␤-1,3-glucan as its major component. A PCR-based strategy was used to clone a ␤-1,3-glucanase-encoding gene, designated cmg1, from a cDNA library of the fungus. The nucleotide and deduced amino acid sequences of this gene showed high levels of similarity to the sequences of other fungal exo-␤-1,3-glucanase genes. The calculated molecular mass of the deduced protein (without the predicted 24-amino-acid N-terminal secretion signal peptide) was 83,346 Da, and the estimated pI was 4.73. Saccharomyces cerevisiae INVSc1 expressing the cmg1 gene secreted a ϳ100-kDa ␤-1,3-glucanase enzyme (as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis) into the culture medium. N-terminal sequence analysis of the purified recombinant enzyme revealed that the secreted enzyme starts at Ala-32, seven amino acids downstream from the predicted signal peptidase cleavage site. The purified recombinant glucanase inhibited in vitro mycelial growth of S. sclerotiorum by 35 and 85% at concentrations of 300 and 600 g ml ؊1 , respectively. A single copy of the cmg1 gene is present in the genome of C. minitans. Northern analyses indicated increases in the transcript levels of cmg1 due to both carbon starvation and the presence of ground sclerotia of S. sclerotiorum; only slight repression was observed in the presence of 2% glucose. Expression of cmg1 increased during parasitic interaction with S. sclerotiorum.

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Co-operative action by endo- and exo-β-(1→3)-glucanases from parasitic fungi in the degradation of cell-wall glucans of Sclerotinia sclerotiorum (Lib.) de Bary

Cited by 83 publications

References 19 publications

Purification and characterization of an endo-beta-1,6-glucanase from Trichoderma harzianum that is related to its mycoparasitism

Purification and characterization of an endo-beta-1,6-glucanase from Trichoderma harzianum that is related to its mycoparasitism

Purification and characterization of four extracellular 1,3- -glucanases of Botrytis cinerea

Expression of cmg1 , an Exo-β-1,3-Glucanase Gene from Coniothyrium minitans , Increases during Sclerotial Parasitism

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