Effects of French Bean Tissue and Leaf Protoplasts on Colletotrichum lindemuthianum Polygalacturonase

Cervone, Felice; Andebrhan, T.; Coutts, Robert H.A.; Wood, R. K. S.

doi:10.1111/j.1439-0434.1981.tb03385.x

Cited by 17 publications

(2 citation statements)

References 17 publications

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“…Interestingly, though produced in vitro on media containing pectic substances or isolated hypocotyl cell walls, enrfo-polygalacturonase was not detectable in vivo during biotrophic or necrotrophic disease development (Wijesundera et al, 1989). This may be due to the presence in bean {P. vulgaris) cell walls of an inhibitor of this hydrolase (Cervone et al, 1981;Lafitte et al, 1984;Toubart et al, 1992). Biochemical studies have been confirmed by cytochemical experiments, in which endo-po\y-galacturonase was labelled by gold-conjugated polygalacturonase-inhibiting protein, and pectin degradation was detected by probing with Aplysia gonad lectin (Benhamou et al, 1991).…”

Section: Enzyme Production During Differentiation Of Infection Hyphamentioning

confidence: 99%

Infection structures of fungal plant pathogens – a cytological and physiological evaluation

1993

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SUMMARY Many fungi differentiate specific infection structures in order to infect the host plant. The spore attaches to the host surface, the cuticle, and the germ tube may recognize suitable penetration sites, over which an appressorium is formed. Additional wall layers in appressoria of many fungi suggest that this structure supports increasing pressure during the penetration process. During appressorium formation, synthesis of polymer‐degrading enzymes is often initiated. Cutinases, cellulases and pectin‐degrading enzymes can be formed in a developmentally controlled or adaptive, i.e. substrate‐dependent, fashion. The penetration hypha develops below the appressorium. This hypha has a new wall structure and exhibits features which serve to breach the plant cell wall. However, at present it is not clear whether penetration hyphae arising from appressoria are more efficient in penetration or induce less damage than hyphae which penetrate without detectable special adaptations. The infection hypha differentiates within the host. During differentiation a characteristic set of enzymes is synthesized to enable successful establishment of the host‐pathogen relationship. If, as in most cases, multiple forms of cell wall‐degrading enzymes are formed by the pathogen, mutagenesis or deletion of a gene encoding one of these enzymes very often has no effect on pathogenicity or even virulence. Proof is missing very often that an enzyme is needed at the right time and at the right site of infection. Events occurring during differentiation of fungal infection structures are reviewed with special emphasis on Magnaporthe grisea, Colletotrichum spp., and rust fungi, and common features which may be of importance to the success of infection are discussed.

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Section: Enzyme Production During Differentiation Of Infection Hyphamentioning

confidence: 99%

Infection structures of fungal plant pathogens – a cytological and physiological evaluation

1993

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“…niger PG are similar to those of other fungal PGs (8). Nevertheless, the enzyme exhibited a specific activity considerably higher than those of PGs purified to homogeneity from phytopathogenic fungi that successfully attack and colonize living plants (7,10,29 …”

Section: Elicitation Of Necrosis In Vigna By Polygalacturonasementioning

confidence: 82%

Elicitation of Necrosis in Vigna unguiculata Walp. by Homogeneous Aspergillus niger Endo-Polygalacturonase and by α-d-Galacturonate Oligomers

Cervone¹,

Lorenzo²,

Degrà³

et al. 1987

Plant Physiol.

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Endo-polygalacturonase (PG) was purified from a commercial preparation of Aspergillus niger pectinase by means of carboxymethylcellulose chromatography, preparative isoelectric focusing, and gel permeation through Sephadex G-50. The enzyme was electrophoretically homogeneous and consisted of a single polypeptide chain with a molecular weight of 33,500. The enzyme exhibited a specific activity significantly higher than those of purified polygalacturonases from phytopathogenic fungi.Galacturonate oligomers with a degree of polymerization higher than four appeared quickly as products of the enzymic hydrolysis of Napolygalacturonate. The oligomers were later degraded to di-and monogalacturonate. The homogeneous enzyme and growing mycelium of Aspergillus niger separately elicited a necrotic response in cowpea (Vigna unguiculata Walp.) pods. Heat-inactivated PG and PG inactivated with specific antibodies did not elicit necrosis, suggesting that the catalytic activity of the enzyme is necessary for its function as an elicitor. The PG-released oligosaccharides from Vigna cell wall and the galacturonides with a degree of polymerization greater than four separately elicited necrosis, whereas di-and monogalacturonate did not.

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Polygalacturonase-Inhibiting Proteins (PGIPs): Their Role in Specificity and Defense against Pathogenic Fungi

Lorenzo¹,

Cervone²

1997

Plant-Microbe Interactions

144

195

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Effects of French Bean Tissue and Leaf Protoplasts on Colletotrichum lindemuthianum Polygalacturonase

Cited by 17 publications

References 17 publications

Infection structures of fungal plant pathogens – a cytological and physiological evaluation

Infection structures of fungal plant pathogens – a cytological and physiological evaluation

Elicitation of Necrosis in Vigna unguiculata Walp. by Homogeneous Aspergillus niger Endo-Polygalacturonase and by α-d-Galacturonate Oligomers

Polygalacturonase-Inhibiting Proteins (PGIPs): Their Role in Specificity and Defense against Pathogenic Fungi

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