Natural Inhibitors of Fungal Polygalacturonases in Infected Fruit Tissues

Fielding, A. H.

doi:10.1099/00221287-123-2-377

Cited by 24 publications

(20 citation statements)

References 7 publications

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“…Cell walls of some plant tissues contain proteins (PGIP) that counteract cell wall-degrading microorganisms by inhibiting their PG activity (1-4, 6, 9-11, 21,22,24,25). Molecular Cannon-Fenske No.…”

mentioning

confidence: 99%

Purification and Characterization of a Polygalacturonase-Inhibiting Protein from Phaseolus vulgaris L.

Cervone¹,

Lorenzo²,

Degrà³

et al. 1987

Plant Physiol.

132

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Homogeneous endo-polygalacturonase (PG) was covalently bound to cyanogen-bromide-activated Sepharose, and the resulting PG-Sepharose conjugate was utilized to purify, by affinity chromatography, a protein from Phaseolus vulgaris hypocotyls that binds to and inhibits PG. Isoelectric focusing of the purified PG-inhibiting protein (PGIP) showed a major protein band that coincided with PG-inhibiting activity. PGIP formed a complex with PG at pH 5.0 and at low salt concentrations. The complex dissociated in 0.5 M Na-acetate and pH values lower than 4.5 or higher than 6.0. Formation of the PG-PGIP complex resulted in complete inhibition of PG activity. PG activity was restored upon dissociation of the complex. The protein exhibited inhibitory activity toward PGs from Colktotrichum lindemuthianum, Fusarium moniliforme and Aspergillus niger. The possible role of PGIP in regulating the activity of fungal PG's and their ability to elicit plant defense reactions are discussed.

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mentioning

confidence: 99%

Purification and Characterization of a Polygalacturonase-Inhibiting Protein from Phaseolus vulgaris L.

Cervone¹,

Lorenzo²,

Degrà³

et al. 1987

Plant Physiol.

132

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“…This is consistent with most of the known plant PGIPs which fall in this range with monocot wheat PGIP being 40.3 kDa (Kemp et al, 2003) and cotton PGIP is 34 kDa (James and Dubery, 2001). In addition, protein bands lower than 20 kDa and higher than 43 kDa were also observed in the 2 peak lanes which could also be putative PGIPs as occasionally some plant species have shown the presence of PGIPs with molecular weights of 15 kDa in peach (Fielding, 1981) and 91 kDa in pear (Abu-Goukh et al, 1983). Hence further purification of pearl millet PGIPs to homogeneity will be crucial in determining the actual inhibitory protein.…”

Section: Discussionmentioning

confidence: 97%

“…The PGIPs from orange (Barmore and Nguyen, 1985), bean (Cervone et al, 1987) and guava (Deo and Shastri, 2003) were found be active at 60°C. The peach PGIP was stable at 80°C (Fielding, 1981), whereas PGIP of chilli stable at 50°C retained some residual inhibitory activity even at 90°C (Shivshanker et al, 2010).…”

Section: Discussionmentioning

confidence: 99%

Partial purification and characterization of polygalacturonase-inhibitor proteins from pearl millet

Prabhu

Kini²,

Shetty³

2012

Afr. J. Biotechnol.

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Polygalacturonase-inhibitor proteins (PGIPs) are plant cell wall glycoproteins, involved in the inhibition of microbial endo-polygalacturonases (EPGs). The present study involved activity guided partial purification of pearl millet [Pennisetum glaucum (L.) R.Br.] protein extract by cation exchange chromatography, which resulted in two pooled protein peaks -Peak-A and Peak-B, both of which showed inhibitory activity against the Aspergillus niger EPG. Protein separation of the two peaks by gel electrophoresis showed prominent bands between 29 and 43 kDa, consistent with the molecular weights of the known plant PGIPs. The two PGIP peaks were further studied for their inhibitory activities with respect to three parameters viz., inhibitor concentration, pH and temperature effects. Enzyme inhibition was partial and increased with inhibitor concentration. The Peak-B was found to be the more active inhibitor of the two. The results indicate the presence of at least two isoforms of PGIP in pearl millet. This is the first such study to be undertaken in understanding the presence of the PGIPs in millets.

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“…Pectin-lyase (PL) was measured in the culture filtrates according to the thiobarbituric acid method (Fielding, 1981). The absorbance was read using Camspec M330 (UV/visible) spectrophotometer at 550 nm and PL activity and was expressed as arbitrary units over a particular period at 27±2°C.…”

Section: Pectin-lyase Assaysmentioning

confidence: 99%

“…After incubation for three days at 27±2° C under natural light and dark conditions, tissues were excised from the necrotic sites along with healthy margins (Fielding, 1981) and 3 g were ground in a chilled mortar in 30 ml of 100 mM Tris-HCl buffer (pH 7.6) containing cystein hydrochloride (10 mg l -1 ) and 1 M NaCl. The suspension was kept for 1 h at 4º C and the extract was filtered through a few layers of muslin and centrifuged 5 min at 2000 g. Enzyme activities of the supernatant were assayed as described below.…”

Section: Enzyme Sample Preparation From P Meadiiinfected Petiole Tismentioning

confidence: 99%

Effect of rubber petiole cell walls and virulence of strains on secretion of pectic enzymes by <i>Pytophthora meadii</i>

Jayasuriya

Wijesundera

Thennakoon

2009

Ceylon J. Sci. (Biol. Sci.)

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The characteristics of the pectic enzyme polygalacturonase (PG) of Phytophthora meadii isolates from petioles of rubber (Hevea brasiliensis) genotypes were compared in relation to (i) aggressiveness (virulence) in infecting detached petioles of a susceptible rubber genotype (PB86) or (ii) in relation to the availability of purified rubber petiole cell walls (obtained from a Phytophthora-resistant clone, RRIC100) in the growth medium, as the sole carbon source. The four most highly aggressive isolates produced PG forms varying within mw 48-60 kDa, while, the highly aggressive MAD86 isolate produced two PG forms of mw 48 and 70 kDa. Moderately or weakly aggressive isolates produced PG forms within the range of 62-66 kDa. With rubber petiole cell walls in the growth medium, the four most highly aggressive isolates produced PG forms of mw 42-62 kDa, while, MAD86 produced a much smaller PG form of 21 kDa. Weak or moderately aggressive isolates produced similar PG forms in both cell wall and pectin media. Quite smaller PG molecules produced in rubber cell wall medium could be due to elicitor molecular fragments bound to rubber cell walls, which may induce P. meadii to secret specific PG forms via signal transduction pathway. None of the isolates produced pectin lyase (PL) in any growth medium. Neither PG nor PL activity was detected in P. meadii-infected petioles.

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Natural Inhibitors of Fungal Polygalacturonases in Infected Fruit Tissues

Cited by 24 publications

References 7 publications

Purification and Characterization of a Polygalacturonase-Inhibiting Protein from Phaseolus vulgaris L.

Purification and Characterization of a Polygalacturonase-Inhibiting Protein from Phaseolus vulgaris L.

Partial purification and characterization of polygalacturonase-inhibitor proteins from pearl millet

Effect of rubber petiole cell walls and virulence of strains on secretion of pectic enzymes by <i>Pytophthora meadii</i>

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