Proteins from Plant Cell Walls Inhibit Polygalacturonases Secreted by Plant Pathogens

Albersheim, Peter; Anderson, Anne J.

doi:10.1073/pnas.68.8.1815

Cited by 203 publications

(72 citation statements)

References 27 publications

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“…Selected protease inhibitors were ineffective in inhibiting PGIP activity (Table II). All these results strongly suggested that the PGIP we have purified is likely to be the same protein characterized by other authors (3,28).…”

supporting

confidence: 62%

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

Cervone¹,

Lorenzo²,

Degrà³

et al. 1987

Plant Physiol.

131

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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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supporting

confidence: 62%

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

Cervone¹,

Lorenzo²,

Degrà³

et al. 1987

Plant Physiol.

131

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“…between 10 and 15 are potent elicitors of plant defense responses, but are only transiently produced by the action of EPG in vitro. A polygalacturonase-inhibiting protein (PGIP) has been found to be present in the cell walls of all dicotyledonous plants that have been examined (Albersheim and Anderson, 1971;Cervone et a/., 1986;. In vjtro experiments have demonstrated that addition of PGlP to fungal EPG in the presence of polygalacturonic acid results in the prolonged existence in the reaction mixture of elicitor-active oligogalacturonides (d.p.s.…”

Section: Introductionmentioning

confidence: 99%

Polygalacturonase‐inhibiting protein accumulates in Phaseolus vulgaris L. in response to wounding, elicitors and fungal infection

et al. 1994

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Summary Polygalacturonase‐inhibiting protein (PGIP) is a cell wall‐associated protein that specifically binds to and inhibits the activity of fungal endopolygalacturonases. The Phaseolus vulgaris gene encoding PGIP has been cloned and characterized. Using a fragment of the cloned pgip gene as a probe in Northern blot experiments, it is demonstrated that the pgip mRNA accumulates in suspension‐cultured bean cells following addition of elicitor‐active oligogalacturonides or fungal glucan to the medium. Rabbit polyclonal antibodies specific for PGIP were generated against a synthetic peptide designed from the N‐terminal region of PGIP; the antigenicity of the peptide was enhanced by coupling to KLH. Using the antibodies and the cloned pgip gene fragment as probes in Western and Northern blot experiments, respectively, it is shown that the levels of PGIP and its mRNA are increased in P. vulgaris hypocotyls in response to wounding or treatment with salicylic acid. Using gold‐labeled goat‐anti‐rabbit secondary antibodies in EM studies, it has also been demonstrated that, in bean hypocotyls infected with Colletotrichum lindemuthianum, the level of PGIP preferentially increases in those cells immediately surrounding the infection site. The data support the hypothesis that synthesis of PGIP constitutes an active defense mechanism of plants that is elicited by signal molecules known to induce plant defense genes.

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“…To do so, fungal and bacterial pathogens are armed with a deconstructing mixture of enzymes that depolymerize polysaccharides in the plant cell wall (1). At the same time, plants can secrete proteins that inhibit these degradative glycosidases, including polygalacturonase-inhibitor proteins (2), pectin lyase inhibitor proteins (3), and two different classes of endoxylanase inhibitors (4,5).…”

mentioning

confidence: 99%

Structural Basis for Inhibition of Aspergillus niger Xylanase by Triticum aestivum Xylanase Inhibitor-I

Sansen

Ranter

Gebruers

et al. 2004

Journal of Biological Chemistry

118

132

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Plants developed a diverse battery of defense mechanisms in response to continual challenges by a broad spectrum of pathogenic microorganisms. Their defense arsenal includes inhibitors of cell wall-degrading enzymes, which hinder a possible invasion and colonization by antagonists. The structure of Triticum aestivum xylanase inhibitor-I (TAXI-I), a first member of potent TAXI-type inhibitors of fungal and bacterial family 11 xylanases, has been determined to 1.7-Å resolution. Surprisingly, TAXI-I displays structural homology with the pepsin-like family of aspartic proteases but is proteolytically nonfunctional, because one or more residues of the essential catalytical triad are absent. The structure of the TAXI-I⅐Aspergillus niger xylanase I complex, at a resolution of 1.8 Å, illustrates the ability of tight binding and inhibition with subnanomolar affinity and indicates the importance of the C-terminal end for the differences in xylanase specificity among different TAXI-type inhibitors.

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Proteins from Plant Cell Walls Inhibit Polygalacturonases Secreted by Plant Pathogens

Cited by 203 publications

References 27 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.

Polygalacturonase‐inhibiting protein accumulates in Phaseolus vulgaris L. in response to wounding, elicitors and fungal infection

Structural Basis for Inhibition of Aspergillus niger Xylanase by Triticum aestivum Xylanase Inhibitor-I

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