The Polygalacturonase-Inhibiting Protein PGIP2 of <i>Phaseolus vulgaris</i> Has Evolved a Mixed Mode of Inhibition of Endopolygalacturonase PG1 of <i>Botrytis cinerea</i>

Sicilia, Francesca; Fernández‐Recio, Juan; Caprari, Claudio; Lorenzo, Giulia De; Tsernoglou, Demetrius; Cervone, Felice; Federici, L.

doi:10.1104/pp.105.067546

Cited by 59 publications

(86 citation statements)

References 51 publications

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“…The crystal structure of F. moniliforme FmPG1 showed that this protein has two additional loops that form a lid over the active site, causing the substrate-binding cleft to become narrower [28]. This lid is absent in other PGs, such as B. cinerea BcPG1 [29 ], and may have evolved to prevent binding of substrate-mimicking inhibitors.…”

Section: Wheat Inhibitor Xip-i Targets Fungal Gh11 and Gh10 Xylanasesmentioning

confidence: 99%

“…However, predicting interactions between PG and PGIPs is not straightforward since PGIPs appear to bind PGs in different orientations [30 ]. PvPGIP2 is a competitive inhibitor of FmPG1 but it inhibits BcPG1 in a noncompetitively mixed mode, allowing the substrate to bind with reduced affinity and reduced kinetics of hydrolysis [29 ]. Docking studies of PvPGIP2 with a model of BcPG1 indicates that PvPGIP2 binds BcPG1 in a different orientation, allowing the substrate to interact (Figure 2f) [29 ].…”

Section: Detailed Analysis Of the Pgs Of Fusarium And Beanmentioning

confidence: 99%

“…PvPGIP2 is a competitive inhibitor of FmPG1 but it inhibits BcPG1 in a noncompetitively mixed mode, allowing the substrate to bind with reduced affinity and reduced kinetics of hydrolysis [29 ]. Docking studies of PvPGIP2 with a model of BcPG1 indicates that PvPGIP2 binds BcPG1 in a different orientation, allowing the substrate to interact (Figure 2f) [29 ]. This model indicates that a single PGIP can be versatile in binding and inhibiting their targets in different orientations.…”

Section: Detailed Analysis Of the Pgs Of Fusarium And Beanmentioning

confidence: 99%

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Enzyme–inhibitor interactions at the plant–pathogen interface

Misas-Villamil

Hoorn

2008

Current Opinion in Plant Biology

115

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The plant apoplast during plant-pathogen interactions is an ancient battleground that holds an intriguing range of attacking enzymes and counteracting inhibitors. Examples are pathogen xylanases and polygalacturonases that are inhibited by plant proteins like TAXI, XIP, and PGIP; and plant glucanases and proteases, which are targeted by pathogen proteins such as GIP1, EPI1, EPIC2B, and AVR2. These seven well-characterized inhibitors have different modes of action and many probably evolved from inactive enzymes themselves. Detailed studies of the structures, sequence variation, and mutated proteins uncovered molecular struggles between these enzymes and their inhibitors, resulting in positive selection for variant residues at the contact surface, where single residues determine the outcome of the interaction. Introduction Extracellular plant-pathogen interactions probably existed long before the evolution of pathogen effector translocation systems and plant resistance (R) genes. The molecular basis of these interactions is mostly undiscovered but some have been investigated in detail and reveal intriguing mechanisms. Here we will highlight major recent findings of extracellular enzyme-inhibitor interactions at the plant-pathogen interface.Although extracellular plant-pathogen interactions are complex, they can be simplified by assuming that they evolved in several stages (Figure 1). First, micro-organisms became pathogens by attacking plants using cell-wall-degrading enzymes and other hydrolases ( Figure 1A). In response to this attack, plants secrete inhibitors that suppress these hydrolases ( Figure 1B). Initially, these inhibitors were probably constitutively produced, but upon evolution of pathogen recognition systems the production and secretion of these proteins became inducible, becoming part of the arsenal of pathogenesis-related (PR) proteins. Besides suppression of pathogen attack, counter attack mechanisms also evolved in plants through the induced secretion of hydrolytic enzymes ( Figure 1C). Examples are the well-studied PR proteins including endo-b-1,3-glucanases (PR-2), chitinases (PR-3), and proteases (PR-7) [1 ]. Pathogens, in turn, responded to this counter attack by producing inhibitors that suppress these enzymes ( Figure 1D). The fifth and latest step was a sophisticated refinement of the pathogen recognition system by the evolution of R genes that recognize the manipulation of plant targets by pathogens, inducing a severe defense response that includes cell death ( Figure 1E). Aspects of this simplified model are consistent with the 'zigzag' model for the plant immune system, which explains the suppression of basal defense responses by pathogen effector proteins, followed by the evolution of efficient effector recognition by R proteins [2].Antagonistic interactions between organisms at the molecular level result in enzymes that evade inhibition, and inhibitors that adapt to these new enzymes. These 'molecular struggles' result in positive selection for variation of residues at the interactio...

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Section: Wheat Inhibitor Xip-i Targets Fungal Gh11 and Gh10 Xylanasesmentioning

confidence: 99%

Section: Detailed Analysis Of the Pgs Of Fusarium And Beanmentioning

confidence: 99%

Section: Detailed Analysis Of the Pgs Of Fusarium And Beanmentioning

confidence: 99%

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Enzyme–inhibitor interactions at the plant–pathogen interface

Misas-Villamil

Hoorn

2008

Current Opinion in Plant Biology

115

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“…In some cases a single PGIP isoform inhibits different PGs with a different mechanism, i.e. competitive, noncompetitive, and/or mixed (King et al, 2002;Sicilia et al, 2005;Bonivento et al, 2008). Genes encoding PGIPs are under selective pressure for diversification and a number of hot spots for the interaction with PGs have been identified on the inhibitor concave surface and validated by site-directed mutagenesis (Casasoli et al, 2009).…”

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confidence: 99%

Structural Resolution of the Complex between a Fungal Polygalacturonase and a Plant Polygalacturonase-Inhibiting Protein by Small-Angle X-Ray Scattering

et al. 2011

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We report here the low-resolution structure of the complex formed by the endo-polygalacturonase from Fusarium phyllophilum and one of the polygalacturonase-inhibiting protein from Phaseolus vulgaris after chemical cross-linking as determined by small-angle x-ray scattering analysis. The inhibitor engages its concave surface of the leucine-rich repeat domain with the enzyme. Both sides of the enzyme active site cleft interact with the inhibitor, accounting for the competitive mechanism of inhibition observed. The structure is in agreement with previous site-directed mutagenesis data and has been further validated with structure-guided mutations and subsequent assay of the inhibitory activity. The structure of the complex may help the design of inhibitors with improved or new recognition capabilities to be used for crop protection.

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“…Moreover, a single PGIP is often capable of inhibiting different fungal PGs with different mechanisms: for example PGIP2 from Phaseolus vulgaris (PvPGIP2) inhibits Fusarium moniliforme PG (FmPG), Aspergillus niger PGII (AnPGII), and Botrytis cinerea PG1 with a competitive, noncompetitive and mixed mode of action, respectively. [10][11][12] We have determined the crystal structure of a PG from the phytopathogenic fungus Colletotrichum lupini (CluPG1), the causal agent of lupin anthracnose. Moreover we have characterized its enzymatic activity, analyzed the inhibition mode exerted by PvPGIP2 on the enzyme and compared our data with those on AnPGII and FmPG, whose 3D structures and inhibition kinetics are already known.…”

Section: Introductionmentioning

confidence: 99%