Endo- and exopolygalacturonases of Ralstonia solanacearum are inhibited by polygalacturonase-inhibiting protein (PGIP) activity in tomato stem extracts

Schacht, Tanja; Unger, Christoph; Pich, Andreas; Wydra, Kerstin

doi:10.1016/j.plaphy.2011.02.001

Cited by 40 publications

(29 citation statements)

References 59 publications

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“…PGIPs from ‘Bartlett’ pear (Abu-Goukh et al , 1983) and orange (Barmore and Nguyen, 1985) retained significant activity at 60 °C. The latest study on PGIP isolated from tomato was found to retain partial inhibitory activity, even at 100 °C (Schacht et al , 2011). …”

Section: Resultsmentioning

confidence: 99%

Experimental and bioinformatic characterization of a recombinant polygalacturonase-inhibitor protein from pearl millet and its interaction with fungal polygalacturonases

Prabhu

Singh

Kolkenbrock

et al. 2014

Journal of Experimental Botany

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Section: Resultsmentioning

confidence: 99%

Experimental and bioinformatic characterization of a recombinant polygalacturonase-inhibitor protein from pearl millet and its interaction with fungal polygalacturonases

Prabhu

Singh

Kolkenbrock

et al. 2014

Journal of Experimental Botany

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“…However, recent studies have identified PGIP as a potentially important player also in plant defense against bacteria: PGIPs were seen to play a role in resistance of Chinese cabbage against P. carotovorum ssp. carotovorum (Hwang et al, 2010) and PGIPS from tomato where shown to inhibit PGs from Ralstonia solanacearum (Schacht et al, 2011). …”

Section: Oligogalacturonide Signalingmentioning

confidence: 99%

Pathogenicity of and plant immunity to soft rot pectobacteria

Davidsson¹,

Kariola²,

Niemi³

et al. 2013

Front. Plant Sci.

151

149

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Soft rot pectobacteria are broad host range enterobacterial pathogens that cause disease on a variety of plant species including the major crop potato. Pectobacteria are aggressive necrotrophs that harbor a large arsenal of plant cell wall-degrading enzymes as their primary virulence determinants. These enzymes together with additional virulence factors are employed to macerate the host tissue and promote host cell death to provide nutrients for the pathogens. In contrast to (hemi)biotrophs such as Pseudomonas, type III secretion systems (T3SS) and T3 effectors do not appear central to pathogenesis of pectobacteria. Indeed, recent genomic analysis of several Pectobacterium species including the emerging pathogen Pectobacterium wasabiae has shown that many strains lack the entire T3SS as well as the T3 effectors. Instead, this analysis has indicated the presence of novel virulence determinants. Resistance to broad host range pectobacteria is complex and does not appear to involve single resistance genes. Instead, activation of plant innate immunity systems including both SA (salicylic acid) and JA (jasmonic acid)/ET (ethylene)-mediated defenses appears to play a central role in attenuation of Pectobacterium virulence. These defenses are triggered by detection of pathogen-associated molecular patterns (PAMPs) or recognition of modified-self such as damage-associated molecular patterns (DAMPs) and result in enhancement of basal immunity (PAMP/DAMP-triggered immunity or pattern-triggered immunity, PTI). In particular plant cell wall fragments released by the action of the degradative enzymes secreted by pectobacteria are major players in enhanced immunity toward these pathogens. Most notably bacterial pectin-degrading enzymes release oligogalacturonide (OG) fragments recognized as DAMPs activating innate immune responses. Recent progress in understanding OG recognition and signaling allows novel genetic screens for OG-insensitive mutants and will provide new insights into plant defense strategies against necrotrophs such as pectobacteria.

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“…Previous studies on thermal tolerance of PGIPs have shown them to be thermostable. PGIPs isolated from orange retained considerable activity at 60 °C48, and that from tomato retained partial inhibitory activity at 100 °C49. In this study, GhPGIP1 inhibited VdPG1 effectively with an inhibition rate of 26.88–31.45% over a pH range of 4.2–4.8, and inhibited FovPG1 over a pH range of 8.0–9.0, with an inhibition rate of 23.79–29.61% (Fig.…”

Section: Discussionmentioning

confidence: 50%

Molecular evidence for the involvement of a polygalacturonase-inhibiting protein, GhPGIP1, in enhanced resistance to Verticillium and Fusarium wilts in cotton

Liu

Zhang

Sun

et al. 2017

Sci Rep

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Polygalacturonase-inhibiting protein (PGIP), belonging to a group of plant defence proteins, specifically inhibits endopolygalacturonases secreted by pathogens. Herein, we showed that purified GhPGIP1 is a functional inhibitor of Verticillium dahliae and Fusarium oxysporum f. sp. vasinfectum, the two fungal pathogens causing cotton wilt. Transcription of GhPGIP1 was increased in cotton upon infection, wounding, and treatment with defence hormone and H2O2. Resistance by GhPGIP1 was examined by its virus-induced gene silencing in cotton and overexpression in Arabidopsis. GhPGIP1-silenced cotton was highly susceptible to the infections. GhPGIP1 overexpression in transgenic Arabidopsis conferred resistance to the infection, accompanied by enhanced expression of pathogenesis-related proteins (PRs), isochorismate synthase 1 (ICS1), enhanced disease susceptibility 1 (EDS1), and phytoalexin-deficient 4 (PAD4) genes. Transmission electron microscopy revealed cell wall alteration and cell disintegration in plants inoculated with polygalacturonase (PGs), implying its role in damaging the cell wall. Docking studies showed that GhPGIP1 interacted strongly with C-terminal of V. dahliae PG1 (VdPG1) beyond the active site but weakly interacted with C-terminal of F. oxysporum f. sp. vasinfectum (FovPG1). These findings will contribute towards the understanding of the roles of PGIPs and in screening potential combat proteins with novel recognition specificities against evolving pathogenic factors for countering pathogen invasion.

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Endo- and exopolygalacturonases of Ralstonia solanacearum are inhibited by polygalacturonase-inhibiting protein (PGIP) activity in tomato stem extracts

Cited by 40 publications

References 59 publications

Experimental and bioinformatic characterization of a recombinant polygalacturonase-inhibitor protein from pearl millet and its interaction with fungal polygalacturonases

Experimental and bioinformatic characterization of a recombinant polygalacturonase-inhibitor protein from pearl millet and its interaction with fungal polygalacturonases

Pathogenicity of and plant immunity to soft rot pectobacteria

Molecular evidence for the involvement of a polygalacturonase-inhibiting protein, GhPGIP1, in enhanced resistance to Verticillium and Fusarium wilts in cotton

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