Evidence that polygalacturonase is a virulence determinant in Erwinia carotovora

Lei, Shau-Ping; Lin, Hun-Chi; Heffernan, L; Wilcox, Gary

doi:10.1128/jb.164.2.831-835.1985

Cited by 49 publications

(15 citation statements)

References 17 publications

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“…carotovoru strain has been reported to contain more than one endopolygalacturonase activity, the peh genes cloned from several Erw. carotorora strains (Lei et al 1985;Zink and Chatterjce 1985;Plastow et al 1986;Roberts et al 1986;Willis er al. 1987;Hinton et ul.…”

Section: Discussionmentioning

confidence: 99%

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A note on the primary structure and expression of an Erwinia carotovora polygalacturonase‐encoding gene (peh1) in Escherichia coli and Saccharomyces cerevisiae

Laing

Pretorius

1993

Journal of Applied Bacteriology

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A 1209-base pair (bp) DNA fragment containing the endopolygalacturonase-encoding gene (peh1) from Erwinia carotovora subsp. carotovora was amplified by the polymerase chain reaction (PCR) technique and expressed in Escherichia coli. The nucleotide sequence of the PCR product was determined and found to be highly homologous to the primary structures of other polygalacturonase-encoding genes. The peh1 DNA fragment encoding the mature polygalacturonase was inserted between two different yeast expression-secretion cassettes and a yeast gene terminator, generating recombinant yeast-integrating shuttle plasmids pAMS10 and pAMS11. These YIp5-derived plasmids were transformed and stably integrated into the genome of a laboratory strain of Saccharomyces cerevisiae. Transcription initiation signals present in these expression-secretion cassettes were derived from the yeast alcohol dehydrogenase (ADC1P) or mating pheromone alpha-factor (MF alpha 1P) gene promoters. The transcription termination signals were derived from the yeast tryptophan synthase gene terminator (TRP5T). Secretion of polygalacturonase was directed by the signal sequence of the yeast mating pheromone alpha-factor (MF alpha 1S). Northern blot analysis revealed the presence of peh1 mRNA in the yeast transformants and a polypectate agarose test was used to monitor polygalacturonase production.

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Section: Discussionmentioning

confidence: 99%

“…Recently, peh genes have been cloned from several strains of Erm. carotovora into Escherichia coli (Lei et al 1985;Zink and Chatterjee 1985;Plastow et al 1986;Roberts et al 1986;Willis et al 1987;Hinton et al 1990;Saarilahti et al 1990). In two of these Erw.…”

Section: Introductionmentioning

confidence: 99%

A note on the primary structure and expression of an Erwinia carotovora polygalacturonase‐encoding gene (peh1) in Escherichia coli and Saccharomyces cerevisiae

Laing

Pretorius

1993

Journal of Applied Bacteriology

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“…Procedures for quantification of extracellular and intracellular enzymes were as described previously (Chatterjee et al, 1985;Lei et al, 1985;Liao, 1989;Lanham et al, 1991). A modified method of PECTINASE ACTMTY OF SPOILAGE BACTERIA.…”

Section: Preparation Of Extracellular and Intracellular Enzyme Samplesmentioning

confidence: 99%

“…Activity of PL was determined spectrophotometrically (Lei et al, 1985). An appropriate amount of supernatant fluid or cell extract was 176-JOURNAL OF FOOD SCIENCE-Volume 59, No.…”

Section: Pl Assaymentioning

confidence: 99%

Pectinase Activity of Vegetable Spoilage Bacteria in Modified Atmosphere

Hao

BRACKElT

1994

Journal of Food Science

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A modified atmosphere of 10% CO*, 5% O2 and 85% Nz was used to determine effects on pectinase activities of vegetable spoilage bacteria. Cultures of Erwinia carotovora, Pseudomonasji'uorescens, and Xanthomonas campesti, grown at 25°C in liquid medium held under the modified atmosphere were assayed for polygalacturonase and pectate lyase activities. Erwinia and Pseudomonas exhibited higher polygalacturonase and pectate lyase activities thanXanthomonas whether grown under modified atmosphere or air. In some cases, bacteria grown under air exhibited higher pectinase activity. In general modified atmosphere did not significantly reduce pectinase activities in any of the bacteria tested.

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“…Plant pathogens produce a variety of virulence factors including toxins, hormones and plant cell wall-degrading enzymes. Polygalacturonases (EC 3.2.1.15) are plant cell wall-degrading enzymes that are virulence factors for a number of bacterial and fungal plant pathogens, including Agrobacterium vitis, Pectobacterium carotovora, Xylella fastidiosa and Botrytis cinerea (Bishop et al, 1988;Lei et al, 1985;Roper et al, 2007). Polygalacturonases catalyse the random hydrolysis of 1,4-α-Dgalactosiduronic linkages in pectate and other galacturonans, which, in turn, provides the pathogen with nutrients and facilitates its movement within the infected plant by the degradation of pectic polymers, which are structural components of the plant cell wall (Collmer and Keen, 1986).…”

Section: Introductionmentioning

confidence: 99%

A phage display‐selected peptide inhibitor of Agrobacterium vitis polygalacturonase

Warren

Kasun

Leonard

et al. 2015

Molecular Plant Pathology

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Agrobacterium vitis, the causal agent of crown gall of grapevine, is a threat to viticulture worldwide. A major virulence factor of this pathogen is polygalacturonase, an enzyme that degrades pectin components of the xylem cell wall. A single gene encodes for the polygalacturonase gene. Disruption of the polygalacturonase gene results in a mutant that is less pathogenic and produces significantly fewer root lesions on grapevines. Thus, the identification of peptides or proteins that could inhibit the activity of polygalacturonase could be part of a strategy for the protection of plants against this pathogen. A phage-displayed combinatorial peptide library was used to isolate peptides with a high binding affinity to A. vitis polygalacturonase. These peptides showed sequence similarity to regions of Oryza sativa (EMS66324, Japonica) and Triticum urartu (NP_001054402, wild wheat) polygalacturonase-inhibiting proteins (PGIPs). Furthermore, these panning experiments identified a peptide, SVTIHHLGGGS, which was able to reduce A. vitis polygalacturonase activity by 35% in vitro. Truncation studies showed that the IHHL motif alone is sufficient to inhibit A. vitis polygalacturonase activity.

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Evidence that polygalacturonase is a virulence determinant in Erwinia carotovora

Cited by 49 publications

References 17 publications

A note on the primary structure and expression of an Erwinia carotovora polygalacturonase‐encoding gene (peh1) in Escherichia coli and Saccharomyces cerevisiae

A note on the primary structure and expression of an Erwinia carotovora polygalacturonase‐encoding gene (peh1) in Escherichia coli and Saccharomyces cerevisiae

Pectinase Activity of Vegetable Spoilage Bacteria in Modified Atmosphere

A phage display‐selected peptide inhibitor of Agrobacterium vitis polygalacturonase

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