β-(1,3) glucanase activity and quantity of fungus in relation to Fusarium wilt in resistant and susceptible near-isogenic lines of muskmelon

Netzer, D.; Kritzman, G.; Chet, I.

doi:10.1016/0048-4059(79)90024-9

Cited by 50 publications

(10 citation statements)

References 18 publications

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“…melonis (Netzer and Kritzman, 1979). However, in these studies, it was not clear which isoform was involved, nor was it clear whether the enzymes were intra-or extracellularly located.…”

Section: Discussionmentioning

confidence: 71%

Mass Spectrometric Identification of Isoforms of PR Proteins in Xylem Sap of Fungus-Infected Tomato

et al. 2002

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The protein content of tomato (Lycopersicon esculentum) xylem sap was found to change dramatically upon infection with the vascular wilt fungus Fusarium oxysporum. Peptide mass fingerprinting and mass spectrometric sequencing were used to identify the most abundant proteins appearing during compatible or incompatible interactions. A new member of the PR-5 family was identified that accumulated early in both types of interaction. Other pathogenesis-related proteins appeared in compatible interactions only, concomitantly with disease development. This study demonstrates the feasibility of using proteomics for the identification of known and novel proteins in xylem sap, and provides insights into plant-pathogen interactions in vascular wilt diseases.

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“…melonis (Netzer and Kritzman, 1979). However, in these studies, it was not clear which isoform was involved, nor was it clear whether the enzymes were intra-or extracellularly located.…”

Section: Discussionmentioning

confidence: 71%

Mass Spectrometric Identification of Isoforms of PR Proteins in Xylem Sap of Fungus-Infected Tomato

et al. 2002

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“…Several authors have suggested that such enzymes may function as disease resistance factors by attacking the pathogen cell wall and inducing lysis or other inhibitory effects (12,14,15). Our results and those of Nichols et al (13) suggest that the role of plant carbohydrases may be more subtle and involve the release of elicitor-active carbohydrates from the cell surface of the pathogen.…”

Section: Discussionmentioning

confidence: 99%

β-1,3-Endoglucanase from Soybean Releases Elicitor-Active Carbohydrates from Fungus Cell Walls

Keen¹,

Yoshikawa²

1983

Plant Physiol.

246

110

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Cetavion Precipition Solid cetavlon (hexadecyl trimethylammonium bromide, Sigma) was added to the dialyzed, crude enzyme to give a 0.5% (w/v) concentration, and the mixture was stirred on an ice bath for 3 h. Following centrifugation for 10 mi at 15,000g, the supematant fluids were dialyzed against several changes of 3 mm Tris-HCI (pH 7. CM Blo-Gel Chromatography. The enzyme from DEAE-cellulose was adjusted to pH 5.0 with HCI and pumped through a 2.7-x 15-cm column of CM Bio-gel A (Bio-Rad) equilibrated with 3 mm K-acetate (pH 5.0). Following application of the enzyme (approximately 2,000 ml), the column was washed with 150 ml of acetate buffer and eluted with 350 ml of the buffer containing 0.1 N NaCl. Finally, the column was washed with 250 ml of acetate buffer containing 0.4 M NaCl before reequilibration and reuse.Electrofocusing. The CM fractionated enzyme was dialyzed against water and electrofocused using an LKB 8100 preparative column with pH 3 to 10 Ampholines (LKB) with sucrose as the density gradient medium. The cathode was at the top of the column and separations were performed at 400 v for 48 h at I°C. Gel Fltration. Dialyzed enzyme preparations from the CM Biogel or the electrofocusing column were concentrated in dialysis bags using Aquacide I (Calbiochem) and applied to 0.9-x 67-cm columns of Bio-gel P-150. For preparative work, enzyme from the CM Bio-gel column (1 kg of cotyledons) was applied in approximately 5 ml to a 2.5-x 83-cm column of Sephacryl S-300. All columns were equilibrated and eluted with 10 mm K-acetate (

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“…Plant disease resistance depends on the ability to tolerate a pathogenic agent or restrict its development (Netzer et al 1979). Since the plant cell wall represents the boundary interface with pathogens, one may expect that active defense reactions occur at the cell-surface level .…”

Section: Introductionmentioning

confidence: 99%

Time-course study of the accumulation of hydroxyproline-rich glycoproteins in root cells of susceptible and resistant tomato plants infected by Fusarium oxysporum f. sp. radicis-lycopersici

Benhamou

Mazau

Grenier

et al. 1991

Planta

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The accumulation of hydroxyproline-rich glycoproteins (HRGPs) in cell walls of dicotyledonous plants is thought to be involved in the defense response to pathogens. An antiserum raised against deglycosylated HRGPs from melon was used for studying the subcellular localization of these glycoproteins in susceptible and resistant tomato (Lycopersicon esculentum Mill.) root tissues infected by Fusarium oxysporum f.sp. radicis-lycopersici. A time-course of HRGP accumulation revealed that these glycoproteins increased earlier and to a higher extent in resistant than in susceptible cultivars. In the compatible interaction, increase in HRGPs was largely correlated with pathogen invasion and appeared to occur as a result of wall damage. In the incompatible interaction, HRGPs accumulated in the walls of uninvaded cells, thus indicating a possible role in the protection against fungal penetration. The occurrence of substantial amounts of HRGPs in papillae, known to be physical barriers formed in response to infection, and in intercellular spaces provides additional support to the concept that such glycoproteins play an important role in disease resistance.

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β-(1,3) glucanase activity and quantity of fungus in relation to Fusarium wilt in resistant and susceptible near-isogenic lines of muskmelon

Cited by 50 publications

References 18 publications

Mass Spectrometric Identification of Isoforms of PR Proteins in Xylem Sap of Fungus-Infected Tomato

Mass Spectrometric Identification of Isoforms of PR Proteins in Xylem Sap of Fungus-Infected Tomato

β-1,3-Endoglucanase from Soybean Releases Elicitor-Active Carbohydrates from Fungus Cell Walls

Time-course study of the accumulation of hydroxyproline-rich glycoproteins in root cells of susceptible and resistant tomato plants infected by Fusarium oxysporum f. sp. radicis-lycopersici

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