Effects of French Bean Tissue and Leaf Protoplasts on Colletotrichum lindemuthianum Polygalacturonase

Colletotrichum lindemuthianum is the causal agent of anthracnose in Phaseolus vulgaris L. (French bean). The α and β races of the fungus were used in this study with French bean cultivar ‘Great Northern’. Whole plants inoculated with the α race developed brown lesions on the hypocotyls (susceptible response). The β race caused small limited lesions, indicating a more resistant interaction. Extracellular products and cell wall materials were isolated from β race cultures and extracellular products from α race cultures. The extracts were size fractionated. By using a cotyledon bioassay, elicitor activity was demonstrated on ‘Dark Red Kidney’ within fractions from the α race. Fractions from the β race had little activity on ‘Dark Red Kidney’ or ‘Great Northern’ cotyledons. Protoplasts were isolated from ‘Great Northern’ bean hypocotyl tissue and incubated with the fungal fractions. Even at low concentrations (0.01 μg glucose equivalent∙mL−1), the β race culture filtrate rapidly killed a greater percentage of protoplasts (30%) than the α race (15%). The β race wall extract had little effect upon protoplast viability. The proportion of nonviable protoplasts depended on the incubation period and the concentration of the fungal material. Heat treatment of the culture filtrates and wall extract did not decrease their lethal effects. The results suggest that protoplasts may be valuable in examining the nature of certain plant–pathogen interactions.

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Infection and Phytoalexin Accumulation in French Bean Leaves Injected with Spores of Colletotrichum lindemuthianum

Journal of Phytopathology ◽

10.1111/j.1439-0434.1982.tb01743.x ◽

1982 ◽

Vol 103 (3) ◽

pp. 189-197 ◽

Cited By ~ 4

Author(s):

M. K. Theodorou ◽

Jane C. M. Scanlon ◽

I. M. Smith

Keyword(s):

French Bean ◽

Colletotrichum Lindemuthianum ◽

Bean Leaves

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Effect of biocontrol agents and fungicides against anthracnose of French bean caused by Colletotrichum lindemuthianum (Sacc. and Magn.) in mid-hill of Garhwal Himalaya

International Journal of Chemical Studies ◽

10.22271/chemi.2020.v8.i2aj.9101 ◽

2020 ◽

Vol 8 (2) ◽

pp. 2352-2355

Author(s):

N Pandey ◽

S Ravi

Keyword(s):

French Bean ◽

Colletotrichum Lindemuthianum ◽

Garhwal Himalaya ◽

Biocontrol Agents

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Elicitor-induced prolyl hydroxylase from French bean (Phaseolus vulgaris). Localization, purification and properties

Biochemical Journal ◽

10.1042/bj2290693 ◽

1985 ◽

Vol 229 (3) ◽

pp. 693-699 ◽

Cited By ~ 31

Author(s):

G P Bolwell ◽

M P Robbins ◽

R A Dixon

Keyword(s):

Phaseolus Vulgaris ◽

Cultured Cells ◽

Smooth Endoplasmic Reticulum ◽

Sodium Dodecyl ◽

French Bean ◽

Exchange Chromatography ◽

Prolyl Hydroxylase ◽

Colletotrichum Lindemuthianum ◽

Phytopathogenic Fungus ◽

Kinetic Properties

The enzyme prolyl hydroxylase (proline: 2-oxoglutarate dioxygenase, EC 1.14.11.12), induced in suspension-cultured cells of Phaseolus vulgaris L. (French bean) by treatment with an elicitor preparation from the phytopathogenic fungus Colletotrichum lindemuthianum, has been investigated. The enzyme, which catalyses the hydroxylation of poly-L-proline with the stoichiometric decarboxylation of 2-oxoglutarate, has been shown to be localized mainly in smooth endoplasmic reticulum. After solubilization from microsomal membranes, the hydroxylase was purified by ion-exchange chromatography and affinity chromatography on poly-L-proline-Sepharose 4B. The subunit Mr, as assessed by sodium dodecyl sulphate/poly-acrylamide-gel electrophoresis, was 65 000, the subunit apparently being recovered as a doublet: the subunits associate under non-denaturing conditions to give at least a tetramer. The bean hydroxylase has kinetic properties and cofactor requirements similar to those previously reported for the enzyme from other plants. Elicitor treatment of suspension-cultured bean cells leads to a rapid induction of prolyl hydroxylase activity concomitant with induction of a protein: arabinosyl-transferase and increased levels of an arabinosylated hydroxyproline-rich protein.

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