Effect of Botrytis cinerea infection and elicitation on beta-1,3-glucanase and chitinase activity in bean leaves and cell cultures

• Autorzy: Kuzniak E , Urbanek H. , Michalak A. , Herka K.

Warianty tytułu

PL

Wplyw zakazenia Botrytis cinerea i elicytacji na aktywnosc beta-1,3-glukanazy i chitynazy w lisciach i kulturach zawiesinowych fasoli

• Języki publikacji: EN

Abstrakty

EN

The activity of ß-1,3-glucanase and chitinase in bean plants treated with B. cinerea products or/and infected and in cell cultures after application of fungal products has been studied. Botrytis cinerea infection and culture filtrates, ethanol precipitates, glucan and conidial extract treatment markedly enhanced the activity of both hydrolases. Cell cultures treated with B. cinerea products reacted similarly to intact plants. In plants pretreated with 2-day culture filtrate and conidial extract and then infected, ß-1,3-glucanase and chitinase were induced stronger than after infection without pretreatment.

PL

W pracy badano aktywność 3-1,3-glukanazy i chitynazy w liściach fasoli (Phaseolus vulgaris L.) odm. „Złota Saxa" hodowanej w szklarni po potraktowaniu produktami otrzymanymi z hodowli Botrytis cinerea Pers. lub/i po zakażeniu oraz w kulturach zawiesinowych traktowanych produktami grzyba. Stwierdzono wyraźny wzrost aktywności obu enzymów w liściach zarówno po zakażeniu, jak i po potraktowaniu ekstraktem z zarodników, filtratami, osadami alkoholowymi i glukanem z hodowli B. cinerea Pers. Reakcja kultur zawiesinowych fasoli pod wpływem produktów B. cirenea Pers. była podobna do stwierdzonej w liściach. Indukcja p-l,3-glukanazy i chitynazy w liściach uprzednio traktowanych ekstraktem z zarodników i filtratem z 2-dniowej hodowli grzyba, a następnie zakażonych była silniejsza niż w liściach nietraktowanych po zakażeniu.

Słowa kluczowe

PL

fasola Zlota Saxa; fasola; aktywnosc enzymatyczna; beta-1,3-glukanazy; liscie; Botrytis cinerea; infekcja grzybowa; chitynaza; odmiany roslin

EN

Zlota Saxa cultivar; bean; enzyme activity; beta-1,3-glucanase; leaf; Botrytis cinerea; fungal infection; chitinase; plant cultivar

• Wydawca: -
• Czasopismo: Acta Agrobotanica
• Rocznik: 1994
• Tom: 47
• Numer: 2
• Strony: 63-71
• Opis fizyczny: s.63-71,rys.,tab.,bibliogr.

Twórcy

autor

Kuzniak E

• Uniwersytet Lodzki, Banacha 12/16, 90-237 Lodz

autor

Urbanek H.

• Uniwersytet Lodzki, Banacha 12/16, 90-237 Lodz

autor

Michalak A.

• Uniwersytet Lodzki, Banacha 12/16, 90-237 Lodz

autor

Herka K.

• Uniwersytet Lodzki, Banacha 12/16, 90-237 Lodz

Bibliografia

• Benhamou N., Joosten H. A. J., de Wit P. J. G. M.,1990. Subcellular localization of chitinase and of its potential substrate in tomato root tissues infected by Fusarium oxysporum f. sp. radicis-lycopersici. Plant Physiol. 92: 1108-1120.
• Bhandal I. S., Paxton J. D., Widholm J. M., 1987. Phytophthora megasperma culture filtrate and cell wall preparation stimulate glyceollin production and reduce cell viability in suspension cultures of soybean. Phytochem. 26: 2691-2694.
• Dalkin K., Edwards R., Edington B., Dixon R. A.,1990. Stress responses in alfalfa (Medicago sativa L.) I. Induction of phenylpropanoid biosynthesis and hydrolytic enzymes in elicitor-treated cell suspension cultures. Plant Physiol. 92: 440-446.
• Dixon R. A., 1985. Isolation and maintenance of callus and cell suspension cultures. [In]: Plant cell culture: a practical approach. R. A. Dixon (ed.), IRL Press, Oxford, Washington, pp. 1-20.
• Hughes R. K., Dickerson A. G., 1991. Modulation of elicitor-induced chitinase and β-l,3-glucanase activity by hormones in Phaseolus vulgaris. Plant Cell Physiol. 32: 853-861.
• Kauffmann S., Baillieul F., Genetet I., Kopp M., Fritig B., 1993. Two proteins secreted by Phytophthora megasperma elicit necrosis and defence-related responses in tobacco. [In]: Mechanisms of plant defense responses. B. Fritig, M. Legrand (ed.), Kluwer Academic Publishers, pp. 140-143.
• Keen N. T., Yoshikawa M., 1983. β-l,3-Endoglucanase from soybean release elicitor-active carbohydrates from fungus cell walls. Plant Physiol. 71: 460-465.
• Kirsch C., Hahlbrock K., Kombrink E., 1993. Purification and characterization of extracellular, acidic chitinase isoenzymes from elicitor- stimulated parsley cells. J. Biochem. 213: 419-425.
• Kombrink E., Hahlbrock K., 1986. Responses of cultured parsley cells to elicitors from phytopathogenic fungi. Plant Physiol. 81: 216-222.
• Kurosaki F., Tashiro N., Nishi A., 1990. Chitinase induction in carrot cell cultures treated with various fungal components. Bioch. Int. 20: 99-106.
• Mauch F., Hadwiger L. A., Boller T., 1984. Ethylene: symptom, not signal for the induction of chitinase and β-l,3-glucanase in pea pods by pathogens and elicitors. Plant Physiol. 76: 607-611.
• Mauch F., Mauch - Mani B., Boller T., 1988. Antifungal hydrolases in pea tissue. II. Inhibition of fungal growth by combination of chitinase and β-l,3-glucanase. Plant Physiol. 88: 936-942.
• Meins F., Ahl P., 1989. Induction of chitinase and β-1,3-glucanase in tobacco plants infected with Pseudomonas tabaci and Phytophthora parasitica var. nicotianae. Plant Sci. 61: 155-161.
• Nelson N., 1944. A photometric adaptation of the Somogyi method for the determination of glucose. J. Biol. Chem. 153: 375-380.
• Tuzun S. M., Rao N., Vogeli U., Schradl Ch. L., Kuć J., 1989. Induced systemic resistance to blue mold: Early induction and accumulation of β-l,3-glucanases, chitinases and other pathogenesis-related proteins (b-proteins) in immunized tobacco. Phytopathology 79: 978-983.
• Urbanek H., Kuźniak-Gębarowska E., Herka K., 1991. Elicitation of defence responses in bean leaves by Botrytis cinerea polygalacturonase. Acta Physiol. Plant. 13: 43-50.
• Urbanek H., Zalewska-Sobczak J., 1984. Multiplicity of cell wall degrading glycosidic hydrolases produced by apple infecting Botrytis cinerea. Phytopath. Z. 110: 261-271.
• Van den Bulcke M., Bauw G., De Rycke R., Castersana C., van Montagu M., Vanderckhove J., 1990. The role of vacuolar and secreted pathogenesis-related β-l,3-glucanases and chitinases in the defence response of plants. Bull. Sci. Bot. Fr. 137: 51 -63.