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Biocell ; 27(2): 173-179, Aug. 2003.
Article in English | LILACS | ID: lil-384246

ABSTRACT

Vicilins (7S storage proteins) found in various legume seeds have been previously shown to interfere with the germination of spores or conidia of phytopathogenic fungi and inhibit yeast growth and glucose stimulated acidification of the medium by yeast cells. In the present work vicilins from cowpea (Vigna unguiculata) seeds were added to the growth medium of Saccharomyces cerevisiae cells and Fusarium oxysporum conidia. Helix pomatia lectin, wheat germ agglutinin and Ulex europaeus lectin were used to identify differences in the binding of the vicilins to the surface of cells of S. cerevisiae and F. oxysporum treated with this protein. After the growth period, the material in suspension (yeast cells) was centrifuged and the final pellet was also treated with different sugar (glucose, sucrose, glucosamine, N-acetyl-glucosamine) concentrations and 0.1 M HCl for extraction of vicilins associated to chitinous structures present in yeast cells. Our results showed that vicilin sub-units were present in the different sugar extracts of yeast cells pretreated with the vicilins and these proteins were eluted by 0.5 M solutions of sugars in the following order of efficiency of elution: N-acetyl-glucosamine, sucrose/glucose and glucosamine.


Subject(s)
Carbohydrates/pharmacology , Binding, Competitive/drug effects , Cell Membrane/drug effects , Cell Wall/drug effects , Plant Proteins/pharmacology , Acetylglucosamine/pharmacology , Fungi/drug effects , Fungi/growth & development , Fungi/ultrastructure , Fusarium/drug effects , Fusarium/growth & development , Fusarium/ultrastructure , Glucosamine/pharmacology , Glucose/pharmacology , Binding, Competitive/physiology , Microscopy, Electron , Cell Membrane/metabolism , Cell Membrane/ultrastructure , Cell Wall/metabolism , Cell Wall/ultrastructure , Sucrose/pharmacology , Saccharomyces cerevisiae/drug effects , Saccharomyces cerevisiae/growth & development , Saccharomyces cerevisiae/ultrastructure , Binding Sites/drug effects , Binding Sites/physiology
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