Comparative characterization of lectins of pathogenic and saprophytic filamentous fungi Fusarium solani

Abstract

In the present study, we isolated, purified and characterized the lectin of the phytopathogenic fungus Fusarium solani 6 and compared it with the properties of the lectin of the saprophytic strain Fusarium solani 4. Electrophoretically homogeneous lectin was obtained from the mycelium of the fungus F. solani 6 by hydrophobic chromatography and gel filtration. The molecular weight of the native lectin molecule was established to be 30.0 kDa, and it was found that it consists of two identical subunits. Comparison of the physicochemical properties of the lectin of the phytopathogenic strain with the lectin of the saprophytic strain showed that the F. solani 6 lectin was a more thermostable and alkali-resistant protein. F. solani 6 lectin showed affinity for simple sugars, and F. solani 4 lectin - for glycoproteins. In contrast to the lectin of a saprophytic fungus, the treatment of pea seedling roots with F. solani lectin 6 before they were infected with the phytopathogen led to a decrease in the degree of damage to the plant root system and the prevalence of Fusarium. These results open up prospects for further study of the phytopathogen lectin and its potential application as a means of eliciting action.