Uma nova lectina lactose-específica isolada do fungo Langermannia bicolor com propriedades antibiofilme

Abstract

Constituted by a complex matrix of biopolymers, the structure of the bacterial biofilm acts as a strategy of resistance to environmental stress conditions, including for example host immunity and antibiotic action. This problem has intensified the search for molecules with antibiofilm action, such as those capable of interfering with the matrix structure of the biofilm and thus allowing the action of antibiotic drugs. In this context, the lectins, proteins of non-immune origin capable of binding specifically to biofilm carbohydrates, stand out. The aims of this work are isolate and characterize the lectin from the basidiomycete Langermannia bicolor (LLB) and evaluate its binding potential to bacteria and antibiofilm activity. LLB was isolated after separation with cation-exchange chromatography and gel filtration, showing specificity calcium-dependent to bind lactose, as well as high stability at different pH and temperatures values. LLB did not affect the human red blood cells and murine fibroblast strains (3T3) viability. Although LLB had no antibacterial activity, it was able to agglutinate (interaction dependent on its recognizing domain) and significantly reduce total biofilm biomass preventing early biofilm formation and preformed biofilm in Staphylococcus aureus and Pseudomonas aeruginosa. Moreover, these data suggest LLB as a future candidate for prototype antibiofilm, however further studies should be conducted to elucidate the mechanism of action as well as its possible combination with conventional antibiotics as a therapeutic strategy to reduce the development of bacterial resistance.