The influence of carbohydrates in the interaction of Paracoccidioides brasiliensis with CCL-6 cells in vitro

Abstract

Introduction:Little is known about the early events in the interaction between Paracoccidioides brasiliensis and its host. To understand the effect of carbohydrates in the interaction between the fungus and epithelial cell in culture, we analyzed the influence of different carbohydrate solutions on the adhesion of P. brasiliensis yeast cells to CCL-6 cells in culture. Methods: Fungal cells were cultivated with the epithelial cell line, and different concentrations of D-fucose, N-acetyl-glucosamine, D-mannose, D-glucosamine, D-galactosamine, sorbitol and fructose were added at the beginning of the experiment. Six hours after the treatment, the cells were fixed and observed by light microscopy. The number of P. brasiliensis cells that were adhered to the CCL-6 monolayer was estimated. Results: The number of adhesion events was diminished following treatments with D-fucose, N-acetyl-glucosamine, D-mannose, D-glucosamine and D-galactosamine as compared to the untreated controls. Sorbitol and fructose-treated cells had the same adhesion behavior as the observed in the control. P. brasiliensis propagules were treated with fluorescent lectins. The FITC-labeled lectins WGA and Con-A bound to P. brasiliensis yeast cells, while SBA and PNA did not. Conclusions: The perceptual of adhesion between P. brasiliensis and CCL-6 cells decreased with the use of D-mannose, N-acetyl-glucosamine and D-glucosamine. The assay using FITC-labeled lectins suggests the presence of N-acetyl-glucosamine, α-mannose and α-glucose on the P. brasiliensis cell surface. An enhanced knowledge of the mediators of adhesion on P. brasiliensis could be useful in the future for the development of more efficient and less harmful methods for disease treatment and control.

Unravelling the interactions of the environmental hostAcanthamoeba castellaniiwith fungi through the recognition by mannose‐binding proteins

“…Both identified MBPs (L8GXW7 and Q6J288) bear a domain of unknown function (DUF4114), with a signature site of the secondary structure of ConA‐like lectins/glucanases superfamily, as described (Garate et al, ). Our findings suggest that the fungal mannose‐dependent association to Ac might be one of the most important, as correlated to fungal association to epithelial cells thought CCL‐6, which could be inhibited by soluble mannose (Silva, Pimenta, Silva, Correa, & Correa Junior, ).…”