Cell wall glycoproteins participate in the adhesion of Sporothrix schenckii to epithelial cells
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Updated: Jun 6, 2026

Glycan Profiling of Plant Cell Wall Polymers using Microarrays
Published on: December 17, 2012
Gerardo Sandoval-Bernal1, Gloria Barbosa-Sabanero, Mineko Shibayama
1División de Ciencias Naturales y Exactas Campus Guanajuato, Departamento de Biología, Universidad de Guanajuato, Noria Alta S/N, Col. Noria Alta, 36000, Guanajuato, Guanajuato, México.
Abstract:
Sporothrix schenckii is the etiologic agent of sporotrichosis. This fungal infection is an emerging disease potentially fatal in immunocompromised patients. The adhesion to host cells is a crucial early event related with the dissemination of pathogens. In order to clarify the mechanisms of adhesion of S. schenckii yeast cell to epithelial cells, we studied the biochemical basis of this process. The electrophoretic analysis of cell wall protein from S. schenckii coupled at ConA and stained with HRP, revealed nine different proteins with MW ≥ 180, 115, 90, 80, 58, 40, 36, 22 and 18 kDa. Using ligand-like assay with biotinylated S. schenckii surface proteins, five proteins with MW ≥ 190, 180, 115, 90 and 80 kDa which have affinity to epithelial cells were identified. The adhesion of yeast to epithelial monolayer was significantly inhibited when S. schenckii was pretreated with concanavalinA (ConA) and wheat germ agglutinin (WGA) lectins, alkali, periodate, trypsin, endoglycosidase H (EndoH), salt solutions and detergents. The ability of adhesion of S. schenckii yeast was recovered by blocking the lectin with sugar complementary. These data suggest that surface glycoprotein with mannose and glucose residue could be participate in the process of fungal adhesion to epithelial cells.
Insights
Sporothrix schenckii adhesion to host cells involves surface glycoproteins. Mannose and glucose residues on these glycoproteins are key to fungal attachment, impacting sporotrichosis infection spread.
Area of Science:
- Mycology
- Infectious Diseases
- Biochemistry
Background:
- Sporothrix schenckii causes sporotrichosis, an emerging fungal infection.
- Pathogen adhesion to host cells is critical for disease dissemination, especially in immunocompromised individuals.
Purpose of the Study:
- To elucidate the biochemical mechanisms underlying Sporothrix schenckii yeast cell adhesion to epithelial cells.
- To identify specific S. schenckii surface components involved in host cell interaction.
Main Methods:
- Electrophoretic analysis of S. schenckii cell wall proteins coupled with Concanavalin A (ConA).
- Ligand-binding assays using biotinylated S. schenckii surface proteins to assess epithelial cell affinity.
- Inhibition assays using lectins (ConA, WGA), enzymatic treatments (trypsin, endoglycosidase H), and chemical treatments (alkali, periodate, detergents, salt solutions).
Main Results:
- Nine S. schenckii cell wall proteins were identified via electrophoresis (MW ≥ 18-180 kDa).
- Five surface proteins (MW ≥ 80-190 kDa) demonstrated affinity for epithelial cells.
- Adhesion was significantly inhibited by lectins, enzymatic, and chemical treatments, with recovery upon lectin blocking by complementary sugars.
Conclusions:
- Surface glycoproteins containing mannose and glucose residues are implicated in S. schenckii adhesion to epithelial cells.
- These findings provide insights into the molecular basis of sporotrichosis pathogenesis and potential therapeutic targets.
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