Characterization of the recognition of Candida species by mannose-binding lectin using surface plasmon resonance

Abstract

The interaction of mannose-binding lectins (MBLs) with Candida albicans has been analyzed previously by microscopy and flow cytometry. We recently demonstrated that serum MBL levels vary during infection with Candida spp. and that serum MBLs are capable of interacting with yeast cell wall components. The aim of this study was to use, for the first time, surface plasmon resonance (SPR) technology to characterize the interaction between living label-free yeasts and non-mutated MBL purified from human serum. Our preliminary results demonstrate the robustness of this tool, which revealed specific and differential reactivities between the principal Candida spp. of medical interest. This model offers new perspectives as a tool for the characterization of yeast strains carrying mutations in gene coding for the mannosylation of fungal cell wall glycans and will enable better characterization of the interactions between C-lectins and glycan motifs expressed on the surface of yeasts.

Dissection of the anti-Candida albicans mannan immune response using synthetic oligomannosides reveals unique properties of β-1,2 mannotriose protective epitopes

“…The sensorship was regenerated with 0.25 M EDTA buffer. For each sample, the results are expressed as the difference between the tested flow cell and reference flow cell (flow cell without immobilized rMBL) as previously described 12 . Normalization of results was performed according to the molecular mass of each BSTO.…”

“…Three polypeptide chains make up a triple helix with a collagenous region 11 , which is the basic circulating subunit of MBL. In serum, MBL is composed of oligomers of subunits from dimers to hexamers, which are effector forms of the lectins for glycan or pathogen interactions 12 , 13 . MBL interacts with terminal-D-mannose residues, L-fucose, and GlcNAc 14 , 15 but also with bacteria, virus, molds, yeasts, and parasites.…”

Fluorescence assay for glycan expression on living cancer cells based on competitive strategy coupled with dual-functionalized nanobiocomposites

“…15 Recently, glycan assays based on lectinglycan interaction have gained much attention due to the high efficiency of lectin arrays and the availability of diverse natural and engineered lectins. [16][17][18][19][20] Fluorescence assay has been widely applied in the detection of various biomolecules including protein, peptide and DNA owing to features such as the relatively mild sample preparation process and rapid signal output. 16,17,21 In most of the conventional uorescence assays, uorescent labels are directly tagged on the analytes due to their lack of uorescent groups for signal generation.…”