Abstract
The carbohydrate residues of the surface coat of 20 axenic cultures of Blastocystic hominis were studied using FITC-labelled lectins (ConA, WGA, DBA, HPA, SBA, PNA, UEAI and LPA). The specific affinity of reactive lectins was determinated by competitive inhibition assay with specific carbohydrates or by enzymatic pre-treatment of cells. All stocks strongly bound ConA and HPA; WGA, UEAI and LPA were partially reactive, and the remaining lectins were nonreactive. Inhibition assays showed abolition (WGA, LPA, UEAI and HPA) or partial reduction (ConA) of lectin affinity, which demonstrated the specificity of binding assay. These results indicate that B. hominis has surface components containing α-D-mannose, α-D-glucose, N-acetyl-α-D-glucosamine, α-L-fucose, chitin and sialic acid.
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