The surface anionogenic groups and sialoglycoconjugate structures of yeast forms were analysed by cell microelectrophoresis, binding assays with lectins and viral particles, ultrastructural cytochemistry, enzymic digestion and flow cytofluorimetry. yeast forms, particularly the budding primordia, reacted strongly with cationized ferritin. Binding assays showed that the reaction with sialic-acid-specific lectin (LFA) was distributed over the entire cell wall. Treatment of yeast forms with neuraminidase significantly reduced their negative surface charge and LFA labelling, which suggests that sialic acid residues are major anionogenic groups exposed on the surface. Furthermore, after neuraminidase treatment, labelling with (peanut) agglutinin increased due to unmasking of subterminal βD-galactopyranosyl residues. The sialic acid linkages to galactose are α2,6 and α2,3 as assessed, respectively, by fungal attachment to M1/5 and M1/5 HS8 strains of influenza A virus and binding of and agglutinins. The α2,6 linkage clearly predominated in both experiments. Flow cytofluorimetry analysis revealed the heterogenicity of P. brasiliensis yeast cell populations, which comprised young and mature budding yeasts. Both express binding sites to LFA and agglutinin.


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