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Fig. 4 | BMC Microbiology

Fig. 4

From: Candida albicans and Candida glabrata triosephosphate isomerase – a moonlighting protein that can be exposed on the candidal cell surface and bind to human extracellular matrix proteins

Fig. 4

Use of anti-Tpi1 antibodies to displace labeled VTR and FN from binding to C. albicans and C. glabrata cells. Binding experiments were performed for C. albicans and C. glabrata in the wells of MaxiSorp microplates (1 x 106 cells per well) or in Eppendorf tubes (3 x 107 cells per tube), respectively. The candidal cells grown in RPMI 1640 medium were pre-incubated with anti-S. cerevisiae Tpi1 antibodies (1 µg/mL) followed by 50 µL of biotin-labeled human VTR or FN proteins at a final concentration of 250 nM. This was followed in all cases by an incubation for 1.5 h at 37°C. After washing off unbound protein, the amounts of bound VTR or FN were determined using an SA-HR/TMB system. The level of binding of the biotinylated human protein to the Candida spp. cells without antibodies was considered to be 100%. Bars represent the mean values from three determinations, with standard deviations. Statistical significance levels were determined using a one-way ANOVA test against the signal from the control sample containing the biotinylated proteins with no antibody pre-incubation; *p<0.05 and **p<0.01

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