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Fig. 3 | BMC Microbiology

Fig. 3

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. 3

Western-blotting identification of Tpi1 in whole mixtures of cell wall proteins from C. albicans and C. glabrata. (A) Equal amounts of total proteins (20 µL at a concentration of 0.5 mg/mL) isolated under different culture conditions, i.e. YPD, YPDA and RPMI 1640 medium, were resolved by SDS-PAGE in the Laemmli system under reducing conditions. Thereafter, the protein bands were transferred to a PVDF membrane and probed with a primary anti-Tpi1 antibody and an alkaline phosphatase-labelled secondary antibody. Protein bands were visualized using a BCIP/NBT system. The uncropped scan of the blot is presented. 1 µg of S. cerevisiae Tpi was used as a control. (B) The Tpi1 amount within the mixture of Candida spp. cell wall proteins was determined by densitometric analysis of the obtained blots using ImageJ software. The raw results were corrected for the slightly different reactivities of anti-S. cerevisiae Tpi1 antibody with the purified Tpi protein from C. glabrata and C. albicans (based on the calibration presented in Figure S1B in the Supplementary materials). Bars represent the mean values with standard deviations from two independent experiments

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BMC Microbiology

ISSN: 1471-2180

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