The widespread and prolonged usage of azoles had led to the acquisition of azole resistance by Candida albicans. The molecular basis of this resistance in not very clear, although various mechanisms have been implicated as the overexpression of or mutation in the lanosterol-14a -demethylase, failure of drug accumulation mediated by drug extrusion pumps such as Cdr1, Cdr2 ( ATP-binding cassette family). Mukhopadhyay et al [1] have observed that Cdr1p and Pdr5p are sensitive to modification in the membrane lipid components, i.e., ergosterol and sphingolipids. In order to study the contribution of membrane lipids in drug susceptibilities, we used a D cgt mutant of C.albicans, defective in glucosylceramide biosynthesis and C.albicans wild-type for the isolation of the drug extrusion pump. Enriched plasma membrane fractions were prepared as described by Gouffeau & Dufour [ 2 ]. Proteins were analysed on 10% SDS-PAGE and the gels were stained with Comassie Blue. Proteins were transferred onto nitrocellulose membrane and a ~170 kDa band was detected by chemiluminescence using an anti-Pdr5p antibody of Saccharomyces cerevisiae. The classical inhibitor of Pdr5p, the oligomycin, was used to check the effect in both strains. The pattern at pH 7.5 was the same : ~40% of inhibition at 10m g/ml. In this way, enzymatic assays using classical modulators as trifluorperazine and verapamil, are current under way in order to check differences between the wild-type and mutant strain.