Stress adaptation is critical for the survival of microbes in dynamic environments, and in particular, for fungal pathogens to survive in and colonise host niches. Proteomic analyses have the potential to significantly enhance our understanding of these adaptive responses by providing insight into the post-transcriptional regulatory mechanisms that contribute to the outputs as well as testing presumptions about the regulation of protein levels based on transcript profiling. Therefore, in this study we used label-free, quantitative mass spectrometry to re-examine the response of the major fungal pathogen of humans, Candida albicans, to osmotic stress. Of the 1,262 proteins that were identified, 84 (7.7%) were reproducibly down-regulated in response to 1 M NaCl. These changes reflected the decrease in ribosome biogenesis and translation that often accompanies stress exposure. The 64 up-regulated proteins (5.1% of the total) included the glycerol biosynthetic enzymes, Gpd2 and Gpp1/Rhr2, as well as enzymes of central metabolism that may contribute to carbon flux to glycerol, a key osmolyte for this yeast. The up-regulated proteins also included proteins with functions during stress such as Hsp12, Hsp21, Cat1, Gsh2, Glx3 and Tps2, which was consistent with a perturbation of redox homeostasis and increased synthesis of the stress protectant trehalose during salt stress. These data reinforce the view that adaptation to salt stress involves a transient reduction in ribosome biogenesis and translation together with the accumulation of the osmolyte, glycerol. Given the small proportion of C. albicans proteins whose abundances are affected by salt stress, the results highlight the specificity of the metabolic response to salt stress.