Specificity of the osmotic stress response in Candida albicans highlighted by quantitative proteomics

Jacobsen, Mette D, Beynon, Robert J ORCID: 0000-0003-0857-495X, Gethings, Lee A, Claydon, Amy J, Langridge, James I, Vissers, Johannes PC, Brown, Alistair JP and Hammond, Dean E ORCID: 0000-0002-6326-8739 (2018) Specificity of the osmotic stress response in Candida albicans highlighted by quantitative proteomics. Scientific Reports, 8 (1). 14492-.

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Official URL: https://www.nature.com/articles/s41598-018-32792-6

Abstract

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 post-transcriptional regulatory mechanisms that contribute to the outputs, as well as testing presumptions about the regulation of protein levels based on transcript profiling. Here, 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 were down-regulated in response to 1M NaCl, reflecting the decrease in ribosome biogenesis and translation that often accompanies stress. The 64 up-regulated proteins included central metabolic enzymes required for glycerol synthesis, a key osmolyte for this yeast, as well as proteins with functions during 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. The specificity of the response to salt stress is highlighted by the small proportion of quantified C. albicans proteins (5%) whose relative elevated abundances were statistically significant.

Item Type:	Article
Uncontrolled Keywords:	Mechanisms of disease, Pathogens
Depositing User:	Symplectic Admin
Date Deposited:	10 Oct 2018 15:21
Last Modified:	19 Jan 2023 01:14
DOI:	10.1038/s41598-018-32792-6
Open Access URL:	https://doi.org/10.1038/s41598-018-32792-6
Related URLs:	Author Publisher
URI:	https://livrepository.liverpool.ac.uk/id/eprint/3027368