Proteomic analysis of cytoplasmic and surface proteins from yeast cells, hyphae, and biofilms of Candida albicans

Candida albicans is a human commensal and opportunistic pathogen that participates in biofilm formation on host surfaces and on medical devices. We used DIGE analysis to assess the cytoplasmic and non-covalently attached cell-surface proteins in biofilm formed on polymethylmethacrylate and planktoni...

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Published inProteomics (Weinheim) Vol. 9; no. 8; pp. 2230 - 2252
Main Authors Martínez-Gomariz, Montserrat, Perumal, Palani, Mekala, Satish, Nombela, César, Chaffin, W. LaJean, Gil, Concha
Format Journal Article
LanguageEnglish
Published Weinheim Wiley-VCH Verlag 01.04.2009
WILEY‐VCH Verlag
Wiley-VCH
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Summary:Candida albicans is a human commensal and opportunistic pathogen that participates in biofilm formation on host surfaces and on medical devices. We used DIGE analysis to assess the cytoplasmic and non-covalently attached cell-surface proteins in biofilm formed on polymethylmethacrylate and planktonic yeast cells and hyphae. Of the 1490 proteins spots from cytoplasmic and 580 protein spots from the surface extracts analyzed, 265 and 108 were differentially abundant respectively (>1.5-fold, p <0.05). Differences of both greater and lesser abundance were found between biofilms and both planktonic conditions as well as between yeast cells and hyphae. The identity of 114 cytoplasmic and 80 surface protein spots determined represented 73 and 25 unique proteins, respectively. Analyses showed that yeast cells differed most in cytoplasmic profiling while biofilms differed most in surface profiling. Several processes and functions were significantly affected by the differentially abundant cytoplasmic proteins. Particularly noted were many of the enzymes of respiratory and fermentative pentose and glucose metabolism, folate interconversions and proteins associated with oxidative and stress response functions, host response, and multi-organism interaction. The differential abundance of cytoplasmic and surface proteins demonstrated that sessile and planktonic organisms have a unique profile.
Bibliography:http://dx.doi.org/10.1002/pmic.200700594
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Present address: 1209 Fox Run Drive Plainsboro, NJ 08536
Present address: Center for Advanced Studies in Botany, University of Madras, Guindy Campus, Chennai, India 600025
ISSN:1615-9853
1615-9861
DOI:10.1002/pmic.200700594