Proteomic analysis of cytoplasmic and surface proteins from yeast cells, hyphae, and biofilms of Candida albicans
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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.
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Many hundreds of mRNAs and proteins are differentially expressed between biofilms and planktonic cells.
“These studies have revealed that many hundreds of mRNAs and proteins are differentially expressed between biofilms and planktonic cells.”
From <i>Candida albicans</i> Biofilms and Human Disease (2015) · cites this paper as [115]
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- Authors
- Martínez‐Gomariz, M., Perumal, P., Mekala, S., Nombela, C., Chaffin, W. L., & Gil, C.
- Affiliations
- Texas Tech University (US)
- Universidad Complutense de Madrid (ES)
- Corresponding author
- Gil, Concha
- Venue
- PROTEOMICS
- Publisher
- Wiley
- Published
- 2009-04
- Volume
- 9
- Issue
- 8
- Pages
- 2230-2252
- ISSN
- 1615-9853 (ISSN-L)
- 1615-9861
- PMC
- PMC2818216
- OpenAlex
- W2124008198
- Cited by
- 101
- References
- 62
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 3 · 2023: 3 · 2022: 2 · 2021: 9 · 2020: 7 · 2019: 4 · 2018: 3 · 2017: 14 · 2016: 5 · 2015: 8 · 2014: 12 · 2013: 6 · 2012: 7
- FWCI
- 2.53
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- PROTEOMICS (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Fogarty International Center (1 RO3TW006307, R03TW006307)
- National Institute of Dental and Craniofacial Research (R01DE014029)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Health Sciences › Medicine › Infectious Diseases › Antifungal resistance and susceptibility
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Yeasts and Rust Fungi Studies
- Keywords
- Candida albicans, biofilm, fungal hyphae, cytosolic proteins, cell surface proteins, differentially abundant proteins, poly(methyl methacrylate), folate metabolism, oxidative stress response, host-pathogen interaction
- MeSH terms
- Candida albicans, Cell Membrane, Cytoplasm, Fungal Proteins, Membrane Proteins, Electrophoresis, Gel, Two-Dimensional, Oxidative Stress, Biofilms, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Proteome, Hyphae, Metabolic Networks and Pathways
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