title: Proteomics for the analysis of the Candida albicans biofilm lifestyle.
abstract: Candida albicans is an opportunistic pathogenic fungus capable of causing infections in immunocompromised patients. Candidiasis is often associated with the formation of biofilms on the surface of inert or biological materials. Biofilms are structured microbial communities attached to a surface and encased within a matrix of exopolymeric substance (EPS). At present, very little is known about the changes in protein profiles that occur during the transition from the planktonic to the biofilm mode of growth. Here, we report the use of proteomics for the comparative analysis of subcellular fractions obtained from C. albicans biofilm and planktonic cultures, including cell surface-associated proteins and secreted components present in liquid culture supernatants (for planktonic cultures) and EPS (for biofilms). The analysis revealed a high degree of similarity between the protein profiles associated with the planktonic and biofilm extracts, and led to the identification of several differentially expressed protein spots. Among the differentially expressed proteins, there was a preponderance of metabolic enzymes that have been described as cell surface proteins and immunodominant antigens. Proteins found in the biofilm matrix included a few predicted to form part of the secretome, and also many secretion-signal-less proteins. These observations contribute to our understanding of the C. albicans biofilm lifestyle.
authors.affiliation: Department of Biology and South Texas Center for Emerging Infectious Diseases, The University of Texas at San Antonio, TX 78249, USA.
authors.forename: Derek P
authors.initials: DP
authors.lastname: Thomas
authors.forename: Stefano P
authors.initials: SP
authors.lastname: Bachmann
authors.forename: Jose L
authors.initials: JL
authors.lastname: Lopez-Ribot
mesh_terms: D018441:Biofilms / Q000254:growth & development*; D002176:Candida albicans / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D015180:Electrophoresis, Gel, Two-Dimensional; D005656:Fungal Proteins / Q000032:analysis* / Q000235:genetics / Q000302:isolation & purification / Q000502:physiology; D006801:Humans; D013058:Mass Spectrometry; D010449:Peptide Mapping; D010933:Plankton / Q000737:chemistry / Q000502:physiology; D040901:Proteomics / Q000379:methods*; D013347:Subcellular Fractions
chemical_list: D005656:Fungal Proteins