The authors also used an A.

fumigatus echinocandin-resistant strain to confirm the specificity of protein identification and demonstrated that potential biomarkers of caspofungin resistance, changing 12-fold or more, include Asp f1, a PT repeat family protein, a subunit of the nascent polypeptide-associated complex, the citrate synthase Cit1, and FKBP-type peptidyl-prolyl isomerase, a mitochondrial hypoxia response domain protein, 4-hydroxyphenylpyruvate PS-341 cost dioxygenase and one UFP. Furthermore, parallel microarray analysis of gene expression alterations in response to caspofungin exposure provided a broadly similar response (e.g. elevation in ribosomal protein transcripts at 24 h); however, opposite gene/protein responses were observed in some cases. Ultimately, alterations in intracellular or extracellular protein expression

should improve our understanding of fungal drug resistance and facilitate the development of strategies to circumvent drug resistance with concomitant efficacy potentiation of current antifungal drugs. In an effort to identify proteins associated with yeast–hyphal transition in Candida albicans, which is strongly associated with the virulence potential of this organism, analysis of the TSA HDAC manufacturer acidic subproteome was undertaken (Monteoliva et al., 2011). This led to the identification of 21 differentially abundant acidic proteins, 10 of which had not been found previously upon comparative 2D-PAGE/DIGE analysis and underscores the necessity for multiple comparative proteomic strategies. Candida albicans–macrophage interactions were studied using proteomics (Fernández-Arenas et al., 2007). Here, a combination of 2D-PAGE and MALDI-ToF/ToF MS showed Thiamet G the differential expression of 132 yeast proteins upon macrophage interaction. This study was the first to explore C. albicans–macrophage interaction using proteomics, and identified 67 proteins that were either downregulated (carbon-compound metabolism) or upregulated

(lipid, fatty acid, glyoxylate and tricarboxylic acid cycles) in expression upon co-culture. Fusarium graminearum is a filamentous fungal pathogen of wheat, maize and grains; as such, it is a major threat to the global food supply (Kikot et al., 2009). Moreover, Fusarium spp. are potent producers of mycotoxins, which can cause significant disease in humans. Although initial proteomic studies involving F. graminearum focused on altered plant protein responses to fungal exposure (Zhou et al., 2006), genome availability and improvements in protein extraction techniques have meant that Fusarium proteomics research has intensified since 2007 (Paper et al., 2007; Taylor et al., 2008). Indeed, Pasquali et al. (2010) have produced an online video tutorial to demonstrate the intricacies of protein extraction from Fusarium strains.