Abstract
Paracoccidioides genus are the etiologic agents of paracoccidioidomycosis (PCM), a systemic mycosis endemic in Latin America. Few virulence factors have been identified in these fungi. This paper describes support data from the quantitative proteomics of Paracoccidioides brasiliensis attenuated and virulent isolates [1]. The protein compositions of two isolates of the Pb18 strain showing distinct infection profiles were quantitatively assessed by stable isotopic dimethyl labeling and proteomic analysis. The mass spectrometry and the analysis dataset have been deposited to the ProteomeXchange Consortium via the PRIDE partner repository with identifier PXD000804.
Highlights
Paracoccidioides genus are the etiologic agents of paracoccidioidomycosis (PCM), a systemic mycosis endemic in Latin America
This paper describes support data from the quantitative proteomics of Paracoccidioides brasiliensis attenuated and virulent isolates [1]
The protein compositions of two isolates of the Pb18 strain showing distinct infection profiles were quantitatively assessed by stable isotopic dimethyl labeling and proteomic analysis
Summary
Mass spectrometry data and worksheets with peptide and protein identifications. Data dependent LC-MS/MS acquired in LTQ-Orbitrap Velos (Thermo) coupled to EASY-nLC II (Thermo). Attenuated and virulent Paracoccidioides brasiliensis (Pb18) strains were grown in minimal and rich media for comparative proteomic analysis. A large dataset of proteins involved with virulence regulation in P. brasiliensis identified by stable isotopic dimethyl labeling-based mass spectrometry, which were validated by quantitative PCR assays. Using a quantitative shotgun proteomic approach (nLC–ESI–MS/MS) we have previously identified in these dataset proteins with potential role in the regulation of virulence in the pathogenic fungus Paracoccidioides brasiliensis [1]. Each strain was grown in biological duplicates, proteins were extracted, digested with trypsin, labeled with light and heavy formaldehyde, and each biological replicate was analyzed by LC– MS/MS in technical triplicates. Raw data were processed and analyzed in PEAKS Studio 7.0 (Bioinformatics Solutions Inc.) and proteins were quantified by the ratios of heavy/light peptide intensities. Raw data were processed and analyzed in PEAKS Studio 7.0 (Bioinformatics Solutions Inc.) and proteins were quantified by the ratios of heavy/light peptide intensities. qPCR assays were performed to validate the LC–MS/MS data (Fig. 1)
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