Bovine and feline Tritrichomonas foetus total cellular protein mass spectrometry data files
  • Description

    This is the raw data from Mass Spectrometry analysis of spots resolved using two-dimensional analysis from a total protein sample from Tritrichomonas foetus bovine and feline genotypes. The dataset contains data files generated following the analysis of protein spots using LC-MS/MS.

    There are two types of data files.

    .Wiff files were produced using the following procedure: \n\nLC−MS/MS was performed using a QSTAR Elite hybrid Q-TOF mass spectrometer (Applied Biosystems, Sciex, USA). The peptides were washed off the trap at 300 nL min-1 onto a PicoFrit column (75 μm × 100 mm) (New Objective, USA) packed with Magic C18AQ resin (Michrom Bioresources, USA), and the following protocol was used to elute peptides from the column and into the source of a QSTAR Elite hybrid Q-TOF mass spectrometer (Applied Biosystems, Sciex, USA): 5−30% MS buffer B (98% acetonitrile−0.2% formic acid) over 8 minutes, 30−80% MS buffer B over 3 minutes, 80% MS buffer B for 2 minutes, 80−85% MS buffer B for 3 minutes. MS/MS fragmentation ion scans were calibrated using fragments of Glu-Fibrinopeptide B. MS/MS spectral data was converted to Mascot Generic format using TOF/TOF extractor V2.1 (Michigan Proteome Consortium, 2003).

    .raw files were produced using the following procedure:\n\nLC-MS/MS analysis was undertaken using a nanoAcquity UPLC (Waters, USA) coupled to a XevoQToF (Waters, USA) mass spectrometer. The peptides were washed off the trap at 400 nL/min on to a C18 BEH analytical column (75 μm ´ 100 mm)(Waters, USA), packed with 1.7 μm particles of pore size 130 Å and the following protocol was used to elute peptides from the column into the source of a XevoQToF mass spectrometer (Waters, USA): 1-50% MS buffer B (98% acetonitrile, 0.2% formic acid) over 30 minutes, 50-85% MS Buffer B over 2 minutes, 85% MS buffer B 3 minutes, 85-99% over 1 minute. After separation, the peptides were analysed using tandem mass spectrometry, implementing an emitter tip that tapers to 10 µm at 2300 V. A Data Directed Acquisition (DDA) experiment was performed which continuously scanned for peptides of charge state 2+ to 4+ with an intensity of more than 50 counts per second, with a maximum of three ions in any given 3 second scan.

    The data can be accessed via the related website listed below.
    • - Start
      Data publication title Bovine and feline Tritrichomonas foetus total cellular protein mass spectrometry data files
    • Description

      This is the raw data from Mass Spectrometry analysis of spots resolved using two-dimensional analysis from a total protein sample from Tritrichomonas foetus bovine and feline genotypes. The dataset contains data files generated following the analysis of protein spots using LC-MS/MS.

      There are two types of data files.

      .Wiff files were produced using the following procedure: \n\nLC−MS/MS was performed using a QSTAR Elite hybrid Q-TOF mass spectrometer (Applied Biosystems, Sciex, USA). The peptides were washed off the trap at 300 nL min-1 onto a PicoFrit column (75 μm × 100 mm) (New Objective, USA) packed with Magic C18AQ resin (Michrom Bioresources, USA), and the following protocol was used to elute peptides from the column and into the source of a QSTAR Elite hybrid Q-TOF mass spectrometer (Applied Biosystems, Sciex, USA): 5−30% MS buffer B (98% acetonitrile−0.2% formic acid) over 8 minutes, 30−80% MS buffer B over 3 minutes, 80% MS buffer B for 2 minutes, 80−85% MS buffer B for 3 minutes. MS/MS fragmentation ion scans were calibrated using fragments of Glu-Fibrinopeptide B. MS/MS spectral data was converted to Mascot Generic format using TOF/TOF extractor V2.1 (Michigan Proteome Consortium, 2003).

      .raw files were produced using the following procedure:\n\nLC-MS/MS analysis was undertaken using a nanoAcquity UPLC (Waters, USA) coupled to a XevoQToF (Waters, USA) mass spectrometer. The peptides were washed off the trap at 400 nL/min on to a C18 BEH analytical column (75 μm ´ 100 mm)(Waters, USA), packed with 1.7 μm particles of pore size 130 Å and the following protocol was used to elute peptides from the column into the source of a XevoQToF mass spectrometer (Waters, USA): 1-50% MS buffer B (98% acetonitrile, 0.2% formic acid) over 30 minutes, 50-85% MS Buffer B over 2 minutes, 85% MS buffer B 3 minutes, 85-99% over 1 minute. After separation, the peptides were analysed using tandem mass spectrometry, implementing an emitter tip that tapers to 10 µm at 2300 V. A Data Directed Acquisition (DDA) experiment was performed which continuously scanned for peptides of charge state 2+ to 4+ with an intensity of more than 50 counts per second, with a maximum of three ions in any given 3 second scan.

      The data can be accessed via the related website listed below.
      • Data type dataset
    • Keywords
      • LC-MS/MS data
      • Protozoan parasites
      • host adaptation
      • two-dimensional electrophoresis
      • comparative proteomics
    • Funding source
    • Grant number(s)
      • -
      • FoR codes
      SEO codes
    - Coverage
      Temporal (time) coverage
    • Start date 2014/03/07
    • End date 2014/03/20
      • Time period
       
      Spatial (location,mapping) coverage
    • Locations
    - Data
    - Supplements
    • Related publications
        Name Stroud, L. J., Slapeta, J., Padula, M. P., Druery, D., Tsiotsioras, G., Coorssen, J. R., & Stack, C. M. (2017). Comparative proteomic analysis of two pathogenic Tritrichomonas foetus genotypes : there is more to the proteome than meets the eye. International Journal for Parasitology. doi:10.1016/j.ijpara.2016.11.004
      • URL https://doi.org/10.1016/j.ijpara.2016.11.004
      • Notes
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    - License
      The data will be licensed under CC BY: Attribution 3.0 AU
    • Other license
      • Statement of rights in data Copyright Western Sydney University
    - Citation
      Citation Stroud, Leah (2016): Bovine and feline Tritrichomonas foetus total cellular protein mass spectrometry data files. Western Sydney University.

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