Abstract
BackgroundThe spirochete bacterium Treponema pallidum ssp. pallidum is the etiological agent of syphilis, a chronic multistage disease. Little is known about the global T. pallidum proteome, therefore mass spectrometry studies are needed to bring insights into pathogenicity and protein expression profiles during infection.Methodology/Principal FindingsTo better understand the T. pallidum proteome profile during infection, we studied T. pallidum ssp. pallidum DAL-1 strain bacteria isolated from rabbits using complementary mass spectrometry techniques, including multidimensional peptide separation and protein identification via matrix-assisted laser desorption ionization-time of flight (MALDI-TOF/TOF) and electrospray ionization (ESI-LTQ-Orbitrap) tandem mass spectrometry. A total of 6033 peptides were detected, corresponding to 557 unique T. pallidum proteins at a high level of confidence, representing 54% of the predicted proteome. A previous gel-based T. pallidum MS proteome study detected 58 of these proteins. One hundred fourteen of the detected proteins were previously annotated as hypothetical or uncharacterized proteins; this is the first account of 106 of these proteins at the protein level. Detected proteins were characterized according to their predicted biological function and localization; half were allocated into a wide range of functional categories. Proteins annotated as potential membrane proteins and proteins with unclear functional annotations were subjected to an additional bioinformatics pipeline analysis to facilitate further characterization. A total of 116 potential membrane proteins were identified, of which 16 have evidence supporting outer membrane localization. We found 8/12 proteins related to the paralogous tpr gene family: TprB, TprC/D, TprE, TprG, TprH, TprI and TprJ. Protein abundance was semi-quantified using label-free spectral counting methods. A low correlation (r = 0.26) was found between previous microarray signal data and protein abundance.ConclusionsThis is the most comprehensive description of the global T. pallidum proteome to date. These data provide valuable insights into in vivo T. pallidum protein expression, paving the way for improved understanding of the pathogenicity of this enigmatic organism.
Highlights
Treponema pallium ssp. pallidum, referred to as T. pallidum, is the causative agent of syphilis, a multistage chronic disease with an estimated 8 million new cases per year [1]
To better understand the T. pallidum proteome profile during infection, we studied T. pallidum ssp. pallidum DAL-1 strain bacteria isolated from rabbits using complementary mass spectrometry techniques, including multidimensional peptide separation and protein identification via matrix-assisted laser desorption ionization-time of flight (MALDI-TOF/TOF) and electrospray ionization (ESI-LTQ-Orbitrap) tandem mass spectrometry
From the three biological replicates, a total of 6033 T. pallidum peptides were detected corresponding to 557 proteins and 54% of the total predicted proteome (S1 Table)
Summary
Treponema pallium ssp. pallidum, referred to as T. pallidum, is the causative agent of syphilis, a multistage chronic disease with an estimated 8 million new cases per year [1]. Many biomedical experimental approaches such as genetic manipulation have been hampered by its lack of in vitro cultivability [12]. Despite these limitations, numerous studies using T. pallidum harvested from the experimental rabbit model have increased our basic biological understanding of this unique organism, including the description of the genome [13,14], transcriptome [15] and proteome [16,17]. Pallidum is the etiological agent of syphilis, a chronic multistage disease. Little is known about the global T. pallidum proteome, mass spectrometry studies are needed to bring insights into pathogenicity and protein expression profiles during infection
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