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@article{1364062,
author = {Osbak, Kara K. and Houston, Simon and Lithgow, Karen V. and Meehan, Conor J. and Strouhal, Michal and Šmajs, David and Cameron, Caroline E. and Ostade, Xaveer Van and Kenyon, Chris R. and Raemdonck, Geert A. Van},
article_location = {San Francisco},
article_number = {9},
doi = {http://dx.doi.org/10.1371/journal.pntd.0004988},
keywords = {OUTER-MEMBRANE PROTEINS; PENICILLIN-BINDING PROTEIN; GRAM-NEGATIVE BACTERIA; GENOME-SCALE IDENTIFICATION; BARREL ASSEMBLY MACHINERY; SUBSP PALLIDUM; MOONLIGHTING PROTEINS; ANTIGENIC VARIATION; SIGNAL PEPTIDES; SUBCELLULAR-LOCALIZATION},
language = {eng},
issn = {1935-2735},
journal = {PLoS neglected tropical diseases},
title = {Characterizing the Syphilis-Causing Treponema pallidum ssp pallidum Proteome Using Complementary Mass Spectrometry},
volume = {10},
year = {2016}
}
TY - JOUR
ID - 1364062
AU - Osbak, Kara K. - Houston, Simon - Lithgow, Karen V. - Meehan, Conor J. - Strouhal, Michal - Šmajs, David - Cameron, Caroline E. - Ostade, Xaveer Van - Kenyon, Chris R. - Raemdonck, Geert A. Van
PY - 2016
TI - Characterizing the Syphilis-Causing Treponema pallidum ssp pallidum Proteome Using Complementary Mass Spectrometry
JF - PLoS neglected tropical diseases
VL - 10
IS - 9
SP - 1-29
EP - 1-29
PB - Public Library of Science
SN - 19352735
KW - OUTER-MEMBRANE PROTEINS
KW - PENICILLIN-BINDING PROTEIN
KW - GRAM-NEGATIVE BACTERIA
KW - GENOME-SCALE IDENTIFICATION
KW - BARREL ASSEMBLY MACHINERY
KW - SUBSP PALLIDUM
KW - MOONLIGHTING PROTEINS
KW - ANTIGENIC VARIATION
KW - SIGNAL PEPTIDES
KW - SUBCELLULAR-LOCALIZATION
N2 - Background The 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 Findings 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. 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. Conclusions This 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.
ER -
OSBAK, Kara K., Simon HOUSTON, Karen V. LITHGOW, Conor J. MEEHAN, Michal STROUHAL, David ŠMAJS, Caroline E. CAMERON, Xaveer Van OSTADE, Chris R. KENYON a Geert A. Van RAEMDONCK. Characterizing the Syphilis-Causing Treponema pallidum ssp pallidum Proteome Using Complementary Mass Spectrometry. \textit{PLoS neglected tropical diseases}. San Francisco: Public Library of Science, roč.~10, č.~9, s.~1-29. ISSN~1935-2735. doi:10.1371/journal.pntd.0004988. 2016.
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