OSBAK, Kara K., Simon HOUSTON, Karen V. LITHGOW, Conor J. MEEHAN, Michal STROUHAL, David ŠMAJS, Caroline E. CAMERON, Xaveer Van OSTADE, Chris R. KENYON and Geert A. Van RAEMDONCK. Characterizing the Syphilis-Causing Treponema pallidum ssp pallidum Proteome Using Complementary Mass Spectrometry. PLoS neglected tropical diseases. San Francisco: Public Library of Science, vol. 10, No 9, p. 1-29. ISSN 1935-2735. doi:10.1371/journal.pntd.0004988. 2016.
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Basic information
Original name Characterizing the Syphilis-Causing Treponema pallidum ssp pallidum Proteome Using Complementary Mass Spectrometry
Authors OSBAK, Kara K. (56 Belgium), Simon HOUSTON (124 Canada), Karen V. LITHGOW (124 Canada), Conor J. MEEHAN (56 Belgium), Michal STROUHAL (203 Czech Republic, belonging to the institution), David ŠMAJS (203 Czech Republic, guarantor, belonging to the institution), Caroline E. CAMERON (124 Canada), Xaveer Van OSTADE (56 Belgium), Chris R. KENYON (56 Belgium) and Geert A. Van RAEMDONCK (56 Belgium).
Edition PLoS neglected tropical diseases, San Francisco, Public Library of Science, 2016, 1935-2735.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 30300 3.3 Health sciences
Country of publisher United States of America
Confidentiality degree is not subject to a state or trade secret
Impact factor Impact factor: 3.834
RIV identification code RIV/00216224:14110/16:00088426
Organization unit Faculty of Medicine
Doi http://dx.doi.org/10.1371/journal.pntd.0004988
UT WoS 000385627900043
Keywords in English 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
Tags EL OK
Tags International impact, Reviewed
Changed by Changed by: Ing. Mgr. Věra Pospíšilíková, učo 9005. Changed: 8/12/2016 14:35.
Abstract
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.
Links
GAP302/12/0574, research and development projectName: Celogenomové sekvencování v analýze genomů a transkriptomů patogenních bakterií rodu Treponema
Investor: Czech Science Foundation
GP14-29596P, research and development projectName: Genomová variabilita treponem během experimentální infekce
Investor: Czech Science Foundation
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