Detailed Information on Publication Record
2016
Characterizing the Syphilis-Causing Treponema pallidum ssp pallidum Proteome Using Complementary Mass Spectrometry
OSBAK, Kara K., Simon HOUSTON, Karen V. LITHGOW, Conor J. MEEHAN, Michal STROUHAL et. al.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
Language
English
Type of outcome
Článek v odborném periodiku
Field of Study
30300 3.3 Health sciences
Country of publisher
United States of America
Confidentiality degree
není předmětem státního či obchodního tajemství
Impact factor
Impact factor: 3.834
RIV identification code
RIV/00216224:14110/16:00088426
Organization unit
Faculty of Medicine
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
Tags
International impact, Reviewed
Změněno: 8/12/2016 14:35, Ing. Mgr. Věra Pospíšilíková
Abstract
V originále
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 project |
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| GP14-29596P, research and development project |
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