Characterizing the syphilis-causing Treponema pallidum ssp. pallidum proteome using complementary mass spectrometry

dc.contributor.authorOsbak, Kara Ken_ZA
dc.contributor.authorHouston, Simonen_ZA
dc.contributor.authorLithgow, Karen Ven_ZA
dc.contributor.authorMeehan, Conor Jen_ZA
dc.contributor.authorStrouhal, Michalen_ZA
dc.contributor.authorŠmajs, Daviden_ZA
dc.contributor.authorCameron, Caroline Een_ZA
dc.contributor.authorVan Ostade, Xaveeren_ZA
dc.contributor.authorKenyon, Chris Ren_ZA
dc.contributor.authorVan Raemdonck, Geert Aen_ZA
dc.date.accessioned2016-10-31T07:38:04Z
dc.date.available2016-10-31T07:38:04Z
dc.date.issued2016en_ZA
dc.description.abstractAuthor Summary: Syphilis remains a major cause of morbidity and mortality worldwide. The bacterium causing syphilis, Treponema pallidum ssp. pallidum , has evolved into a highly distinctive organism that is only able survive (and be propagated) in mammals. In humans it can evade the immune system for decades with devastating consequences. Much remains to be learned about how it accomplishes this. Only a minority of its predicted proteins have been detected experimentally thus far. We aimed to more comprehensively characterize the proteins of this organism. Since it cannot be cultured in vitro , we cultured T . pallidum in rabbits and analyzed extracted proteins using different mass spectrometry methods, a manner of detecting proteins with high accuracy. In total, we detected more than half of the predicted number of proteins that could be expressed by this bacterium (N = 557). For approximately half of the proteins, we succeeded in characterizing their predicted cellular location using an array of bioinformatic tools and catalogued their function. This is the most comprehensive analysis of the T . pallidum proteome to date. This study lays the groundwork for other protein investigations of this unique organism.en_ZA
dc.identifier.apacitationOsbak, K. K., Houston, S., Lithgow, K. V., Meehan, C. J., Strouhal, M., Šmajs, D., ... Van Raemdonck, G. A. (2016). Characterizing the syphilis-causing Treponema pallidum ssp. pallidum proteome using complementary mass spectrometry. <i>PLOS Neglected Tropical Diseases</i>, http://hdl.handle.net/11427/22355en_ZA
dc.identifier.chicagocitationOsbak, 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." <i>PLOS Neglected Tropical Diseases</i> (2016) http://hdl.handle.net/11427/22355en_ZA
dc.identifier.citationOsbak, K. K., Houston, S., Lithgow, K. V., Meehan, C. J., Strouhal, M., Šmajs, D., ... & Van Raemdonck, G. A. (2016). Characterizing the syphilis-causing Treponema pallidum ssp. pallidum proteome using complementary mass spectrometry. PLoS Negl Trop Dis, 10(9), e0004988. doi:10.1371/journal.pntd.0004988en_ZA
dc.identifier.ris TY - Journal Article AU - Osbak, Kara K AU - Houston, Simon AU - Lithgow, Karen V AU - Meehan, Conor J AU - Strouhal, Michal AU - Šmajs, David AU - Cameron, Caroline E AU - Van Ostade, Xaveer AU - Kenyon, Chris R AU - Van Raemdonck, Geert A AB - Author Summary: Syphilis remains a major cause of morbidity and mortality worldwide. The bacterium causing syphilis, Treponema pallidum ssp. pallidum , has evolved into a highly distinctive organism that is only able survive (and be propagated) in mammals. In humans it can evade the immune system for decades with devastating consequences. Much remains to be learned about how it accomplishes this. Only a minority of its predicted proteins have been detected experimentally thus far. We aimed to more comprehensively characterize the proteins of this organism. Since it cannot be cultured in vitro , we cultured T . pallidum in rabbits and analyzed extracted proteins using different mass spectrometry methods, a manner of detecting proteins with high accuracy. In total, we detected more than half of the predicted number of proteins that could be expressed by this bacterium (N = 557). For approximately half of the proteins, we succeeded in characterizing their predicted cellular location using an array of bioinformatic tools and catalogued their function. This is the most comprehensive analysis of the T . pallidum proteome to date. This study lays the groundwork for other protein investigations of this unique organism. DA - 2016 DB - OpenUCT DO - 10.1371/journal.pntd.0004988 DP - University of Cape Town J1 - PLOS Neglected Tropical Diseases LK - https://open.uct.ac.za PB - University of Cape Town PY - 2016 T1 - Characterizing the syphilis-causing Treponema pallidum ssp. pallidum proteome using complementary mass spectrometry TI - Characterizing the syphilis-causing Treponema pallidum ssp. pallidum proteome using complementary mass spectrometry UR - http://hdl.handle.net/11427/22355 ER - en_ZA
dc.identifier.urihttp://dx.doi.org/10.1371/journal.pntd.0004988en_ZA
dc.identifier.urihttp://hdl.handle.net/11427/22355
dc.identifier.vancouvercitationOsbak KK, Houston S, Lithgow KV, Meehan CJ, Strouhal M, Šmajs D, et al. Characterizing the syphilis-causing Treponema pallidum ssp. pallidum proteome using complementary mass spectrometry. PLOS Neglected Tropical Diseases. 2016; http://hdl.handle.net/11427/22355.en_ZA
dc.language.isoengen_ZA
dc.publisherPublic Library of Scienceen_ZA
dc.publisher.departmentInstitute of Infectious Disease and Molecular Medicineen_ZA
dc.publisher.facultyFaculty of Health Sciencesen_ZA
dc.publisher.institutionUniversity of Cape Town
dc.rightsThis is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.en_ZA
dc.rights.holder© 2016 Osbak et alen_ZA
dc.rights.urihttp://creativecommons.org/licenses/by/4.0en_ZA
dc.sourcePLOS Neglected Tropical Diseasesen_ZA
dc.source.urihttp://journals.plos.org/plosntdsen_ZA
dc.subject.otherTreponema pallidumen_ZA
dc.subject.otherOuter membrane proteinsen_ZA
dc.subject.otherProteomesen_ZA
dc.subject.otherPeptidesen_ZA
dc.subject.otherChaperone proteinsen_ZA
dc.subject.otherIntegral membrane proteinsen_ZA
dc.subject.otherMembrane proteinsen_ZA
dc.subject.otherRabbitsen_ZA
dc.titleCharacterizing the syphilis-causing Treponema pallidum ssp. pallidum proteome using complementary mass spectrometryen_ZA
dc.typeJournal Articleen_ZA
uct.type.filetypeText
uct.type.filetypeImage
uct.type.publicationResearchen_ZA
uct.type.resourceArticleen_ZA
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