Houston, SimonGomez, AlloysiusGeppert, AndrewGoodyear, Mara C.Cameron, Caroline E.2026-05-072026-05-072024Houston, S., Gomez, A., Geppert, A., Goodyear, M. C., & Cameron, C. E. (2024). In-depth proteome coverage of in vitro-cultured Treponema pallidum and quantitative comparison analyses with in vivo-grown treponemes. Journal of Proteome Research, 23(5), 1725–1743. https://doi.org/10.1021/acs.jproteome.3c00891https://doi.org/10.1021/acs.jproteome.3c00891https://hdl.handle.net/1828/23856Previous mass spectrometry (MS)-based global proteomics studies have detected a combined total of 86% of all Treponema pallidum proteins under infection conditions (in vivo-grown T. pallidum). Recently, a method was developed for the long-term culture of T. pallidum under in vitro conditions (in vitro-cultured T. pallidum). Herein, we used our previously reported optimized MS-based proteomics approach to characterize the T. pallidum global protein expression profile under in vitro culture conditions. These analyses provided a proteome coverage of 94%, which extends the combined T. pallidum proteome coverage from the previously reported 86% to a new combined total of 95%. This study provides a more complete understanding of the protein repertoire of T. pallidum. Further, comparison of the in vitro-expressed proteome with the previously determined in vivo-expressed proteome identifies only a few proteomic changes between the two growth conditions, reinforcing the suitability of in vitro-cultured T. pallidum as an alternative to rabbit-based treponemal growth. The MS proteomics data have been deposited in the MassIVE repository with the data set identifier MSV000093603 (ProteomeXchange identifier PXD047625).enCC BY-NC-NDTreponema pallidumsyphilisglobal proteomicsmass spectrometry (MS)protein expression profileouter membrane proteinsvaccine candidatesSexual and Reproductive Health and Rights (SRHR) Aspiration Research ClusterArticleDepartment of Biochemistry and Microbiology