In-Depth Proteome Coverage of In Vitro-Cultured Treponema pallidum and Quantitative Comparison Analyses with In Vivo-Grown Treponemes.
Simon HoustonAlloysius GomezAndrew GeppertMara C GoodyearCaroline E CameronPublished in: Journal of proteome research (2024)
Previous 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).
Keyphrases
- mass spectrometry
- liquid chromatography
- multiple sclerosis
- high resolution
- endothelial cells
- ms ms
- high performance liquid chromatography
- gas chromatography
- electronic health record
- capillary electrophoresis
- healthcare
- affordable care act
- label free
- machine learning
- protein protein
- dna methylation
- high throughput sequencing