Deep proteome coverage advances knowledge of Treponema pallidum protein expression profiles during infection.


Journal

Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288

Informations de publication

Date de publication:
25 10 2023
Historique:
received: 19 06 2023
accepted: 17 10 2023
medline: 27 10 2023
pubmed: 26 10 2023
entrez: 25 10 2023
Statut: epublish

Résumé

Comprehensive proteome-wide analysis of the syphilis spirochete, Treponema pallidum ssp. pallidum, is technically challenging due to high sample complexity, difficulties with obtaining sufficient quantities of bacteria for analysis, and the inherent fragility of the T. pallidum cell envelope which further complicates proteomic identification of rare T. pallidum outer membrane proteins (OMPs). The main aim of the present study was to gain a deeper understanding of the T. pallidum global proteome expression profile under infection conditions. This will corroborate and extend genome annotations, identify protein modifications that are unable to be predicted at the genomic or transcriptomic levels, and provide a foundational knowledge of the T. pallidum protein expression repertoire. Here we describe the optimization of a T. pallidum-specific sample preparation workflow and mass spectrometry-based proteomics pipeline which allowed for the detection of 77% of the T. pallidum protein repertoire under infection conditions. When combined with prior studies, this brings the overall coverage of the T. pallidum proteome to almost 90%. These investigations identified 27 known/predicted OMPs, including potential vaccine candidates, and detected expression of 11 potential OMPs under infection conditions for the first time. The optimized pipeline provides a robust and reproducible workflow for investigating T. pallidum protein expression during infection. Importantly, the combined results provide the deepest coverage of the T. pallidum proteome to date.

Identifiants

pubmed: 37880309
doi: 10.1038/s41598-023-45219-8
pii: 10.1038/s41598-023-45219-8
pmc: PMC10600179
doi:

Substances chimiques

Proteome 0
Bacterial Proteins 0

Types de publication

Journal Article Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

18259

Subventions

Organisme : NIAID NIH HHS
ID : R37 AI051334
Pays : United States
Organisme : NIAID NIH HHS
ID : U19 AI144133
Pays : United States
Organisme : NIH HHS
ID : R37AI051334
Pays : United States

Informations de copyright

© 2023. Springer Nature Limited.

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Auteurs

Simon Houston (S)

Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC, Canada.

Alloysius Gomez (A)

Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC, Canada.

Andrew Geppert (A)

Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC, Canada.

Azad Eshghi (A)

University of Victoria-Genome BC Proteomics Centre, University of Victoria, Victoria, BC, Canada.

Derek S Smith (DS)

University of Victoria-Genome BC Proteomics Centre, University of Victoria, Victoria, BC, Canada.

Sean Waugh (S)

Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC, Canada.

Darryl B Hardie (DB)

University of Victoria-Genome BC Proteomics Centre, University of Victoria, Victoria, BC, Canada.

David R Goodlett (DR)

Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC, Canada.
University of Victoria-Genome BC Proteomics Centre, University of Victoria, Victoria, BC, Canada.

Caroline E Cameron (CE)

Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC, Canada. caroc@uvic.ca.
Division of Allergy and Infectious Diseases, Department of Medicine, University of Washington, Seattle, WA, USA. caroc@uvic.ca.

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