Shift in vacuolar to cytosolic regime of infecting Salmonella from a dual proteome perspective

PLoS Pathog. 2023 Aug 3;19(8):e1011183. doi: 10.1371/journal.ppat.1011183. eCollection 2023 Aug.

Abstract

By applying dual proteome profiling to Salmonella enterica serovar Typhimurium (S. Typhimurium) encounters with its epithelial host (here, S. Typhimurium infected human HeLa cells), a detailed interdependent and holistic proteomic perspective on host-pathogen interactions over the time course of infection was obtained. Data-independent acquisition (DIA)-based proteomics was found to outperform data-dependent acquisition (DDA) workflows, especially in identifying the downregulated bacterial proteome response during infection progression by permitting quantification of low abundant bacterial proteins at early times of infection when bacterial infection load is low. S. Typhimurium invasion and replication specific proteomic signatures in epithelial cells revealed interdependent host/pathogen specific responses besides pointing to putative novel infection markers and signalling responses, including regulated host proteins associated with Salmonella-modified membranes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / metabolism
  • Epithelial Cells / metabolism
  • HeLa Cells
  • Humans
  • Proteome* / metabolism
  • Proteomics*
  • Salmonella typhimurium / physiology

Substances

  • Proteome
  • Bacterial Proteins

Grants and funding

This work was supported by the European Research Council (ERC) under the European Union's Horizon 2020 research and innovation program (PROPHECY grant agreement No 803972) to PVD, the Fonds Wetenschappelijk Onderzoek (FWO-Vlaanderen) (project number G051120N) to PVD, and by Ghent University Concerted Research Actions (grant BOF23/GOA/001) to PVD and (grant BOF14/GOA/013) to KG. PW and MDM authors received a salary from the PROPHECY grant. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.