Phosphoproteomic analysis of mammalian infective Trypanosoma brucei subjected to heat shock suggests atypical mechanisms for thermotolerance

CHER-PHENG OOI, Corinna Benz, Michael D. Urbaniak

Research output: Contribution to journalArticle

Abstract

The symptoms of African sleeping sickness, caused by the parasite Trypanosoma brucei, can include periods of fever as high as 41 °C which triggers a heat shock response in the parasite. To capture events involved in sensing and responding to heat shock in the mammalian infective form we have conducted a SILAC-based quantitative proteomic and phosphoproteomic analysis of T. brucei cells treated at 41 °C for 1h. Our analysis identified 193 heat shock responsive phosphorylation sites with an average of 5-fold change in abundance, but only 20 heat shock responsive proteins with average of 1.5-fold change. These data indicate that protein abundance does not rapidly respond (≤1 h) to heat shock, and that the changes observed in phosphorylation site abundance are larger and more widespread. The heat shock responsive phosphorylation sites showed enrichment of RNA binding proteins with putative roles in heat shock response included P-body / stress granules and the eukaryotic translation initiation 4F complex. The ZC3H11-MKT1 complex, which stabilises mRNAs of thermotolerance proteins, appears to represent a key signal integration node in the heat shock response.
Original languageEnglish
Article number103735
JournalJournal of Proteomics
Volume219
Early online date19 Mar 2020
DOIs
Publication statusPublished - 15 May 2020

Keywords

  • African sleeping sickness
  • Trypanosoma brucei
  • heat shock
  • SILAC
  • phosphoproteomics

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    CHER-PHENG OOI, PhD

    • Biology - Senior Lecturer in Microbiology

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