The Toxoplasma gondii active serine hydrolase 4 regulates parasite division and intravacuolar parasite architecture

Ian T. Foe, Ouma Onguka, Katherine Amberg-Johnson, Rikki M. Garner, Neri Amara, Wandy Beatty, Ellen Yeh, Matthew Bogyo

Research output: Contribution to journalArticlepeer-review

5 Scopus citations

Abstract

Hydrolase are enzymes that regulate diverse biological processes, including posttranslational protein modifications. Recent work identified four active serine hydrolases (ASHs) in Toxoplasma gondii as candidate depalmitoylases. However, only TgPPT1 (ASH1) has been confirmed to remove palmitate from proteins. ASH4 (TgME49_264290) was reported to be refractory to genetic disruption. We demonstrate that recombinant ASH4 is an esterase that processes short acyl esters but not palmitoyl thioesters. Genetic disruption of ASH4 causes defects in cell division and premature scission of parasites from residual bodies. These defects lead to the presence of vacuoles with a disordered intravacuolar architecture, with parasites arranged in pairs around multiple residual bodies. Importantly, we found that the deletion of ASH4 correlates with a defect in radial dispersion from host cells after egress. This defect in dispersion of parasites is a general phenomenon that is observed for disordered vacuoles that occur at low frequency in wild-type parasites, suggesting a possible general link between intravacuolar organization and dispersion after egress.

Original languageEnglish
Article numbere00393-18
JournalmSphere
Volume3
Issue number5
DOIs
StatePublished - Sep 1 2018

Keywords

  • ASH proteins
  • Cell division
  • Intravacuolar organization
  • Serine hydrolase

Fingerprint

Dive into the research topics of 'The Toxoplasma gondii active serine hydrolase 4 regulates parasite division and intravacuolar parasite architecture'. Together they form a unique fingerprint.

Cite this