The chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosol
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Author(s)
Spillman, Natalie J.
Beck, Josh R.
Goldberg, Daniel E.
Ganesan, Suresh M.
Niles, Jacquin
Date Issued
May 2017
Journal
Cellular Microbiology
Publisher
Wiley Blackwell
Citation
Spillman, Natalie J. et al. “The Chaperonin TRiC Forms an Oligomeric Complex in the Malaria Parasite Cytosol.” Cellular Microbiology 19, 6 (January 2017): e12719 © 2017 John Wiley & Sons Ltd
Version
Author's final manuscript
Abstract
The malaria parasite exports numerous proteins into its host red blood cell (RBC). The trafficking of these exported effectors is complex. Proteins are first routed through the secretory system, into the parasitophorous vacuole (PV), a membranous compartment enclosing the parasite. Proteins are then translocated across the PV membrane in a process requiring ATP and unfolding. Once in the RBC compartment the exported proteins are then refolded and further trafficked to their final localizations. Chaperones are important in the unfolding and refolding processes. Recently, it was suggested that the parasite TRiC chaperonin complex is exported, and that it is involved in trafficking of exported effectors. Using a parasite-specific antibody and epitope-tagged transgenic parasites we could observe no export of Plasmodium TRiC into the RBC. We tested the importance of the parasite TRiC by creating a regulatable knockdown line of the TRiC-θ subunit. Loss of the parasite TRiC-θ led to a severe growth defect in asexual development, but did not alter protein export into the RBC. These observations indicate that the TRiC proteins play a critical role in parasite biology, though their function, within the parasite, appears unrelated to protein trafficking in the RBC compartment. Keywords: chaperonin; malaria; protein export; regulatable expression; T‐complex protein; TRiC
MIT Department
Massachusetts Institute of Technology. Department of Biological Engineering
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DOI of Published Version
https://doi.org/10.1111/CMI.12719
