The chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosol.

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 obser

SUBMITTER: Spillman NJ 

PROVIDER: S-EPMC5429184 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature