In:
PLOS Pathogens, Public Library of Science (PLoS), Vol. 19, No. 7 ( 2023-7-31), p. e1011006-
Abstract:
A key element of Plasmodium biology and pathogenesis is the trafficking of ~10% of the parasite proteome into the host red blood cell (RBC) it infects. To cross the parasite-encasing parasitophorous vacuole membrane, exported proteins utilise a channel-forming protein complex termed the Plasmodium translocon of exported proteins (PTEX). PTEX is obligatory for parasite survival, both in vitro and in vivo , suggesting that at least some exported proteins have essential metabolic functions. However, to date only one essential PTEX-dependent process, the new permeability pathways, has been described. To identify other essential PTEX-dependant proteins/processes, we conditionally knocked down the expression of one of its core components, PTEX150, and examined which pathways were affected. Surprisingly, the food vacuole mediated process of haemoglobin (Hb) digestion was substantially perturbed by PTEX150 knockdown. Using a range of transgenic parasite lines and approaches, we show that two major Hb proteases; falcipain 2a and plasmepsin II, interact with PTEX core components, implicating the translocon in the trafficking of Hb proteases. We propose a model where these proteases are translocated into the PV via PTEX in order to reach the cytostome, located at the parasite periphery, prior to food vacuole entry. This work offers a second mechanistic explanation for why PTEX function is essential for growth of the parasite within its host RBC.
Type of Medium:
Online Resource
ISSN:
1553-7374
DOI:
10.1371/journal.ppat.1011006
DOI:
10.1371/journal.ppat.1011006.g001
DOI:
10.1371/journal.ppat.1011006.g002
DOI:
10.1371/journal.ppat.1011006.g003
DOI:
10.1371/journal.ppat.1011006.g004
DOI:
10.1371/journal.ppat.1011006.g005
DOI:
10.1371/journal.ppat.1011006.g006
DOI:
10.1371/journal.ppat.1011006.g007
DOI:
10.1371/journal.ppat.1011006.g008
DOI:
10.1371/journal.ppat.1011006.s001
DOI:
10.1371/journal.ppat.1011006.s002
DOI:
10.1371/journal.ppat.1011006.s003
DOI:
10.1371/journal.ppat.1011006.s004
DOI:
10.1371/journal.ppat.1011006.s005
DOI:
10.1371/journal.ppat.1011006.s006
DOI:
10.1371/journal.ppat.1011006.s007
DOI:
10.1371/journal.ppat.1011006.s008
DOI:
10.1371/journal.ppat.1011006.s009
DOI:
10.1371/journal.ppat.1011006.s010
DOI:
10.1371/journal.ppat.1011006.s011
DOI:
10.1371/journal.ppat.1011006.s012
DOI:
10.1371/journal.ppat.1011006.s013
DOI:
10.1371/journal.ppat.1011006.s014
DOI:
10.1371/journal.ppat.1011006.s015
DOI:
10.1371/journal.ppat.1011006.s016
DOI:
10.1371/journal.ppat.1011006.s017
DOI:
10.1371/journal.ppat.1011006.s018
DOI:
10.1371/journal.ppat.1011006.s019
DOI:
10.1371/journal.ppat.1011006.s020
DOI:
10.1371/journal.ppat.1011006.s021
DOI:
10.1371/journal.ppat.1011006.s022
DOI:
10.1371/journal.ppat.1011006.s023
DOI:
10.1371/journal.ppat.1011006.s024
Language:
English
Publisher:
Public Library of Science (PLoS)
Publication Date:
2023
detail.hit.zdb_id:
2205412-1
Bookmarklink