EXP1 is required for organisation of EXP2 in the intraerythrocytic malaria parasite vacuole.
Plasmodium falciparum
BioID2
Cpf1/Cas12a
EXP1
EXP2
parasitophorous vacuole
Journal
Cellular microbiology
ISSN: 1462-5822
Titre abrégé: Cell Microbiol
Pays: India
ID NLM: 100883691
Informations de publication
Date de publication:
05 2020
05 2020
Historique:
received:
30
08
2019
revised:
04
12
2019
accepted:
07
01
2020
pubmed:
29
1
2020
medline:
3
6
2021
entrez:
29
1
2020
Statut:
ppublish
Résumé
Intraerythrocytic malaria parasites reside within a parasitophorous vacuole membrane (PVM) that closely overlays the parasite plasma membrane. Although the PVM is the site of several transport activities essential to parasite survival, the basis for organisation of this membrane system is unknown. Here, we performed proximity labeling at the PVM with BioID2, which highlighted a group of single-pass integral membrane proteins that constitute a major component of the PVM proteome but whose function remains unclear. We investigated EXP1, the longest known member of this group, by adapting a CRISPR/Cpf1 genome editing system to install the TetR-DOZI-aptamers system for conditional translational control. Importantly, although EXP1 was required for intraerythrocytic development, a previously reported in vitro glutathione S-transferase activity could not account for this essential EXP1 function in vivo. EXP1 knockdown was accompanied by profound changes in vacuole ultrastructure, including apparent increased separation of the PVM from the parasite plasma membrane and formation of abnormal membrane structures. Furthermore, although activity of the Plasmodium translocon of exported proteins was not impacted by depletion of EXP1, the distribution of the translocon pore-forming protein EXP2 but not the HSP101 unfoldase was substantially altered. Collectively, our results reveal a novel PVM defect that indicates a critical role for EXP1 in maintaining proper organisation of EXP2 within the PVM.
Identifiants
pubmed: 31990132
doi: 10.1111/cmi.13168
pmc: PMC7138706
mid: NIHMS1551704
doi:
Substances chimiques
Antigens, Protozoan
0
Membrane Proteins
0
Protozoan Proteins
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
e13168Subventions
Organisme : NHLBI NIH HHS
ID : K99 HL133453
Pays : United States
Organisme : NHLBI NIH HHS
ID : R00 HL133453
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM089778
Pays : United States
Informations de copyright
© 2020 John Wiley & Sons Ltd.
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