Maturation and substrate processing topography of the Plasmodium falciparum invasion/egress protease plasmepsin X

Egress of Plasmodium from host erythrocytes is mediated by effector proteins. Aspartic protease plasmepsin X (PM X) regulates the activity for many of these effectors, is essential for replication and is a promising drug target. Here, Mukherjee et al. map the self-cleavage sites of PM X, show that t...

Full description

Bibliographic Details
Main Authors: Sumit Mukherjee, Suong Nguyen, Eashan Sharma, Daniel E. Goldberg
Format: Article
Language:English
Published: Nature Portfolio 2022-08-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-022-32271-7
_version_ 1811315386092617728
author Sumit Mukherjee
Suong Nguyen
Eashan Sharma
Daniel E. Goldberg
author_facet Sumit Mukherjee
Suong Nguyen
Eashan Sharma
Daniel E. Goldberg
author_sort Sumit Mukherjee
collection DOAJ
description Egress of Plasmodium from host erythrocytes is mediated by effector proteins. Aspartic protease plasmepsin X (PM X) regulates the activity for many of these effectors, is essential for replication and is a promising drug target. Here, Mukherjee et al. map the self-cleavage sites of PM X, show that the N-terminal part of its prodomain is required for intracellular trafficking and correlate the maturation and subcellular activity of PM X in microneme, exoneme and rhoptry organelle function.
first_indexed 2024-04-13T11:29:23Z
format Article
id doaj.art-25ea7224dd2341d39f04aceddad87f86
institution Directory Open Access Journal
issn 2041-1723
language English
last_indexed 2024-04-13T11:29:23Z
publishDate 2022-08-01
publisher Nature Portfolio
record_format Article
series Nature Communications
spelling doaj.art-25ea7224dd2341d39f04aceddad87f862022-12-22T02:48:36ZengNature PortfolioNature Communications2041-17232022-08-0113111410.1038/s41467-022-32271-7Maturation and substrate processing topography of the Plasmodium falciparum invasion/egress protease plasmepsin XSumit Mukherjee0Suong Nguyen1Eashan Sharma2Daniel E. Goldberg3Division of Infectious Diseases, Department of Medicine, and Department of Molecular Microbiology, Washington University School of MedicineDivision of Infectious Diseases, Department of Medicine, and Department of Molecular Microbiology, Washington University School of MedicineDivision of Infectious Diseases, Department of Medicine, and Department of Molecular Microbiology, Washington University School of MedicineDivision of Infectious Diseases, Department of Medicine, and Department of Molecular Microbiology, Washington University School of MedicineEgress of Plasmodium from host erythrocytes is mediated by effector proteins. Aspartic protease plasmepsin X (PM X) regulates the activity for many of these effectors, is essential for replication and is a promising drug target. Here, Mukherjee et al. map the self-cleavage sites of PM X, show that the N-terminal part of its prodomain is required for intracellular trafficking and correlate the maturation and subcellular activity of PM X in microneme, exoneme and rhoptry organelle function.https://doi.org/10.1038/s41467-022-32271-7
spellingShingle Sumit Mukherjee
Suong Nguyen
Eashan Sharma
Daniel E. Goldberg
Maturation and substrate processing topography of the Plasmodium falciparum invasion/egress protease plasmepsin X
Nature Communications
title Maturation and substrate processing topography of the Plasmodium falciparum invasion/egress protease plasmepsin X
title_full Maturation and substrate processing topography of the Plasmodium falciparum invasion/egress protease plasmepsin X
title_fullStr Maturation and substrate processing topography of the Plasmodium falciparum invasion/egress protease plasmepsin X
title_full_unstemmed Maturation and substrate processing topography of the Plasmodium falciparum invasion/egress protease plasmepsin X
title_short Maturation and substrate processing topography of the Plasmodium falciparum invasion/egress protease plasmepsin X
title_sort maturation and substrate processing topography of the plasmodium falciparum invasion egress protease plasmepsin x
url https://doi.org/10.1038/s41467-022-32271-7
work_keys_str_mv AT sumitmukherjee maturationandsubstrateprocessingtopographyoftheplasmodiumfalciparuminvasionegressproteaseplasmepsinx
AT suongnguyen maturationandsubstrateprocessingtopographyoftheplasmodiumfalciparuminvasionegressproteaseplasmepsinx
AT eashansharma maturationandsubstrateprocessingtopographyoftheplasmodiumfalciparuminvasionegressproteaseplasmepsinx
AT danielegoldberg maturationandsubstrateprocessingtopographyoftheplasmodiumfalciparuminvasionegressproteaseplasmepsinx