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...
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Format: | Article |
Language: | English |
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Nature Portfolio
2022-08-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-022-32271-7 |
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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 |
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