Characterization of the malaria parasite Plasmodium falciparum Tepsin homolog
ABSTRACT Plasmodium parasites rely on the invasion of human erythrocytes for their survival. This invasion process is facilitated by specialized organelles (rhoptry, micronemes, and dense granules) housed within a distinctive structure known as the apical complex. How the apical complex is generated...
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American Society for Microbiology
2025-08-01
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| Series: | Microbiology Spectrum |
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| Online Access: | https://journals.asm.org/doi/10.1128/spectrum.03288-24 |
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| author | Stéphanie Roucheray Maria R. Narciso Dave Richard |
| author_facet | Stéphanie Roucheray Maria R. Narciso Dave Richard |
| author_sort | Stéphanie Roucheray |
| collection | DOAJ |
| description | ABSTRACT Plasmodium parasites rely on the invasion of human erythrocytes for their survival. This invasion process is facilitated by specialized organelles (rhoptry, micronemes, and dense granules) housed within a distinctive structure known as the apical complex. How the apical complex is generated is still enigmatic, especially how specificity is achieved in the vesicular trafficking between the Golgi apparatus and the apical organelles, but phosphoinositide lipids might potentially be involved. Here, we describe the characterization of a putative phosphoinositide-binding protein containing an Epsin NH2-terminal homology (ENTH) domain, Pf3D7_1459600. We show that this protein is structurally homologous to human Tepsin. Surprisingly, unlike other Tepsins, the ENTH domain of PfTepsin binds non-specifically to phosphoinositides in vitro, potentially through a positively charged pocket. Colocalization assays revealed that PfTepsin potentially transits between the Golgi apparatus and some of the apical organelles in developing schizonts. Finally, we provide evidence that PfTepsin potentially interacts with members of the clathrin and adaptor protein 4 complexes.IMPORTANCEMalaria takes an enormous toll on affected societies, and new drugs are urgently required. Understanding how the parasite causing malaria replicates could lead to potential new drug targets. Our work characterizes a protein called Tepsin that could potentially be important for the parasite to generate organelles critical for its survival. |
| format | Article |
| id | doaj-art-a3c8e625c7d94f51b8f341c642b765db |
| institution | DOAJ |
| issn | 2165-0497 |
| language | English |
| publishDate | 2025-08-01 |
| publisher | American Society for Microbiology |
| record_format | Article |
| series | Microbiology Spectrum |
| spelling | doaj-art-a3c8e625c7d94f51b8f341c642b765db2025-08-20T02:56:43ZengAmerican Society for MicrobiologyMicrobiology Spectrum2165-04972025-08-0113810.1128/spectrum.03288-24Characterization of the malaria parasite Plasmodium falciparum Tepsin homologStéphanie Roucheray0Maria R. Narciso1Dave Richard2Department of Microbiology-Infectious Diseases and Immunology, Faculty of Medicine, Université Laval, Quebec City, CanadaDepartment of Chemistry and Biology, Molecular Science Graduate Program, Toronto Metropolitan University, Toronto, CanadaDepartment of Microbiology-Infectious Diseases and Immunology, Faculty of Medicine, Université Laval, Quebec City, CanadaABSTRACT Plasmodium parasites rely on the invasion of human erythrocytes for their survival. This invasion process is facilitated by specialized organelles (rhoptry, micronemes, and dense granules) housed within a distinctive structure known as the apical complex. How the apical complex is generated is still enigmatic, especially how specificity is achieved in the vesicular trafficking between the Golgi apparatus and the apical organelles, but phosphoinositide lipids might potentially be involved. Here, we describe the characterization of a putative phosphoinositide-binding protein containing an Epsin NH2-terminal homology (ENTH) domain, Pf3D7_1459600. We show that this protein is structurally homologous to human Tepsin. Surprisingly, unlike other Tepsins, the ENTH domain of PfTepsin binds non-specifically to phosphoinositides in vitro, potentially through a positively charged pocket. Colocalization assays revealed that PfTepsin potentially transits between the Golgi apparatus and some of the apical organelles in developing schizonts. Finally, we provide evidence that PfTepsin potentially interacts with members of the clathrin and adaptor protein 4 complexes.IMPORTANCEMalaria takes an enormous toll on affected societies, and new drugs are urgently required. Understanding how the parasite causing malaria replicates could lead to potential new drug targets. Our work characterizes a protein called Tepsin that could potentially be important for the parasite to generate organelles critical for its survival.https://journals.asm.org/doi/10.1128/spectrum.03288-24malariaprotein traffickingGolgiTepsin |
| spellingShingle | Stéphanie Roucheray Maria R. Narciso Dave Richard Characterization of the malaria parasite Plasmodium falciparum Tepsin homolog Microbiology Spectrum malaria protein trafficking Golgi Tepsin |
| title | Characterization of the malaria parasite Plasmodium falciparum Tepsin homolog |
| title_full | Characterization of the malaria parasite Plasmodium falciparum Tepsin homolog |
| title_fullStr | Characterization of the malaria parasite Plasmodium falciparum Tepsin homolog |
| title_full_unstemmed | Characterization of the malaria parasite Plasmodium falciparum Tepsin homolog |
| title_short | Characterization of the malaria parasite Plasmodium falciparum Tepsin homolog |
| title_sort | characterization of the malaria parasite plasmodium falciparum tepsin homolog |
| topic | malaria protein trafficking Golgi Tepsin |
| url | https://journals.asm.org/doi/10.1128/spectrum.03288-24 |
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