Characterisation of complexes formed by parasite proteins exported into the host cell compartment of Plasmodium falciparum infected red blood cells
| Autor: | Paul R Sanders, Betty Kouskousis, Thorey K Jonsdottir, Hayley E Bullen, Paul R. Gilson, Natalie A. Counihan, Brendan S. Crabb, Mikha Gabriela, Tania F. de Koning-Ward, Joyanta K Modak |
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| Rok vydání: | 2021 |
| Předmět: |
Erythrocytes
Immunoprecipitation Plasmodium falciparum Immunology exported proteins J‐dots malaria Maurer's clefts Protozoan Proteins Biology Proteomics Microbiology 03 medical and health sciences Virology medicine Animals Humans Parasite hosting Parasites Cytoskeleton Research Articles new permeability pathways 030304 developmental biology 0303 health sciences Gene knockdown 030306 microbiology Erythrocyte Membrane RhopH biology.organism_classification Cell biology Protein Transport Red blood cell medicine.anatomical_structure Function (biology) Research Article |
| Zdroj: | Cellular Microbiology |
| ISSN: | 1462-5822 1462-5814 |
| DOI: | 10.1111/cmi.13332 |
| Popis: | During its intraerythrocytic life cycle, the human malaria parasite Plasmodium falciparum supplements its nutritional requirements by scavenging substrates from the plasma through the new permeability pathways (NPPs) installed in the red blood cell (RBC) membrane. Parasite proteins of the RhopH complex: CLAG3, RhopH2, RhopH3, have been implicated in NPP activity. Here we studied 13 exported proteins previously hypothesised to interact with RhopH2, to study their potential contribution to the function of NPPs. NPP activity assays revealed that the 13 proteins do not appear to be individually important for NPP function, as conditional knockdown of these proteins had no effect on sorbitol uptake. Intriguingly, reciprocal immunoprecipitation assays showed that five of the 13 proteins interact with all members of the RhopH complex, with PF3D7_1401200 showing the strongest association. Mass spectrometry-based proteomics further identified new protein complexes; a cytoskeletal complex and a Maurer's clefts/J-dot complex, which overall helps clarify protein-protein interactions within the infected RBC (iRBC) and is suggestive of the potential trafficking route of the RhopH complex itself to the RBC membrane. This article is protected by copyright. All rights reserved. |
| Databáze: | OpenAIRE |
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