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ProteomicsPlasmodium falciparum Kelch13, Eps15 and Clathrin HC interactomes obtained using a dimerisation-induced quantitative BioID (DiQ-BioID)
In order to identify Kelch13 interaction partners in living P. falciparum parasites, we established a new type of BioID we termed dimerisation-induced quantitative BioID (DiQ-BioID) that takes advantage of the FKBP-FRB heterodimerisation system. For DiQ-BioID the target is endogenously tagged with F...
ORGANISM(S): Plasmodium falciparum 
2021-12-02 | PXD008219 | Pride
Eps15 Dimerisation-induced quantitative bioid (diq-bioid) Plasmodium falciparum Artemisinin resistance Vesicle trafficking Kelch13 Clathrin hc 
ProteomicsPlasmodium falciparum Chr3C7 and Chr3C16 DiQ-BioID data
As part of a larger study characterizing all unknown 'nonsecretory' proteins encoded on chromosome 3 of P. falciparum parasites, we selected two candidate proteins (Chr3C7 and Chr3C16) to obtain interactomes using dimerisation-induced quantitative BioID (DiQ-BioID). This set of experiments r...
ORGANISM(S): Plasmodium falciparum (isolate 3D7) 
2023-02-17 | PXD035332 | Pride
Chromosome-wide screen Malaria Subcellular localisation Mitosis Plasmodium falciparum 
ProteomicsIdentification of proteins in proximity to VAP and VPS13L1 in P. falciparum blood stages
P. falciparum blood stage parasites maintain an intricate system of membranes, requiring precise mechanisms of lipid synthesis and trafficking. Lipid transfer proteins (LTPs) at interorganelle membrane contact sites (MCSs) have emerged as key for ensuring proper lipid distribution in cells but so fa...
ORGANISM(S): Plasmodium falciparum (isolate 3D7) 
2025-07-28 | PXD066159 | Pride
Malaria Membrane contact sites Erythrocytic stages Lipid transfer proteins Bioid 
ProteomicsProximity labelling of the post-Golgi AP complexes in Plasmodium falciparum
Adaptor protein (AP) complexes are pivotal components of the post-Golgi trafficking and endocytosis process and are involved in the selection, package and sorting of cargo into vesicles to different destination compartments in eukaryotic cells. The main objective of this project was to investigate t...
ORGANISM(S): Plasmodium falciparum (isolate 3D7) 
2025-09-17 | PXD062862 | Pride
Adaptor protein (ap) complexes Malaria Vesicular trafficking. Miniturbo Proximity labelling Plasmodium falciparum Sli Diq-bioid 
ProteomicsPlasmodium falciparum PfEMP1 DiQ-BioID data
PfEMP1 is the major virulence factor of Plasmodium falciparum parasites. PfEMP1 is expressed as an integral membrane protein on the surface of infected red blood cells. As a part of this project, the BioID system was utilized to biotinylate proximal proteins of a functional PfEMP1. In order to do th...
ORGANISM(S): Plasmodium falciparum 
2025-11-13 | PXD052297 | Pride
Var genes Virulence Protein export Malaria Pfemp1 Bira* Selection linked integration Bioid Plasmodium falciparum 
ProteomicsPfcerli2, a duplicated gene in the malaria parasite Plasmodium falciparum essential for invasion of erythrocytes as revealed by phylogenetic and cell biological analysis.
Merozoite invasion of host red blood cells (RBCs) is essential for survival of the human malaria parasite Plasmodium falciparum. Proteins involved with RBC binding and invasion are secreted from dual-club shaped organelles at the apical tip of the merozoite called the rhoptries. Here we characterise...
ORGANISM(S): Homo sapiens (Human) Plasmodium falciparum 
2021-11-15 | PXD028937 | Pride
Plasmodium falciparum Malaria Human red blood cells 
ProteomicsBioID of Plasmodium falciparum rhophtry-neck associated protein (PfAIP) using BirA* fusion-protein
Apicomplexan parasites contain rhoptries, which are specialized secretory organelles that coordinate host cell invasion. During the process of invasion, rhoptries secrete their contents to facilitate interaction with, and entry into, the host cell. Here we report the crystal structure of the rhoptry...
ORGANISM(S): Plasmodium falciparum 
2019-12-12 | PXD016687 | Pride
Malaria Invasion Proximity-based biotinylation Rhoptries Plasmodium 
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