| 2012 |
Crystal structure of P. falciparum GAP50 (PF3D7_0918000) was solved at 1.7 Å resolution, revealing an αββα fold with overall similarity to purple acid phosphatases but with a fundamentally different active-site region; the structure showed two cobalt ions each with only one protein ligand and 18 Å apart (vs. 3.2 Å in purple acid phosphatases), indicating GAP50 is not a functional phosphatase. The C-terminal transmembrane helix anchors GAP50 into the inner membrane complex (IMC), and a short six-residue C-terminal tail interacts with other glideosome proteins. |
X-ray crystallography (1.7 Å resolution crystal structure of the soluble domain of PfGAP50) |
Journal of structural biology |
High |
22387043
|
| 2006 |
P. falciparum GAP50 (PF3D7_0918000) was identified as an integral membrane protein of the IMC that forms a glideosome complex with PfGAP45, PfMyoA, and PfMTIP in late schizonts and merozoites, supporting erythrocyte invasion. The complex was detected by co-immunoprecipitation from late-schizont/merozoite lysates. |
Co-immunoprecipitation from P. falciparum blood-stage parasites; immunofluorescence assay for localization |
Molecular and biochemical parasitology |
Medium |
16513191
|
| 2010 |
GAP50 (PF3D7_0918000) is a core component of the Toxoplasma/Plasmodium glideosome; in Toxoplasma, functional dissection showed GAP50 is a polytopic IMC-anchored protein and forms a complex with GAP45, MyoA, and MLC1. The orthologous P. falciparum GAP45 can functionally substitute in T. gondii (transgenera complementation), supporting conserved complex architecture across the phylum. |
Genetic complementation across genera; co-immunoprecipitation; immunofluorescence; conditional knockdown |
Cell host & microbe |
Medium |
20951968
|
| 2011 |
PfGAP50-GFP (PF3D7_0918000) localizes to the endoplasmic reticulum in early-stage parasites and then redistributes to apical caps during daughter merozoite formation, extending around the merozoite surface in final schizogony. The C-terminal membrane anchor is required for correct trafficking: a construct lacking this anchor is misdirected to the parasitophorous vacuole. Full-length PfGAP50-GFP forms a complex with endogenous PfGAP45 and MTIP as shown by immunoprecipitation and FRAP. |
Live fluorescence imaging of GFP-tagged PfGAP50; FRAP; immunoprecipitation; 3D structured illumination microscopy; domain-deletion transfection |
Eukaryotic cell |
High |
21239623
|
| 2007 |
PfGAP50 (PF3D7_0918000) was identified as part of a high-molecular-weight detergent-resistant membrane (DRM) complex together with GAP45 and myosin A in P. falciparum schizonts, isolated by blue native-PAGE and identified by mass spectrometry. |
Detergent-resistant membrane purification; blue native-PAGE; mass spectrometry |
Molecular and biochemical parasitology |
Medium |
17553576
|
| 2013 |
PfGAP50 (PF3D7_0918000) on the surface of emerging P. falciparum gametes binds human complement regulator factor H (FH) and uses surface-bound FH to inactivate complement protein C3b, protecting parasites from complement-mediated lysis in the mosquito midgut. Neutralization of FH or blockade of PfGAP50 significantly impaired gametogenesis and parasite transmission. |
Binding assays (FH to gamete surface/PfGAP50); complement lysis assays; antibody blockade; gametogenesis inhibition assay |
Cell host & microbe |
Medium |
23332154
|
| 2005 |
Homologues of glideosome-associated proteins including GAP50 (PF3D7_0918000) are present in P. falciparum merozoites and appear to function in erythrocyte invasion; MTRAP, a merozoite TRAP homologue identified in the same study, binds aldolase in vitro, linking the extracellular adhesin to the actin-myosin motor that includes GAP50. |
Immunofluorescence; in vitro aldolase-binding assay; bioinformatic genome analysis |
The Journal of biological chemistry |
Low |
16321976
|
| 2017 |
GAP50 (PF3D7_0918000) was identified by co-immunoprecipitation as a binding partner of PhIL1, a novel IMC-associated protein in both P. falciparum and P. berghei; this interaction places GAP50 in a PhIL1-containing protein complex overlapping with, but distinct from, the canonical glideosome. |
Co-immunoprecipitation / protein interactome (PhIL1 pulldown followed by mass spectrometry) |
Scientific reports |
Low |
29138437
|
| 2017 |
GAP50 (PF3D7_0918000) remains a component of the glideosome complex (together with GAP40, an additional essential light chain ELC, MyoA, MTIP, and other candidate proteins) throughout the P. berghei life cycle in extracellular stages (ookinetes, sporozoites, merozoites); co-expression of MyoA with both light chains (MTIP and ELC) enhances MyoA-dependent actin motility in vitro. |
Immunofluorescence across life cycle stages; in vitro actin motility assay; co-immunoprecipitation/mass spectrometry of glideosome complex |
The Journal of biological chemistry |
Medium |
28893907
|
| 2023 |
PfGAP50 (PF3D7_0918000) co-precipitates with PfGAP45 and PfGAP40, and PfGAP40 knockdown reduces steady-state expression levels of both PfGAP45 and PfGAP50 in schizonts, indicating that GAP40 stabilizes GAP50 protein levels within the glideosome complex. |
Conditional knockdown (TetR-DOZI) of PfGAP40; co-immunoprecipitation; Western blot quantification of GAP50 levels |
Microbiology spectrum |
Medium |
37249423
|
| 2015 |
Antibodies raised against recombinant PfGAP50 (PF3D7_0918000) inhibited zygote formation by up to 55% in an in vitro zygote inhibition assay, demonstrating that GAP50-specific antibodies can block parasite transmission at the gamete/zygote stage. |
In vitro zygote inhibition assay with anti-PfGAP50 rabbit IgG; immunofluorescence assay confirming antibody specificity |
BMC biotechnology |
Low |
26625934
|