Mutant/mutation
The mutant expresses a C-terminal BirA*-myc-tagged version of MDV1/PEG3.

Protein (function)
The protein is a gametocyte specific protein and has been named in P. falciparum MDV-1 (male development gene 1) or PEG3. In P. falciparum gametocytes the protein is associated with the osmiophilic bodies, the parasite membrane and all membranous compartments derived from the parasitophorous vacuole membrane. P. falciparum parasites lacking expression of MDV-1/PEG3 were affected in their capacity to produce functional gametocytes, which were unable to be transmitted through mosquitoes.
The phenotype analyses of a P. berghei mutant lacking expression of MDV1/PEG3 (RMgm-282) indicate that the lack of expression of MDV-1/PEG3 strongly impairs fertilisation and ookinete formation and that the decreased fertilisation rate results from a strongly reduced capacity of both male and female gametocytes/gametes to egress from their host erythrocytes. The results indicate that MDV-1/PEG3 plays a role in disruption of the parasitophorous vacuole membrane (PVM) and the erythrocyte membrane.

Phenotype
Using an anti-myc antibody the MDV1/PEG3::BirA*::myc protein is readily identified by immunofluorescence revealing its gametocyte-specific localization in the mutant with an abundant and typical localization for osmiophilic bodies.

Additional information
This mutant is used in a study aiming at identifying 'gametocyte regressome', i.e. proteins that are released when Plasmodium gametes escape from their host reythrocyte. For the release of mature extracellular gametes two membrane barriers - the parasite parasitophorous vacuole membrane and the host red blood cell membrane - need to be dissolved. Membrane lysis occurs after the release of proteins from specialized secretory vesicles including osmiophilic bodies.
The identified Plasmodium gametocyte egressome includes the proteins released by the parasite during the lysis of the parasitophorous vacuole membrane and red blood cell membrane. BioID of the osmiophilic body protein MDV1/PEG3 revealed a proteome of these gametocyte-specific secretory vesicles. For bioID the mutated biotin ligase BirA* from Escherichia coli was fused to MDV1/PEG3. BioID relies on the fusion of a protein of interest with a mutated BirA ligase (BirA*) that in the presence of excess biotin biotinylates nearby proteins, which can be purified by affinity chromatography using streptavidin.
Fluorescent protein tagging and gene deletion approaches were employed to validate and identify a set of novel factors essential for this lysis and egress process.

Other mutants
See this link for other mutants generated in this study.
See also other MDV1/PEG3 mutants.