Affinage · Plasmodium

OSCP

PF3D7_1310000 · ATP synthase subunit O, mitochondrial, putative

Annotated
2026-09-08
4 papers in source corpus 1 papers cited in narrative 1 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PF3D7_1310000 (OSCP) is a canonical subunit of the mitochondrial ATP synthase in Plasmodium falciparum, localizing to the mitochondrion of blood-stage parasites and assembling as part of a large (>1 MDa) dimeric ATP synthase complex in mitochondrial membranes (PMID:21984828). Beyond its mitochondrial localization and membership in the assembled ATP synthase complex, the individual mechanistic role of OSCP within the complex has not been characterized in the available corpus.

Mechanistic history

Synthesis pass · year-by-year structured walk · 1 step
  1. 2011 Medium

    Whether OSCP is expressed and correctly targeted in P. falciparum was unknown; epitope-tagging established that it localizes to the parasite mitochondrion and is a bona fide component of an assembled, high-molecular-weight ATP synthase complex.

    Evidence Epitope-tagging with immunofluorescence localization and blue native gel electrophoresis of mitochondrial membranes in P. falciparum blood stages

    PMID:21984828

    Open questions at the time
    • OSCP was studied as one of seven subunits collectively; its individual functional contribution to the complex was not dissected
    • No genetic knockout or knockdown to test essentiality of OSCP itself
    • No structural or biochemical characterization of OSCP's role in complex assembly or ATP synthesis

Open questions

Synthesis pass · forward-looking unresolved questions
  • The specific mechanistic role of OSCP within the P. falciparum ATP synthase — its contribution to complex assembly, coupling, or catalysis — remains undefined in the available corpus.
  • No experiment isolates OSCP function apart from the whole complex
  • No essentiality or interaction-mapping data specific to OSCP

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Complex memberships
Mitochondrial ATP synthase complex (>1 MDa dimeric)

Evidence

Reading pass · 1 per-paper finding extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2011 PF3D7_1310000 (OSCP/ATP synthase subunit O) localizes to the mitochondrion of P. falciparum blood stages, as shown by epitope-tagging of canonical ATP synthase subunits including OSCP and immunological detection. The full ATP synthase complex, of which OSCP is a canonical subunit, assembles as a large dimeric complex (>1 million daltons) in mitochondrial membranes as resolved by blue native gel electrophoresis. Epitope-tagging of ATP synthase subunits with immunofluorescence localization; blue native gel electrophoresis of mitochondrial membranes The Journal of biological chemistry Medium 21984828

Source papers

Stage 0 corpus · 4 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2004 The multiple roles of the mitochondrion of the malarial parasite. Parasitology 66 15552397
2015 Triaminopyrimidine is a fast-killing and long-acting antimalarial clinical candidate. Nature communications 59 25823686
2011 ATP synthase complex of Plasmodium falciparum: dimeric assembly in mitochondrial membranes and resistance to genetic disruption. The Journal of biological chemistry 54 21984828
2009 Identification of mitochondrial Complex II subunits SDH3 and SDH4 and ATP synthase subunits a and b in Plasmodium spp. Mitochondrion 27 19682605