{"gene":"PF3D7_1310000","run_date":"2026-09-08T14:19:06","timeline":{"discoveries":[{"year":2011,"finding":"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.","method":"Epitope-tagging of ATP synthase subunits with immunofluorescence localization; blue native gel electrophoresis of mitochondrial membranes","journal":"The Journal of biological chemistry","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct localization by epitope-tag immunofluorescence and native gel electrophoresis in a single lab, two orthogonal methods; OSCP is one of seven subunits studied collectively and is not individually dissected beyond localization and complex membership","pmids":["21984828"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"PF3D7_1310000 (OSCP) is a canonical ATP synthase subunit that localizes to the P. falciparum mitochondrion and is incorporated into a large (>1 MDa) dimeric ATP synthase complex in mitochondrial membranes, but its individual mechanistic role within the complex has not been experimentally dissected beyond complex membership and localization."},"narrative":{"mechanistic_narrative":"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.","teleology":[{"year":2011,"claim":"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","pmids":["21984828"],"confidence":"Medium","gaps":["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"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"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.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No experiment isolates OSCP function apart from the whole complex","No essentiality or interaction-mapping data specific to OSCP"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["Mitochondrial ATP synthase complex (>1 MDa dimeric)"],"partners":[],"other_free_text":["OSCP is a canonical subunit incorporated into the large dimeric P. falciparum ATP synthase complex resolved in mitochondrial membranes; the corpus establishes only its mitochondrial localization and complex membership, not an individual mechanistic role [#0]."]}},"prefetch_data":{},"corpus_meta":[{"pmid":"15552397","id":"PMC_15552397","title":"The multiple roles of the mitochondrion of the malarial parasite.","date":"2004","source":"Parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/15552397","citation_count":66,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["ATP"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"25823686","id":"PMC_25823686","title":"Triaminopyrimidine is a fast-killing and long-acting antimalarial clinical candidate.","date":"2015","source":"Nature communications","url":"https://pubmed.ncbi.nlm.nih.gov/25823686","citation_count":59,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["ATP"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"21984828","id":"PMC_21984828","title":"ATP synthase complex of Plasmodium falciparum: dimeric assembly in mitochondrial membranes and resistance to genetic disruption.","date":"2011","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/21984828","citation_count":54,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["ATP"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"19682605","id":"PMC_19682605","title":"Identification of mitochondrial Complex II subunits SDH3 and SDH4 and ATP synthase subunits a and b in Plasmodium spp.","date":"2009","source":"Mitochondrion","url":"https://pubmed.ncbi.nlm.nih.gov/19682605","citation_count":27,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["ATP"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":4404,"output_tokens":441,"usd":0.009914,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":4965,"output_tokens":997,"usd":0.024875,"stage2_stop_reason":"end_turn"},"total_usd":0.034789,"stage1_batch_id":"msgbatch_011BPjN2BL33F8cJXD1r7V7T","stage2_batch_id":"msgbatch_01Qwg6vP7qxkpL6Gsc7tajsb","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2011,\n      \"finding\": \"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.\",\n      \"method\": \"Epitope-tagging of ATP synthase subunits with immunofluorescence localization; blue native gel electrophoresis of mitochondrial membranes\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct localization by epitope-tag immunofluorescence and native gel electrophoresis in a single lab, two orthogonal methods; OSCP is one of seven subunits studied collectively and is not individually dissected beyond localization and complex membership\",\n      \"pmids\": [\"21984828\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    }\n  ],\n  \"current_model\": \"PF3D7_1310000 (OSCP) is a canonical ATP synthase subunit that localizes to the P. falciparum mitochondrion and is incorporated into a large (>1 MDa) dimeric ATP synthase complex in mitochondrial membranes, but its individual mechanistic role within the complex has not been experimentally dissected beyond complex membership and localization.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"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 [#0]. 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.\",\n  \"teleology\": [\n    {\n      \"year\": 2011,\n      \"claim\": \"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.\",\n      \"evidence\": \"Epitope-tagging with immunofluorescence localization and blue native gel electrophoresis of mitochondrial membranes in P. falciparum blood stages\",\n      \"pmids\": [\"21984828\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"OSCP was studied as one of seven subunits collectively; its individual functional contribution to the complex was not dissected\",\n        \"No genetic knockout or knockdown to test essentiality of OSCP itself\",\n        \"No structural or biochemical characterization of OSCP's role in complex assembly or ATP synthesis\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"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.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No experiment isolates OSCP function apart from the whole complex\",\n        \"No essentiality or interaction-mapping data specific to OSCP\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [],\n    \"localization\": [\n      {\"term_id\": \"GO:0005739\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"pathway\": [],\n    \"complexes\": [\"Mitochondrial ATP synthase complex (>1 MDa dimeric)\"],\n    \"partners\": [],\n    \"other_free_text\": [\n      \"OSCP is a canonical subunit incorporated into the large dimeric P. falciparum ATP synthase complex resolved in mitochondrial membranes; the corpus establishes only its mitochondrial localization and complex membership, not an individual mechanistic role [#0].\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_1310000","name":null,"product":"ATP synthase subunit O, mitochondrial, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_1408500","name":null,"product":"ATP synthase subunit O, mitochondrial, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_1410400","name":null,"product":"ATP synthase subunit O, mitochondrial, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"OSCP","evaluation":null}