{"gene":"PF3D7_0308200","run_date":"2026-09-08T19:44:17","timeline":{"discoveries":[{"year":2017,"finding":"CCT7 (TRiC-θ subunit, PF3D7_0308200) is part of the TRiC chaperonin complex in the P. falciparum parasite cytosol; regulatable knockdown of CCT7 caused a severe growth defect in asexual development, but did not alter protein export into the red blood cell, indicating the complex functions within the parasite rather than in RBC protein trafficking.","method":"Epitope-tagged transgenic parasites, parasite-specific antibody localization, regulatable knockdown (TRiC-θ knockdown line) with asexual growth phenotype readout and protein export assay","journal":"Cellular microbiology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — clean regulatable knockdown with defined cellular phenotype (growth defect) and negative export result; single lab, two orthogonal methods (localization + functional knockdown)","pmids":["28067475"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2019,"finding":"CCT7 (PF3D7_0308200), as part of the TRiC/CCT complex, was found associated with the CAF1/CCR4/NOT complex immunoprecipitated from P. yoelii schizonts, suggesting a physical interaction (direct or indirect) between TRiC and the mRNA deadenylation/translational repression machinery.","method":"Co-immunoprecipitation via GFP-tagged PyCCR4-1 followed by mass spectrometry (SAINT analysis)","journal":"PLoS pathogens","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single Co-IP/MS experiment, CCT7 detected at a less stringent SAINT score threshold (0.1–0.35), single lab, no functional follow-up specific to CCT7","pmids":["30703164"],"is_preprint":false,"attribution":[{"species":"Plasmodium yoelii","strain":""}]},{"year":2022,"finding":"CCT7 (PF3D7_0308200) was detected in a proteomic dataset of the PfCCT complex purified from P. falciparum trophozoites via a FLAG-tagged CCT8 subunit, confirming CCT7 membership in the parasite TRiC/CCT holo-complex.","method":"FLAG-tagged CCT8 affinity purification (Selection Linked Integration) followed by proteomic analysis from synchronized trophozoite-stage cultures","journal":"Frontiers in molecular biosciences","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single affinity purification/proteomics experiment establishing complex membership only; no functional characterization of CCT7 itself","pmids":["36567946"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"PF3D7_0308200 (CCT7) is a subunit of the TRiC/CCT chaperonin complex in the P. falciparum cytosol; its loss causes severe asexual growth defects without affecting protein export to the host red blood cell, and the complex has been detected in association with the CAF1/CCR4/NOT mRNA regulatory machinery in P. yoelii, but no further mechanistic detail specific to CCT7 itself has been established."},"narrative":{"mechanistic_narrative":"PF3D7_0308200 (CCT7) is a subunit of the TRiC/CCT chaperonin complex localized to the Plasmodium falciparum parasite cytosol [PMID:28067475]. Regulatable knockdown of CCT7 causes a severe asexual growth defect but does not perturb protein export into the host red blood cell, indicating that the complex acts within the parasite rather than in host-cell protein trafficking [PMID:28067475]. Its membership in the parasite TRiC/CCT holo-complex has been independently confirmed by affinity purification of the complex via the CCT8 subunit in P. falciparum trophozoites [PMID:36567946]. In P. yoelii, the TRiC/CCT complex including CCT7 was detected in association with the CAF1/CCR4/NOT mRNA deadenylation and translational repression machinery, indicating a physical (direct or indirect) link to mRNA regulation [PMID:30703164]. Beyond complex membership, the growth requirement, and this reported association, no CCT7-specific molecular mechanism, substrate, or structural detail has been characterized in the available corpus.","teleology":[{"year":2017,"claim":"Whether CCT7 functions within the parasite or in host-cell protein trafficking was unknown; localizing it and knocking it down established it as a cytosolic TRiC chaperonin subunit required for asexual growth but dispensable for RBC protein export.","evidence":"Epitope-tagged transgenic parasites with antibody localization plus regulatable knockdown and growth/export phenotype readouts in P. falciparum","pmids":["28067475"],"confidence":"Medium","gaps":["No client/substrate proteins of the CCT7-containing complex identified","Mechanism linking chaperonin loss to the growth defect not defined","No structural characterization of CCT7 within the complex"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2019,"claim":"Whether the parasite TRiC/CCT complex connects to mRNA regulatory machinery was untested; a Co-IP identified CCT7 among proteins associated with the CAF1/CCR4/NOT deadenylation complex, raising a possible physical link.","evidence":"GFP-tagged PyCCR4-1 co-immunoprecipitation followed by mass spectrometry (SAINT analysis) in P. yoelii schizonts","pmids":["30703164"],"confidence":"Low","gaps":["CCT7 detected only at a permissive SAINT threshold (0.1-0.35); association not independently validated","Direct versus indirect interaction not resolved","No functional follow-up specific to CCT7 in this context"],"attribution":[{"species":"Plasmodium yoelii","strain":""}]},{"year":2022,"claim":"Whether CCT7 is a bona fide member of the assembled parasite chaperonin was addressed by purifying the holo-complex through a different subunit and confirming CCT7 co-purifies.","evidence":"FLAG-tagged CCT8 affinity purification (Selection Linked Integration) with proteomics from synchronized P. falciparum trophozoites","pmids":["36567946"],"confidence":"Low","gaps":["Establishes complex membership only, with no functional characterization of CCT7","No stoichiometry or subunit arrangement determined","No substrates of the purified complex identified"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"The specific molecular role of CCT7 within the TRiC/CCT complex, its folding substrates, and the functional significance of the reported CAF1/CCR4/NOT association remain unresolved.","evidence":"","pmids":[],"confidence":"Low","gaps":["No CCT7-specific client proteins identified","Functional consequence of the TRiC-CCR4/NOT association not tested for CCT7","No structural model of CCT7 in the Plasmodium chaperonin"],"attribution":[]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["TRiC/CCT chaperonin complex","CAF1/CCR4/NOT complex (association, P. yoelii)"],"partners":["CCT8 (CO-PURIFYING CHAPERONIN SUBUNIT)","PYCCR4-1 (CAF1/CCR4/NOT, ASSOCIATION IN P. YOELII)"],"other_free_text":["Knockdown of CCT7 causes a severe asexual-stage growth defect but does not affect protein export to the host red blood cell [#0]","Corpus establishes CCT7 primarily through its membership in the parasite TRiC/CCT complex; little CCT7-specific mechanism is defined"]}},"prefetch_data":{},"corpus_meta":[{"pmid":"28067475","id":"PMC_28067475","title":"The chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosol.","date":"2017","source":"Cellular microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/28067475","citation_count":51,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"25615740","id":"PMC_25615740","title":"New Export Pathway in Plasmodium falciparum-Infected Erythrocytes: Role of the Parasite Group II Chaperonin, PfTRiC.","date":"2015","source":"Traffic (Copenhagen, Denmark)","url":"https://pubmed.ncbi.nlm.nih.gov/25615740","citation_count":15,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"36567946","id":"","title":"The malaria parasite chaperonin containing TCP-1 (CCT) complex: Data integration with other CCT proteomes.","date":"2022","source":"Frontiers in molecular biosciences","url":"https://pubmed.ncbi.nlm.nih.gov/36567946","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["CCT7"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"30703164","id":"","title":"Plasmodium male gametocyte development and transmission are critically regulated by the two putative deadenylases of the CAF1/CCR4/NOT complex.","date":"2019","source":"PLoS pathogens","url":"https://pubmed.ncbi.nlm.nih.gov/30703164","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["CCT7"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":6169,"output_tokens":970,"usd":0.016529,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":5711,"output_tokens":1911,"usd":0.038165,"stage2_stop_reason":"end_turn"},"total_usd":0.054694,"stage1_batch_id":"msgbatch_01SRp5hyRc82zNjddxyCCXGk","stage2_batch_id":"msgbatch_01K3BTmBazRo3pRrMvyaPMTY","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2017,\n      \"finding\": \"CCT7 (TRiC-θ subunit, PF3D7_0308200) is part of the TRiC chaperonin complex in the P. falciparum parasite cytosol; regulatable knockdown of CCT7 caused a severe growth defect in asexual development, but did not alter protein export into the red blood cell, indicating the complex functions within the parasite rather than in RBC protein trafficking.\",\n      \"method\": \"Epitope-tagged transgenic parasites, parasite-specific antibody localization, regulatable knockdown (TRiC-θ knockdown line) with asexual growth phenotype readout and protein export assay\",\n      \"journal\": \"Cellular microbiology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — clean regulatable knockdown with defined cellular phenotype (growth defect) and negative export result; single lab, two orthogonal methods (localization + functional knockdown)\",\n      \"pmids\": [\"28067475\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"CCT7 (PF3D7_0308200), as part of the TRiC/CCT complex, was found associated with the CAF1/CCR4/NOT complex immunoprecipitated from P. yoelii schizonts, suggesting a physical interaction (direct or indirect) between TRiC and the mRNA deadenylation/translational repression machinery.\",\n      \"method\": \"Co-immunoprecipitation via GFP-tagged PyCCR4-1 followed by mass spectrometry (SAINT analysis)\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single Co-IP/MS experiment, CCT7 detected at a less stringent SAINT score threshold (0.1–0.35), single lab, no functional follow-up specific to CCT7\",\n      \"pmids\": [\"30703164\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium yoelii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"CCT7 (PF3D7_0308200) was detected in a proteomic dataset of the PfCCT complex purified from P. falciparum trophozoites via a FLAG-tagged CCT8 subunit, confirming CCT7 membership in the parasite TRiC/CCT holo-complex.\",\n      \"method\": \"FLAG-tagged CCT8 affinity purification (Selection Linked Integration) followed by proteomic analysis from synchronized trophozoite-stage cultures\",\n      \"journal\": \"Frontiers in molecular biosciences\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single affinity purification/proteomics experiment establishing complex membership only; no functional characterization of CCT7 itself\",\n      \"pmids\": [\"36567946\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"PF3D7_0308200 (CCT7) is a subunit of the TRiC/CCT chaperonin complex in the P. falciparum cytosol; its loss causes severe asexual growth defects without affecting protein export to the host red blood cell, and the complex has been detected in association with the CAF1/CCR4/NOT mRNA regulatory machinery in P. yoelii, but no further mechanistic detail specific to CCT7 itself has been established.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"PF3D7_0308200 (CCT7) is a subunit of the TRiC/CCT chaperonin complex localized to the Plasmodium falciparum parasite cytosol [#0]. Regulatable knockdown of CCT7 causes a severe asexual growth defect but does not perturb protein export into the host red blood cell, indicating that the complex acts within the parasite rather than in host-cell protein trafficking [#0]. Its membership in the parasite TRiC/CCT holo-complex has been independently confirmed by affinity purification of the complex via the CCT8 subunit in P. falciparum trophozoites [#2]. In P. yoelii, the TRiC/CCT complex including CCT7 was detected in association with the CAF1/CCR4/NOT mRNA deadenylation and translational repression machinery, indicating a physical (direct or indirect) link to mRNA regulation [#1]. Beyond complex membership, the growth requirement, and this reported association, no CCT7-specific molecular mechanism, substrate, or structural detail has been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2017,\n      \"claim\": \"Whether CCT7 functions within the parasite or in host-cell protein trafficking was unknown; localizing it and knocking it down established it as a cytosolic TRiC chaperonin subunit required for asexual growth but dispensable for RBC protein export.\",\n      \"evidence\": \"Epitope-tagged transgenic parasites with antibody localization plus regulatable knockdown and growth/export phenotype readouts in P. falciparum\",\n      \"pmids\": [\"28067475\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No client/substrate proteins of the CCT7-containing complex identified\",\n        \"Mechanism linking chaperonin loss to the growth defect not defined\",\n        \"No structural characterization of CCT7 within the complex\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"Whether the parasite TRiC/CCT complex connects to mRNA regulatory machinery was untested; a Co-IP identified CCT7 among proteins associated with the CAF1/CCR4/NOT deadenylation complex, raising a possible physical link.\",\n      \"evidence\": \"GFP-tagged PyCCR4-1 co-immunoprecipitation followed by mass spectrometry (SAINT analysis) in P. yoelii schizonts\",\n      \"pmids\": [\"30703164\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"CCT7 detected only at a permissive SAINT threshold (0.1-0.35); association not independently validated\",\n        \"Direct versus indirect interaction not resolved\",\n        \"No functional follow-up specific to CCT7 in this context\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium yoelii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Whether CCT7 is a bona fide member of the assembled parasite chaperonin was addressed by purifying the holo-complex through a different subunit and confirming CCT7 co-purifies.\",\n      \"evidence\": \"FLAG-tagged CCT8 affinity purification (Selection Linked Integration) with proteomics from synchronized P. falciparum trophozoites\",\n      \"pmids\": [\"36567946\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"Establishes complex membership only, with no functional characterization of CCT7\",\n        \"No stoichiometry or subunit arrangement determined\",\n        \"No substrates of the purified complex identified\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The specific molecular role of CCT7 within the TRiC/CCT complex, its folding substrates, and the functional significance of the reported CAF1/CCR4/NOT association remain unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No CCT7-specific client proteins identified\",\n        \"Functional consequence of the TRiC-CCR4/NOT association not tested for CCT7\",\n        \"No structural model of CCT7 in the Plasmodium chaperonin\"\n      ],\n      \"attribution\": []\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0051082\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005829\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0006457\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"complexes\": [\n      \"TRiC/CCT chaperonin complex\",\n      \"CAF1/CCR4/NOT complex (association, P. yoelii)\"\n    ],\n    \"partners\": [\n      \"CCT8 (co-purifying chaperonin subunit)\",\n      \"PyCCR4-1 (CAF1/CCR4/NOT, association in P. yoelii)\"\n    ],\n    \"other_free_text\": [\n      \"Knockdown of CCT7 causes a severe asexual-stage growth defect but does not affect protein export to the host red blood cell [#0]\",\n      \"Corpus establishes CCT7 primarily through its membership in the parasite TRiC/CCT complex; little CCT7-specific mechanism is defined\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_0308200","name":null,"product":"T-complex protein 1 subunit eta","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_0406500","name":null,"product":"T-complex protein 1 subunit eta, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_0834500","name":null,"product":"T-complex protein 1 subunit eta, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"CCT7","evaluation":null}