{"gene":"PF3D7_1215000","run_date":"2026-09-08T14:19:06","timeline":{"discoveries":[{"year":2001,"finding":"Trx-Px2 (the larger of the two P. falciparum 2-Cys peroxiredoxins, 24.6 kDa) was recombinantly expressed and found to be active in the glutamine synthetase protector assay, demonstrating peroxidase/antioxidant activity. In oxidizing conditions it is converted to a faster-migrating species on SDS-PAGE, consistent with intramolecular disulfide formation as a regulatory mechanism.","method":"Recombinant overexpression in E. coli; glutamine synthetase protector assay; SDS-PAGE under oxidizing conditions","journal":"European journal of biochemistry","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — in vitro enzymatic assay with recombinant protein, single lab, single study; kinetic characterization was reported only for the smaller paralog (PfTPx1), not Trx-Px2 specifically","pmids":["11231293"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2005,"finding":"Trx-Px2 (PfTPx-2) localizes to the mitochondria of P. falciparum erythrocytic-stage parasites and is expressed during the trophozoite and schizont stages, consistent with a role in detoxifying ROS generated by the mitochondrial respiratory chain.","method":"Confocal laser scanning microscopy with subcellular localization; Western blotting; real-time quantitative RT-PCR","journal":"Parasitology international","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — direct localization by confocal microscopy corroborated by Western blot and RT-PCR in a single lab; functional consequence inferred but not experimentally proven","pmids":["15710548"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2006,"finding":"Trx-Px2 (the mitochondrial peroxiredoxin of P. falciparum) was structurally and biochemically characterized: its crystal structure revealed a fold typical of 2-Cys peroxiredoxins with a dimeric form bearing an intermolecular disulfide between Cys67 and Cys187; in solution it exists primarily as a homodecamer. Kinetically, it strongly prefers the mitochondrial thioredoxin PfTrx2 over the cytosolic PfTrx1 as a reducing partner (KM 11.6 µM vs. 130.4 µM). Substitution of residues Asn62/Tyr63 and Phe139/Ala140 reduced the KM for Trx1 but had no effect on the KM for Trx2, implicating these residues in substrate discrimination. GFP-fusion imaging in erythrocytic stages confirmed mitochondrial localization.","method":"X-ray crystallography; in vitro kinetic assay with recombinant protein; site-directed mutagenesis; GFP-fusion live imaging in parasite erythrocytic stages; solution studies (oligomeric state)","journal":"Molecular microbiology","confidence":"High","confidence_rationale":"Tier 1 / Strong — crystal structure solved, kinetics determined with recombinant protein, active-site mutagenesis performed, and mitochondrial localization independently confirmed by GFP imaging; multiple orthogonal methods in one rigorous study","pmids":["16879648"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2012,"finding":"Genetic disruption of the Trx-Px2 ortholog (pbtpx-2) in P. berghei showed that Trx-Px2 is not essential for asexual blood-stage growth or mosquito midgut oocyst development; KO parasites multiplied at rates comparable to wild-type. A minor delay (1 day) in peak gametocytemia was observed but peak gametocyte numbers were comparable.","method":"Gene disruption (knockout) in P. berghei; RT-PCR and Western blot confirmation of null expression; in vivo growth assays in mice and mosquito infection assays","journal":"Parasites & vectors","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — clean gene knockout with molecular confirmation and multiple independent disruptant populations; negative result (non-essential) robustly established","pmids":["23146411"],"is_preprint":false,"attribution":[{"species":"Plasmodium berghei","strain":""}]}],"current_model":"Trx-Px2 (PF3D7_1215000) is a mitochondrially-localized 2-Cys peroxiredoxin of P. falciparum that exists as a homodecamer in solution and as a disulfide-linked dimer (Cys67–Cys187) in its oxidized form; it preferentially uses the mitochondrial thioredoxin PfTrx2 (KM ~11.6 µM) over cytosolic PfTrx1 (KM ~130 µM) as its reductant, with residues Asn62/Tyr63 and Phe139/Ala140 contributing to this substrate discrimination, and it is not essential for blood-stage or mosquito-stage development in P. berghei."},"narrative":{"mechanistic_narrative":"Trx-Px2 (PF3D7_1215000) is a mitochondrially-localized 2-Cys peroxiredoxin of Plasmodium falciparum that provides thioredoxin-dependent antioxidant defense against reactive oxygen species generated during erythrocytic-stage metabolism [PMID:15710548, PMID:16879648]. The recombinant protein exhibits peroxidase/antioxidant activity in vitro and, under oxidizing conditions, converts to a faster-migrating disulfide-bonded species, consistent with redox-regulated catalysis through intramolecular/intermolecular disulfide formation [PMID:11231293]. Structurally it adopts the canonical 2-Cys peroxiredoxin fold, exists predominantly as a homodecamer in solution, and forms a dimer bearing an intermolecular Cys67–Cys187 disulfide in its oxidized state [PMID:16879648]. Functionally, it discriminates between reducing partners, strongly preferring the mitochondrial thioredoxin PfTrx2 (KM 11.6 µM) over cytosolic PfTrx1 (KM 130.4 µM), with residues Asn62/Tyr63 and Phe139/Ala140 contributing to this substrate selectivity [PMID:16879648]. Its subcellular residence was confirmed by both antibody-based confocal microscopy and GFP-fusion live imaging in erythrocytic stages, where expression peaks in trophozoite and schizont stages [PMID:15710548, PMID:16879648]. Genetic disruption of the P. berghei ortholog established that Trx-Px2 is dispensable for asexual blood-stage growth and mosquito midgut oocyst development, indicating functional redundancy in vivo despite its defined biochemical role [PMID:23146411].","teleology":[{"year":2001,"claim":"Whether the larger P. falciparum 2-Cys peroxiredoxin possessed enzymatic antioxidant activity was unknown; recombinant expression established it as a functional peroxidase whose migration shifts under oxidizing conditions, pointing to disulfide-based redox regulation.","evidence":"Recombinant expression in E. coli, glutamine synthetase protector assay, and SDS-PAGE under oxidizing conditions","pmids":["11231293"],"confidence":"Medium","gaps":["Kinetic constants were not determined for Trx-Px2 specifically in this study","The physiological electron donor was not identified","Single lab, single in vitro assay"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2005,"claim":"The subcellular compartment and stage-specific expression of Trx-Px2 were undefined; localization to the mitochondrion in trophozoite and schizont stages placed it at the site of respiratory-chain ROS production.","evidence":"Confocal microscopy, Western blotting, and real-time quantitative RT-PCR in erythrocytic-stage P. falciparum","pmids":["15710548"],"confidence":"Medium","gaps":["The ROS-detoxification role at the mitochondrion was inferred, not directly demonstrated","Reducing partner not established in this study"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2006,"claim":"The structure, oligomeric state, and reductant specificity of Trx-Px2 were unknown; a crystal structure, solution studies, kinetics, and mutagenesis established its 2-Cys peroxiredoxin fold, homodecameric assembly, Cys67–Cys187 disulfide dimer, and strong preference for mitochondrial PfTrx2, defining a mitochondrial thioredoxin-peroxiredoxin redox couple.","evidence":"X-ray crystallography, in vitro kinetics with recombinant protein, site-directed mutagenesis (Asn62/Tyr63, Phe139/Ala140), and GFP-fusion live imaging","pmids":["16879648"],"confidence":"High","gaps":["In vivo requirement for the PfTrx2 preference was not tested","The peroxide substrate range in vivo was not defined","Regulatory role of oligomeric switching not established in cells"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2012,"claim":"Whether the well-characterized mitochondrial peroxiredoxin is required for parasite viability was unknown; knockout of the P. berghei ortholog showed it is dispensable for asexual blood-stage growth and mosquito oocyst development, revealing functional redundancy despite its defined biochemistry.","evidence":"Gene disruption in P. berghei with RT-PCR/Western confirmation, in vivo mouse growth assays, and mosquito infection assays","pmids":["23146411"],"confidence":"Medium","gaps":["Redundant or compensating antioxidant systems were not identified","The minor delay in peak gametocytemia was not mechanistically explained","Result obtained in P. berghei, not P. falciparum"],"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":null,"claim":"The in vivo antioxidant substrates, the compensating pathways underlying its dispensability, and the physiological significance of its decamer–dimer redox switch remain unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No physiological peroxide substrate identified in parasites","Redundant antioxidant partners masking the KO phenotype are unknown","P. falciparum genetic requirement not directly tested"],"attribution":[]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["Homodecamer in solution; oxidized disulfide-linked (Cys67-Cys187) dimer"],"partners":["PFTRX2 (MITOCHONDRIAL THIOREDOXIN; PREFERRED REDUCTANT, KM 11.6 ΜM)","PFTRX1 (CYTOSOLIC THIOREDOXIN; POOR REDUCTANT, KM 130.4 ΜM)"],"other_free_text":["24.6 kDa 2-Cys peroxiredoxin; substrate discrimination residues Asn62/Tyr63 and Phe139/Ala140 [#2]","Non-essential for asexual blood-stage growth and mosquito oocyst development in P. berghei; minor delay in peak gametocytemia [#3]"]}},"prefetch_data":{},"corpus_meta":[{"pmid":"11231293","id":"PMC_11231293","title":"Thioredoxin peroxidases of the malarial parasite Plasmodium falciparum.","date":"2001","source":"European journal of biochemistry","url":"https://pubmed.ncbi.nlm.nih.gov/11231293","citation_count":63,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"15710548","id":"PMC_15710548","title":"Expression of mRNAs and proteins for peroxiredoxins in Plasmodium falciparum erythrocytic stage.","date":"2005","source":"Parasitology international","url":"https://pubmed.ncbi.nlm.nih.gov/15710548","citation_count":47,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"16879648","id":"PMC_16879648","title":"Structural and biochemical characterization of a mitochondrial peroxiredoxin from Plasmodium falciparum.","date":"2006","source":"Molecular microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/16879648","citation_count":44,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"23146411","id":"PMC_23146411","title":"Mitochondrial peroxidase TPx-2 is not essential in the blood and insect stages of Plasmodium berghei.","date":"2012","source":"Parasites & vectors","url":"https://pubmed.ncbi.nlm.nih.gov/23146411","citation_count":4,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["thioredoxin peroxidase 2"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":4942,"output_tokens":1499,"usd":0.018655,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6432,"output_tokens":2647,"usd":0.049168,"stage2_stop_reason":"end_turn"},"total_usd":0.067823,"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\": 2001,\n      \"finding\": \"Trx-Px2 (the larger of the two P. falciparum 2-Cys peroxiredoxins, 24.6 kDa) was recombinantly expressed and found to be active in the glutamine synthetase protector assay, demonstrating peroxidase/antioxidant activity. In oxidizing conditions it is converted to a faster-migrating species on SDS-PAGE, consistent with intramolecular disulfide formation as a regulatory mechanism.\",\n      \"method\": \"Recombinant overexpression in E. coli; glutamine synthetase protector assay; SDS-PAGE under oxidizing conditions\",\n      \"journal\": \"European journal of biochemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — in vitro enzymatic assay with recombinant protein, single lab, single study; kinetic characterization was reported only for the smaller paralog (PfTPx1), not Trx-Px2 specifically\",\n      \"pmids\": [\"11231293\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2005,\n      \"finding\": \"Trx-Px2 (PfTPx-2) localizes to the mitochondria of P. falciparum erythrocytic-stage parasites and is expressed during the trophozoite and schizont stages, consistent with a role in detoxifying ROS generated by the mitochondrial respiratory chain.\",\n      \"method\": \"Confocal laser scanning microscopy with subcellular localization; Western blotting; real-time quantitative RT-PCR\",\n      \"journal\": \"Parasitology international\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — direct localization by confocal microscopy corroborated by Western blot and RT-PCR in a single lab; functional consequence inferred but not experimentally proven\",\n      \"pmids\": [\"15710548\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2006,\n      \"finding\": \"Trx-Px2 (the mitochondrial peroxiredoxin of P. falciparum) was structurally and biochemically characterized: its crystal structure revealed a fold typical of 2-Cys peroxiredoxins with a dimeric form bearing an intermolecular disulfide between Cys67 and Cys187; in solution it exists primarily as a homodecamer. Kinetically, it strongly prefers the mitochondrial thioredoxin PfTrx2 over the cytosolic PfTrx1 as a reducing partner (KM 11.6 µM vs. 130.4 µM). Substitution of residues Asn62/Tyr63 and Phe139/Ala140 reduced the KM for Trx1 but had no effect on the KM for Trx2, implicating these residues in substrate discrimination. GFP-fusion imaging in erythrocytic stages confirmed mitochondrial localization.\",\n      \"method\": \"X-ray crystallography; in vitro kinetic assay with recombinant protein; site-directed mutagenesis; GFP-fusion live imaging in parasite erythrocytic stages; solution studies (oligomeric state)\",\n      \"journal\": \"Molecular microbiology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — crystal structure solved, kinetics determined with recombinant protein, active-site mutagenesis performed, and mitochondrial localization independently confirmed by GFP imaging; multiple orthogonal methods in one rigorous study\",\n      \"pmids\": [\"16879648\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2012,\n      \"finding\": \"Genetic disruption of the Trx-Px2 ortholog (pbtpx-2) in P. berghei showed that Trx-Px2 is not essential for asexual blood-stage growth or mosquito midgut oocyst development; KO parasites multiplied at rates comparable to wild-type. A minor delay (1 day) in peak gametocytemia was observed but peak gametocyte numbers were comparable.\",\n      \"method\": \"Gene disruption (knockout) in P. berghei; RT-PCR and Western blot confirmation of null expression; in vivo growth assays in mice and mosquito infection assays\",\n      \"journal\": \"Parasites & vectors\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — clean gene knockout with molecular confirmation and multiple independent disruptant populations; negative result (non-essential) robustly established\",\n      \"pmids\": [\"23146411\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"Trx-Px2 (PF3D7_1215000) is a mitochondrially-localized 2-Cys peroxiredoxin of P. falciparum that exists as a homodecamer in solution and as a disulfide-linked dimer (Cys67–Cys187) in its oxidized form; it preferentially uses the mitochondrial thioredoxin PfTrx2 (KM ~11.6 µM) over cytosolic PfTrx1 (KM ~130 µM) as its reductant, with residues Asn62/Tyr63 and Phe139/Ala140 contributing to this substrate discrimination, and it is not essential for blood-stage or mosquito-stage development in P. berghei.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"Trx-Px2 (PF3D7_1215000) is a mitochondrially-localized 2-Cys peroxiredoxin of Plasmodium falciparum that provides thioredoxin-dependent antioxidant defense against reactive oxygen species generated during erythrocytic-stage metabolism [#1, #2]. The recombinant protein exhibits peroxidase/antioxidant activity in vitro and, under oxidizing conditions, converts to a faster-migrating disulfide-bonded species, consistent with redox-regulated catalysis through intramolecular/intermolecular disulfide formation [#0]. Structurally it adopts the canonical 2-Cys peroxiredoxin fold, exists predominantly as a homodecamer in solution, and forms a dimer bearing an intermolecular Cys67\\u2013Cys187 disulfide in its oxidized state [#2]. Functionally, it discriminates between reducing partners, strongly preferring the mitochondrial thioredoxin PfTrx2 (KM 11.6 \\u00b5M) over cytosolic PfTrx1 (KM 130.4 \\u00b5M), with residues Asn62/Tyr63 and Phe139/Ala140 contributing to this substrate selectivity [#2]. Its subcellular residence was confirmed by both antibody-based confocal microscopy and GFP-fusion live imaging in erythrocytic stages, where expression peaks in trophozoite and schizont stages [#1, #2]. Genetic disruption of the P. berghei ortholog established that Trx-Px2 is dispensable for asexual blood-stage growth and mosquito midgut oocyst development, indicating functional redundancy in vivo despite its defined biochemical role [#3].\"\n  ,\n  \"teleology\": [\n    {\n      \"year\": 2001,\n      \"claim\": \"Whether the larger P. falciparum 2-Cys peroxiredoxin possessed enzymatic antioxidant activity was unknown; recombinant expression established it as a functional peroxidase whose migration shifts under oxidizing conditions, pointing to disulfide-based redox regulation.\",\n      \"evidence\": \"Recombinant expression in E. coli, glutamine synthetase protector assay, and SDS-PAGE under oxidizing conditions\",\n      \"pmids\": [\"11231293\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Kinetic constants were not determined for Trx-Px2 specifically in this study\",\n        \"The physiological electron donor was not identified\",\n        \"Single lab, single in vitro assay\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2005,\n      \"claim\": \"The subcellular compartment and stage-specific expression of Trx-Px2 were undefined; localization to the mitochondrion in trophozoite and schizont stages placed it at the site of respiratory-chain ROS production.\",\n      \"evidence\": \"Confocal microscopy, Western blotting, and real-time quantitative RT-PCR in erythrocytic-stage P. falciparum\",\n      \"pmids\": [\"15710548\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"The ROS-detoxification role at the mitochondrion was inferred, not directly demonstrated\",\n        \"Reducing partner not established in this study\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2006,\n      \"claim\": \"The structure, oligomeric state, and reductant specificity of Trx-Px2 were unknown; a crystal structure, solution studies, kinetics, and mutagenesis established its 2-Cys peroxiredoxin fold, homodecameric assembly, Cys67\\u2013Cys187 disulfide dimer, and strong preference for mitochondrial PfTrx2, defining a mitochondrial thioredoxin-peroxiredoxin redox couple.\",\n      \"evidence\": \"X-ray crystallography, in vitro kinetics with recombinant protein, site-directed mutagenesis (Asn62/Tyr63, Phe139/Ala140), and GFP-fusion live imaging\",\n      \"pmids\": [\"16879648\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"In vivo requirement for the PfTrx2 preference was not tested\",\n        \"The peroxide substrate range in vivo was not defined\",\n        \"Regulatory role of oligomeric switching not established in cells\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2012,\n      \"claim\": \"Whether the well-characterized mitochondrial peroxiredoxin is required for parasite viability was unknown; knockout of the P. berghei ortholog showed it is dispensable for asexual blood-stage growth and mosquito oocyst development, revealing functional redundancy despite its defined biochemistry.\",\n      \"evidence\": \"Gene disruption in P. berghei with RT-PCR/Western confirmation, in vivo mouse growth assays, and mosquito infection assays\",\n      \"pmids\": [\"23146411\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Redundant or compensating antioxidant systems were not identified\",\n        \"The minor delay in peak gametocytemia was not mechanistically explained\",\n        \"Result obtained in P. berghei, not P. falciparum\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The in vivo antioxidant substrates, the compensating pathways underlying its dispensability, and the physiological significance of its decamer\\u2013dimer redox switch remain unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No physiological peroxide substrate identified in parasites\",\n        \"Redundant antioxidant partners masking the KO phenotype are unknown\",\n        \"P. falciparum genetic requirement not directly tested\"\n      ],\n      \"attribution\": []\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0051920\", \"supporting_discovery_ids\": [0, 2]},\n      {\"term_id\": \"GO:0008379\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0015035\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005739\", \"supporting_discovery_ids\": [1, 2]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0034599\", \"supporting_discovery_ids\": [0, 1]},\n      {\"term_id\": \"GO:0045454\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"complexes\": [\n      \"Homodecamer in solution; oxidized disulfide-linked (Cys67-Cys187) dimer\"\n    ],\n    \"partners\": [\n      \"PfTrx2 (mitochondrial thioredoxin; preferred reductant, KM 11.6 \\u00b5M)\",\n      \"PfTrx1 (cytosolic thioredoxin; poor reductant, KM 130.4 \\u00b5M)\"\n    ],\n    \"other_free_text\": [\n      \"24.6 kDa 2-Cys peroxiredoxin; substrate discrimination residues Asn62/Tyr63 and Phe139/Ala140 [#2]\",\n      \"Non-essential for asexual blood-stage growth and mosquito oocyst development in P. berghei; minor delay in peak gametocytemia [#3]\"\n    ]\n  }\n}\n```","audit_flag":{"gene":"PF3D7_1215000","tier":"IDENTITY_CHECK","verdict":"identity unverified","subtype":"names_other_cards","uniprot_band":"","rules_fired":"R12","issue":"No cited paper names this card; 4 of 4 cited papers name other catalogue genes (PF3D7_1438900, PF3D7_1457200, PF3D7_0802200). The summary may describe one of those genes."},"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_1215000","name":null,"product":"thioredoxin peroxidase 2","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_1430800","name":null,"product":"thioredoxin peroxidase 2, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_1434500","name":null,"product":"thioredoxin peroxidase 2, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"Trx-Px2","evaluation":null}