{"gene":"PF3D7_1129100","run_date":"2026-09-08T12:51:28","timeline":{"discoveries":[{"year":2017,"finding":"PV1 (PF3D7_1129100) is a component of a novel protein complex called EPIC (Exported Protein-Interacting Complex) located in the parasitophorous vacuole. Inducible knockdown of PV1 results in altered knob morphology, reduced cell rigidity, and decreased binding to CD36, establishing a functional role for PV1 in virulence determinant trafficking.","method":"Epitope-tagged minimal construct co-immunoprecipitation to define the EPIC interactome; inducible knockdown with phenotypic readouts (knob morphology, cell rigidity, CD36 binding)","journal":"Nature Communications","confidence":"High","confidence_rationale":"Tier 2 / Moderate — reciprocal Co-IP defining the complex plus inducible knockdown with multiple orthogonal phenotypic readouts in a single study","pmids":["28691708"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2017,"finding":"Deletion of the Plasmodium berghei homologue of PV1 is associated with attenuation of parasite virulence in vivo.","method":"Genetic deletion in P. berghei followed by in vivo mouse infection assay","journal":"Nature Communications","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — clean genetic knockout with in vivo phenotypic readout but single study, P. berghei homologue only","pmids":["28691708"],"is_preprint":false,"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2018,"finding":"PV1 (PF3D7_1129100) localizes to merozoite dense granules in addition to the parasitophorous vacuole, and partially co-localizes with PTEX component EXP2, suggesting it acts as a PTEX accessory molecule.","method":"Structured illumination microscopy (SIM) with co-localization analysis","journal":"Scientific Reports","confidence":"Medium","confidence_rationale":"Tier 3 / Weak — high-resolution imaging showing co-localization but no functional validation of the PTEX accessory role itself","pmids":["29487358"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2018,"finding":"PV1 (PF3D7_1129100) directly interacts with the exported protein PTP5, and this interaction is mediated through a C-terminal PfPV1 High-affinity Region (PHR) on PTP5. A PTP5 mutant lacking PHR (PTP5ΔPHR) shows export arrest, indicating PHR is essential for PTP5 export.","method":"Co-immunoprecipitation with anti-PV1 antibody; surface plasmon resonance (SPR) to confirm direct binding; SIM analysis of PTP5ΔPHR export arrest","journal":"Scientific Reports","confidence":"High","confidence_rationale":"Tier 1–2 / Moderate — direct binding confirmed by SPR (in vitro), Co-IP, and functional mutagenesis (domain deletion) with export phenotype readout, multiple orthogonal methods in one study","pmids":["29487358"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2011,"finding":"Repeated failure to recover PV1 (PF3D7_1129100) deletion mutants despite verified accessibility of the pv1 locus to gene targeting provides strong genetic evidence that PV1 is essential for intra-erythrocytic survival of P. falciparum.","method":"Gene knockout attempts with control gene-targeting experiments to verify locus accessibility","journal":"PloS One","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — negative-selection genetic essentiality evidence with verified controls, single lab, single method","pmids":["21483790"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2020,"finding":"Recombinant PV1 (PF3D7_1129100) forms tetramers as its structural unit and displays chaperone-like activity in vitro, including the ability to substitute for CtHsp40 in a CtHsp104/CtHsp70/CtHsp40 protein disaggregation system. PV1 may interact with HSP101 to deliver PV proteins to PTEX.","method":"Protein expression and purification; chaperone activity assays in vitro; small-angle X-ray scattering (SAXS) or similar biophysical characterization for tetramer identification; functional substitution assay in disaggregation system","journal":"International Journal of Molecular Sciences","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — in vitro biochemical reconstitution and functional assay, but single lab study with limited replication and the HSP101 interaction inferred rather than directly demonstrated","pmids":["33207549"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"PV1 (PF3D7_1129100) is an essential parasitophorous vacuole and merozoite dense granule protein in P. falciparum that forms tetramers with chaperone-like activity, directly binds exported substrate proteins (e.g. PTP5) via a defined high-affinity region, participates in the EPIC complex in the PV, co-localizes with PTEX component EXP2, and is required for proper knob morphology, cell rigidity, CD36-mediated cytoadherence, and overall intra-erythrocytic survival, likely by capturing PV-lumenal cargo and facilitating their delivery to PTEX for export."},"narrative":{"mechanistic_narrative":"PV1 (PF3D7_1129100) is an essential parasitophorous vacuole protein of Plasmodium falciparum that functions in the trafficking of exported virulence determinants across the parasite-host interface [PMID:28691708, PMID:21483790]. Repeated failure to recover deletion mutants at an accessible locus establishes that PV1 is required for intra-erythrocytic survival [PMID:21483790]. PV1 is a constituent of the parasitophorous-vacuole-localized EPIC (Exported Protein-Interacting Complex), and its inducible knockdown produces altered knob morphology, reduced cell rigidity, and decreased CD36-mediated cytoadherence, linking it functionally to host-cell remodeling [PMID:28691708]. Beyond the vacuole, PV1 localizes to merozoite dense granules and partially co-localizes with the PTEX component EXP2, consistent with a role as a PTEX-associated accessory factor [PMID:29487358]. Mechanistically, PV1 directly binds the exported protein PTP5 through a defined C-terminal PfPV1 High-affinity Region (PHR), and deletion of this region arrests PTP5 export, demonstrating that PV1-cargo engagement is required for substrate delivery [PMID:29487358]. Recombinant PV1 assembles into tetramers and exhibits chaperone-like disaggregation activity in vitro, providing a biochemical basis for capturing PV-lumenal cargo prior to export [PMID:33207549]. In P. berghei, deletion of the PV1 homologue attenuates parasite virulence in vivo, consistent with a conserved role in pathogenesis [PMID:28691708].","teleology":[{"year":2011,"claim":"Whether PV1 is dispensable was unknown; the inability to recover knockouts at a targetable locus established that PV1 is essential for blood-stage growth.","evidence":"Repeated gene-knockout attempts with control experiments verifying locus accessibility in P. falciparum","pmids":["21483790"],"confidence":"Medium","gaps":["Negative-selection evidence only, no conditional system to define the stage or process requiring PV1","Single lab, single method"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2017,"claim":"The molecular context of PV1 was unresolved; defining the EPIC complex and its knockdown phenotypes established PV1 as a PV-resident factor for virulence determinant trafficking.","evidence":"Epitope-tagged co-immunoprecipitation defining the EPIC interactome plus inducible knockdown with knob morphology, cell rigidity, and CD36 binding readouts in P. falciparum","pmids":["28691708"],"confidence":"High","gaps":["Does not identify which EPIC-associated substrates PV1 directly handles","Mechanism connecting EPIC to knob assembly not resolved"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2017,"claim":"Whether the PV1 role is conserved in vivo was untested; deletion of the P. berghei homologue attenuated virulence in a mouse model, extending the function beyond P. falciparum culture.","evidence":"Genetic deletion of the P. berghei homologue with in vivo mouse infection assay","pmids":["28691708"],"confidence":"Medium","gaps":["Homologue only, molecular mechanism of attenuation not defined","Single study"],"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2018,"claim":"How PV1 relates to the export machinery was unclear; imaging placed PV1 in merozoite dense granules and adjacent to EXP2, positioning it as a candidate PTEX accessory molecule.","evidence":"Structured illumination microscopy with co-localization analysis in P. falciparum","pmids":["29487358"],"confidence":"Medium","gaps":["Co-localization does not establish physical or functional coupling to PTEX","No functional validation of the accessory role"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2018,"claim":"It was unknown how PV1 engages export cargo; direct binding to PTP5 via the PHR region and export arrest upon PHR deletion established PV1 as a substrate-capturing factor required for export.","evidence":"Anti-PV1 co-immunoprecipitation, surface plasmon resonance for direct binding, and SIM of PTP5ΔPHR export arrest in P. falciparum","pmids":["29487358"],"confidence":"High","gaps":["Only one cargo (PTP5) shown; breadth of substrate repertoire unknown","Structural basis of the PHR-PV1 interface not resolved"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2020,"claim":"The biochemical activity underlying cargo handling was undefined; recombinant PV1 forms tetramers with chaperone-like disaggregation activity, providing a mechanism for holding cargo before PTEX delivery.","evidence":"Recombinant protein purification, biophysical tetramer characterization, and in vitro chaperone/disaggregation substitution assays in P. falciparum","pmids":["33207549"],"confidence":"Medium","gaps":["HSP101 interaction inferred, not directly demonstrated","In vitro reconstitution only; chaperone activity not validated in vivo","Single lab, limited replication"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"How PV1 hands cargo to the PTEX translocon and whether its chaperone activity operates on the broader exportome in vivo remain unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["Direct PV1-HSP101/PTEX physical coupling not demonstrated","Full substrate repertoire beyond PTP5 unknown","In vivo relevance of tetramer/chaperone activity untested"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["EPIC (Exported Protein-Interacting Complex)"],"partners":["PTP5 (DIRECT, VIA C-TERMINAL PHR REGION)","EXP2 (PARTIAL CO-LOCALIZATION)","HSP101 (INFERRED)"],"other_free_text":["Essential for P. falciparum intra-erythrocytic survival (no viable deletion mutants)","Knockdown reduces knob formation, cell rigidity, and CD36-mediated cytoadherence","Forms tetramers as its structural unit","P. berghei homologue deletion attenuates virulence in vivo"]}},"prefetch_data":{},"corpus_meta":[{"pmid":"28691708","id":"PMC_28691708","title":"An exported protein-interacting complex involved in the trafficking of virulence determinants in Plasmodium-infected erythrocytes.","date":"2017","source":"Nature communications","url":"https://pubmed.ncbi.nlm.nih.gov/28691708","citation_count":63,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PV1","parasitophorous vacuolar protein 1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"29487358","id":"PMC_29487358","title":"PV1, a novel Plasmodium falciparum merozoite dense granule protein, interacts with exported protein in infected erythrocytes.","date":"2018","source":"Scientific reports","url":"https://pubmed.ncbi.nlm.nih.gov/29487358","citation_count":28,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PV1","parasitophorous vacuolar protein 1","PfPV1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"21483790","id":"PMC_21483790","title":"Genetic evidence strongly support an essential role for PfPV1 in intra-erythrocytic growth of P. falciparum.","date":"2011","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/21483790","citation_count":21,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PV1","PfPV1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"33207549","id":"PMC_33207549","title":"PV1 Protein from Plasmodium falciparum Exhibits Chaperone-Like Functions and Cooperates with Hsp100s.","date":"2020","source":"International journal of molecular sciences","url":"https://pubmed.ncbi.nlm.nih.gov/33207549","citation_count":10,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PV1","parasitophorous vacuolar protein 1","PfPV1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":4607,"output_tokens":1669,"usd":0.019428,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6720,"output_tokens":2802,"usd":0.051825,"stage2_stop_reason":"end_turn"},"total_usd":0.071253,"stage1_batch_id":"msgbatch_01DisAaTypwmC8QwdMBuePHo","stage2_batch_id":"msgbatch_0184zxZTqxiEfdYYfPMfkqjb","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2017,\n      \"finding\": \"PV1 (PF3D7_1129100) is a component of a novel protein complex called EPIC (Exported Protein-Interacting Complex) located in the parasitophorous vacuole. Inducible knockdown of PV1 results in altered knob morphology, reduced cell rigidity, and decreased binding to CD36, establishing a functional role for PV1 in virulence determinant trafficking.\",\n      \"method\": \"Epitope-tagged minimal construct co-immunoprecipitation to define the EPIC interactome; inducible knockdown with phenotypic readouts (knob morphology, cell rigidity, CD36 binding)\",\n      \"journal\": \"Nature Communications\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal Co-IP defining the complex plus inducible knockdown with multiple orthogonal phenotypic readouts in a single study\",\n      \"pmids\": [\"28691708\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"Deletion of the Plasmodium berghei homologue of PV1 is associated with attenuation of parasite virulence in vivo.\",\n      \"method\": \"Genetic deletion in P. berghei followed by in vivo mouse infection assay\",\n      \"journal\": \"Nature Communications\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — clean genetic knockout with in vivo phenotypic readout but single study, P. berghei homologue only\",\n      \"pmids\": [\"28691708\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"PV1 (PF3D7_1129100) localizes to merozoite dense granules in addition to the parasitophorous vacuole, and partially co-localizes with PTEX component EXP2, suggesting it acts as a PTEX accessory molecule.\",\n      \"method\": \"Structured illumination microscopy (SIM) with co-localization analysis\",\n      \"journal\": \"Scientific Reports\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Weak — high-resolution imaging showing co-localization but no functional validation of the PTEX accessory role itself\",\n      \"pmids\": [\"29487358\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"PV1 (PF3D7_1129100) directly interacts with the exported protein PTP5, and this interaction is mediated through a C-terminal PfPV1 High-affinity Region (PHR) on PTP5. A PTP5 mutant lacking PHR (PTP5ΔPHR) shows export arrest, indicating PHR is essential for PTP5 export.\",\n      \"method\": \"Co-immunoprecipitation with anti-PV1 antibody; surface plasmon resonance (SPR) to confirm direct binding; SIM analysis of PTP5ΔPHR export arrest\",\n      \"journal\": \"Scientific Reports\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1–2 / Moderate — direct binding confirmed by SPR (in vitro), Co-IP, and functional mutagenesis (domain deletion) with export phenotype readout, multiple orthogonal methods in one study\",\n      \"pmids\": [\"29487358\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2011,\n      \"finding\": \"Repeated failure to recover PV1 (PF3D7_1129100) deletion mutants despite verified accessibility of the pv1 locus to gene targeting provides strong genetic evidence that PV1 is essential for intra-erythrocytic survival of P. falciparum.\",\n      \"method\": \"Gene knockout attempts with control gene-targeting experiments to verify locus accessibility\",\n      \"journal\": \"PloS One\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — negative-selection genetic essentiality evidence with verified controls, single lab, single method\",\n      \"pmids\": [\"21483790\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"Recombinant PV1 (PF3D7_1129100) forms tetramers as its structural unit and displays chaperone-like activity in vitro, including the ability to substitute for CtHsp40 in a CtHsp104/CtHsp70/CtHsp40 protein disaggregation system. PV1 may interact with HSP101 to deliver PV proteins to PTEX.\",\n      \"method\": \"Protein expression and purification; chaperone activity assays in vitro; small-angle X-ray scattering (SAXS) or similar biophysical characterization for tetramer identification; functional substitution assay in disaggregation system\",\n      \"journal\": \"International Journal of Molecular Sciences\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — in vitro biochemical reconstitution and functional assay, but single lab study with limited replication and the HSP101 interaction inferred rather than directly demonstrated\",\n      \"pmids\": [\"33207549\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"PV1 (PF3D7_1129100) is an essential parasitophorous vacuole and merozoite dense granule protein in P. falciparum that forms tetramers with chaperone-like activity, directly binds exported substrate proteins (e.g. PTP5) via a defined high-affinity region, participates in the EPIC complex in the PV, co-localizes with PTEX component EXP2, and is required for proper knob morphology, cell rigidity, CD36-mediated cytoadherence, and overall intra-erythrocytic survival, likely by capturing PV-lumenal cargo and facilitating their delivery to PTEX for export.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"PV1 (PF3D7_1129100) is an essential parasitophorous vacuole protein of Plasmodium falciparum that functions in the trafficking of exported virulence determinants across the parasite-host interface [#0, #4]. Repeated failure to recover deletion mutants at an accessible locus establishes that PV1 is required for intra-erythrocytic survival [#4]. PV1 is a constituent of the parasitophorous-vacuole-localized EPIC (Exported Protein-Interacting Complex), and its inducible knockdown produces altered knob morphology, reduced cell rigidity, and decreased CD36-mediated cytoadherence, linking it functionally to host-cell remodeling [#0]. Beyond the vacuole, PV1 localizes to merozoite dense granules and partially co-localizes with the PTEX component EXP2, consistent with a role as a PTEX-associated accessory factor [#2]. Mechanistically, PV1 directly binds the exported protein PTP5 through a defined C-terminal PfPV1 High-affinity Region (PHR), and deletion of this region arrests PTP5 export, demonstrating that PV1-cargo engagement is required for substrate delivery [#3]. Recombinant PV1 assembles into tetramers and exhibits chaperone-like disaggregation activity in vitro, providing a biochemical basis for capturing PV-lumenal cargo prior to export [#5]. In P. berghei, deletion of the PV1 homologue attenuates parasite virulence in vivo, consistent with a conserved role in pathogenesis [#1].\",\n  \"teleology\": [\n    {\n      \"year\": 2011,\n      \"claim\": \"Whether PV1 is dispensable was unknown; the inability to recover knockouts at a targetable locus established that PV1 is essential for blood-stage growth.\",\n      \"evidence\": \"Repeated gene-knockout attempts with control experiments verifying locus accessibility in P. falciparum\",\n      \"pmids\": [\"21483790\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Negative-selection evidence only, no conditional system to define the stage or process requiring PV1\", \"Single lab, single method\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"The molecular context of PV1 was unresolved; defining the EPIC complex and its knockdown phenotypes established PV1 as a PV-resident factor for virulence determinant trafficking.\",\n      \"evidence\": \"Epitope-tagged co-immunoprecipitation defining the EPIC interactome plus inducible knockdown with knob morphology, cell rigidity, and CD36 binding readouts in P. falciparum\",\n      \"pmids\": [\"28691708\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Does not identify which EPIC-associated substrates PV1 directly handles\", \"Mechanism connecting EPIC to knob assembly not resolved\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"Whether the PV1 role is conserved in vivo was untested; deletion of the P. berghei homologue attenuated virulence in a mouse model, extending the function beyond P. falciparum culture.\",\n      \"evidence\": \"Genetic deletion of the P. berghei homologue with in vivo mouse infection assay\",\n      \"pmids\": [\"28691708\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Homologue only, molecular mechanism of attenuation not defined\", \"Single study\"],\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"How PV1 relates to the export machinery was unclear; imaging placed PV1 in merozoite dense granules and adjacent to EXP2, positioning it as a candidate PTEX accessory molecule.\",\n      \"evidence\": \"Structured illumination microscopy with co-localization analysis in P. falciparum\",\n      \"pmids\": [\"29487358\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Co-localization does not establish physical or functional coupling to PTEX\", \"No functional validation of the accessory role\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"It was unknown how PV1 engages export cargo; direct binding to PTP5 via the PHR region and export arrest upon PHR deletion established PV1 as a substrate-capturing factor required for export.\",\n      \"evidence\": \"Anti-PV1 co-immunoprecipitation, surface plasmon resonance for direct binding, and SIM of PTP5\\u0394PHR export arrest in P. falciparum\",\n      \"pmids\": [\"29487358\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Only one cargo (PTP5) shown; breadth of substrate repertoire unknown\", \"Structural basis of the PHR-PV1 interface not resolved\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"The biochemical activity underlying cargo handling was undefined; recombinant PV1 forms tetramers with chaperone-like disaggregation activity, providing a mechanism for holding cargo before PTEX delivery.\",\n      \"evidence\": \"Recombinant protein purification, biophysical tetramer characterization, and in vitro chaperone/disaggregation substitution assays in P. falciparum\",\n      \"pmids\": [\"33207549\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"HSP101 interaction inferred, not directly demonstrated\", \"In vitro reconstitution only; chaperone activity not validated in vivo\", \"Single lab, limited replication\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How PV1 hands cargo to the PTEX translocon and whether its chaperone activity operates on the broader exportome in vivo remain unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Direct PV1-HSP101/PTEX physical coupling not demonstrated\", \"Full substrate repertoire beyond PTP5 unknown\", \"In vivo relevance of tetramer/chaperone activity untested\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0051082\", \"supporting_discovery_ids\": [5]},\n      {\"term_id\": \"GO:0051787\", \"supporting_discovery_ids\": [3]},\n      {\"term_id\": \"GO:0042803\", \"supporting_discovery_ids\": [5]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0020003\", \"supporting_discovery_ids\": [0, 2]},\n      {\"term_id\": \"GO:0020030\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0046903\", \"supporting_discovery_ids\": [0, 3]},\n      {\"term_id\": \"GO:0065003\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"complexes\": [\n      \"EPIC (Exported Protein-Interacting Complex)\"\n    ],\n    \"partners\": [\n      \"PTP5 (direct, via C-terminal PHR region)\",\n      \"EXP2 (partial co-localization)\",\n      \"HSP101 (inferred)\"\n    ],\n    \"other_free_text\": [\n      \"Essential for P. falciparum intra-erythrocytic survival (no viable deletion mutants)\",\n      \"Knockdown reduces knob formation, cell rigidity, and CD36-mediated cytoadherence\",\n      \"Forms tetramers as its structural unit\",\n      \"P. berghei homologue deletion attenuates virulence in vivo\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_1129100","name":null,"product":"parasitophorous vacuolar protein 1","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_0919100","name":null,"product":"parasitophorous vacuolar protein 1","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_0927100","name":null,"product":"parasitophorous vacuolar protein 1, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"PV1","evaluation":null}