{"gene":"PF3D7_0512000","run_date":"2026-09-08T19:44:17","timeline":{"discoveries":[{"year":2022,"finding":"PF3D7_0512000 (PfPFD6) physically interacts with merozoite surface protein-1 (MSP-1) of P. falciparum, as demonstrated by pull-down assay; in silico analysis identified critical residues involved in the interaction, suggesting PfPFD6 may stabilize or traffic MSP-1.","method":"Pull-down assay (affinity precipitation) and in silico interaction analysis","journal":"FEBS open bio","confidence":"Medium","confidence_rationale":"Tier 3 / Weak — single Co-IP/pull-down from a single lab without reciprocal validation or functional rescue","pmids":["33145997"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2022,"finding":"PF3D7_0512000 (PfPFD6) is significantly expressed at the trophozoite and schizont stages of the asexual intraerythrocytic cycle of P. falciparum.","method":"Stage-specific expression analysis (experimental, method details not specified beyond 'analyzed expression')","journal":"FEBS open bio","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, single method, limited methodological detail in abstract","pmids":["33145997"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2024,"finding":"PF3D7_0512000 (PfPFD6) interacts with Kelch13 protein in P. falciparum intraerythrocytic parasites, as shown by immunoprecipitation coupled to MS/MS analysis, linking PfPFD6 to the artemisinin resistance mechanism.","method":"Immunoprecipitation coupled MS/MS analysis","journal":"The Journal of biological chemistry","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal IP-MS in parasites, supported by orthologous yeast complementation experiment, single lab","pmids":["38925325"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":"3D7"}]},{"year":2024,"finding":"PF3D7_0512000 (PfPFD6) participates in formation of the heterohexameric prefoldin complex with the other five P. falciparum prefoldin subunits (PFD1–5), as revealed by systematic biophysical interaction analysis among all subunits.","method":"Biophysical interaction analysis (systematic pairwise subunit interaction assays)","journal":"The Journal of biological chemistry","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — systematic biophysical analysis across all subunits, single lab","pmids":["38925325"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2024,"finding":"Expression of PfPFD6 (PF3D7_0512000) in orthologous yeast PFD6 mutants reverted the yeast phenotype to artemisinin resistance, establishing a causative functional role for PfPFD6 in the artemisinin resistance mechanism via genetic complementation.","method":"Heterologous complementation in yeast PFD6 mutants; ring survival assays","journal":"The Journal of biological chemistry","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — genetic epistasis via cross-species complementation, single lab, functional phenotypic readout","pmids":["38925325"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":"3D7"}]},{"year":2024,"finding":"PF3D7_0512000 (PfPFD6) interacts with α-tubulin-I in P. falciparum, as shown by immunoprecipitation MS/MS; this interaction, along with the PfPFD6–MSP-1 interaction, is inhibited by the FDA-approved drug Biperiden, which disrupts prefoldin complex formation.","method":"Immunoprecipitation coupled MS/MS; drug inhibition assay with Biperiden","journal":"The Journal of biological chemistry","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — IP-MS identification of substrate plus pharmacological disruption in two parasite strains, single lab","pmids":["38925325"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":"3D7"}]}],"current_model":"PF3D7_0512000 (PfPFD6) is a beta subunit of the P. falciparum heterohexameric prefoldin co-chaperone complex that is expressed predominantly at trophozoite and schizont stages; it physically interacts with MSP-1 and α-tubulin-I (likely as substrates for folding/trafficking) and with Kelch13 (linking it to artemisinin resistance), and its functional expression in yeast PFD6 mutants restores an artemisinin-resistance phenotype, establishing a causative role in the unfolded protein response pathway underlying artemisinin resistance."},"narrative":{"mechanistic_narrative":"PF3D7_0512000 (PfPFD6) is a subunit of the P. falciparum prefoldin co-chaperone system, participating in formation of the heterohexameric prefoldin complex together with the other five parasite prefoldin subunits (PFD1–5) [PMID:38925325]. Consistent with a chaperone role, PfPFD6 physically engages client proteins including merozoite surface protein-1 (MSP-1) [PMID:33145997] and α-tubulin-I [PMID:38925325], interactions that are disrupted by the FDA-approved drug Biperiden, which blocks prefoldin complex assembly [PMID:38925325]. PfPFD6 also interacts with Kelch13 in intraerythrocytic parasites, and heterologous expression of PfPFD6 in yeast PFD6 mutants confers an artemisinin-resistance phenotype, establishing a causative functional link between PfPFD6 and the artemisinin resistance mechanism [PMID:38925325]. PfPFD6 is expressed predominantly at the trophozoite and schizont stages of the asexual intraerythrocytic cycle [PMID:33145997]. Beyond these interaction, complementation, and expression findings, no further mechanistic detail (e.g. structure or folding kinetics) has been characterized in the available corpus.","teleology":[{"year":2022,"claim":"To ask whether PfPFD6 has identifiable client proteins, its physical association with a candidate parasite substrate was tested, establishing MSP-1 as a binding partner.","evidence":"Pull-down assay with in silico interaction analysis in P. falciparum","pmids":["33145997"],"confidence":"Medium","gaps":["Single Co-IP/pull-down without reciprocal validation or functional rescue","Does not demonstrate that PfPFD6 actually folds or traffics MSP-1","Interaction shown for PfPFD6 monomer, not within the assembled complex"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2022,"claim":"To place PfPFD6 in the parasite life cycle, its stage-specific expression was profiled, showing enrichment at trophozoite and schizont stages.","evidence":"Stage-specific expression analysis in P. falciparum","pmids":["33145997"],"confidence":"Low","gaps":["Limited methodological detail reported for the expression assay","No quantification of protein versus transcript levels","Does not address subcellular localization"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2024,"claim":"To establish whether PfPFD6 assembles into a functional co-chaperone, systematic subunit interaction analysis confirmed it participates in the heterohexameric prefoldin complex with PFD1–5.","evidence":"Systematic pairwise biophysical interaction assays across all six subunits in P. falciparum","pmids":["38925325"],"confidence":"Medium","gaps":["No structural model of the assembled complex","Stoichiometry and quaternary architecture not resolved","Single lab"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2024,"claim":"To connect PfPFD6 to drug resistance, IP-MS in parasites and cross-species complementation tested its relationship to Kelch13 and artemisinin resistance, showing PfPFD6 binds Kelch13 and that its expression confers resistance in yeast PFD6 mutants.","evidence":"Immunoprecipitation coupled MS/MS in P. falciparum 3D7 plus heterologous complementation and ring survival assays in yeast PFD6 mutants","pmids":["38925325"],"confidence":"Medium","gaps":["Direct genetic manipulation of PfPFD6 in the parasite not shown","Mechanistic link between prefoldin folding activity and resistance not resolved","Single lab"],"attribution":[{"species":"Plasmodium falciparum","strain":"3D7"}]},{"year":2024,"claim":"To identify additional clients and a pharmacological handle, IP-MS identified α-tubulin-I as a PfPFD6 partner and showed Biperiden disrupts both PfPFD6–α-tubulin-I and PfPFD6–MSP-1 interactions by blocking complex formation.","evidence":"Immunoprecipitation coupled MS/MS and Biperiden inhibition assay in P. falciparum","pmids":["38925325"],"confidence":"Medium","gaps":["Whether Biperiden acts directly on PfPFD6 versus another subunit not resolved","Folding outcome for α-tubulin-I not measured","Single lab"],"attribution":[{"species":"Plasmodium falciparum","strain":"3D7"}]},{"year":null,"claim":"How PfPFD6 mechanistically contributes within the prefoldin complex to client folding/trafficking and to artemisinin resistance in the parasite itself remains unresolved.","evidence":"","pmids":[],"confidence":"Low","gaps":["No direct genetic knockout/knockdown of PfPFD6 in P. falciparum reported","No structural characterization of PfPFD6 or its client-bound complex","Causal chain from prefoldin folding activity to Kelch13-mediated resistance not defined"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["Heterohexameric prefoldin complex (PFD1-6)"],"partners":["MSP-1 (MEROZOITE SURFACE PROTEIN-1)","ALPHA-TUBULIN-I","KELCH13","PREFOLDIN SUBUNITS PFD1-5"],"other_free_text":["Expressed predominantly at trophozoite and schizont stages of the asexual intraerythrocytic cycle [#1]","PfPFD6 interactions with MSP-1 and alpha-tubulin-I are disrupted by the FDA-approved drug Biperiden [#5]","Expression of PfPFD6 in yeast PFD6 mutants confers an artemisinin-resistance phenotype [#4]"]}},"prefetch_data":{},"corpus_meta":[{"pmid":"33145997","id":"PMC_33145997","title":"Prefoldin subunit 6 of Plasmodium falciparum binds merozoite surface protein-1.","date":"2022","source":"FEBS open bio","url":"https://pubmed.ncbi.nlm.nih.gov/33145997","citation_count":4,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PFD6","prefoldin subunit 6","PfPFD6"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"38925325","id":"PMC_38925325","title":"Prefoldins are novel regulators of the unfolded protein response in artemisinin resistant Plasmodium falciparum malaria.","date":"2024","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/38925325","citation_count":2,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PFD6","PfPFD6"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"35111762","id":"","title":"Prefoldin Function in Cellular Protein Homeostasis and Human Diseases.","date":"2022","source":"Frontiers in cell and developmental biology","url":"https://pubmed.ncbi.nlm.nih.gov/35111762","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PFD6"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":4896,"output_tokens":1543,"usd":0.018916,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6518,"output_tokens":2505,"usd":0.047607,"stage2_stop_reason":"end_turn"},"total_usd":0.066523,"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\": 2022,\n      \"finding\": \"PF3D7_0512000 (PfPFD6) physically interacts with merozoite surface protein-1 (MSP-1) of P. falciparum, as demonstrated by pull-down assay; in silico analysis identified critical residues involved in the interaction, suggesting PfPFD6 may stabilize or traffic MSP-1.\",\n      \"method\": \"Pull-down assay (affinity precipitation) and in silico interaction analysis\",\n      \"journal\": \"FEBS open bio\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single Co-IP/pull-down from a single lab without reciprocal validation or functional rescue\",\n      \"pmids\": [\"33145997\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"PF3D7_0512000 (PfPFD6) is significantly expressed at the trophozoite and schizont stages of the asexual intraerythrocytic cycle of P. falciparum.\",\n      \"method\": \"Stage-specific expression analysis (experimental, method details not specified beyond 'analyzed expression')\",\n      \"journal\": \"FEBS open bio\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, single method, limited methodological detail in abstract\",\n      \"pmids\": [\"33145997\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"PF3D7_0512000 (PfPFD6) interacts with Kelch13 protein in P. falciparum intraerythrocytic parasites, as shown by immunoprecipitation coupled to MS/MS analysis, linking PfPFD6 to the artemisinin resistance mechanism.\",\n      \"method\": \"Immunoprecipitation coupled MS/MS analysis\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal IP-MS in parasites, supported by orthologous yeast complementation experiment, single lab\",\n      \"pmids\": [\"38925325\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"3D7\"}\n      ]\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"PF3D7_0512000 (PfPFD6) participates in formation of the heterohexameric prefoldin complex with the other five P. falciparum prefoldin subunits (PFD1–5), as revealed by systematic biophysical interaction analysis among all subunits.\",\n      \"method\": \"Biophysical interaction analysis (systematic pairwise subunit interaction assays)\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — systematic biophysical analysis across all subunits, single lab\",\n      \"pmids\": [\"38925325\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"Expression of PfPFD6 (PF3D7_0512000) in orthologous yeast PFD6 mutants reverted the yeast phenotype to artemisinin resistance, establishing a causative functional role for PfPFD6 in the artemisinin resistance mechanism via genetic complementation.\",\n      \"method\": \"Heterologous complementation in yeast PFD6 mutants; ring survival assays\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — genetic epistasis via cross-species complementation, single lab, functional phenotypic readout\",\n      \"pmids\": [\"38925325\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"3D7\"}\n      ]\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"PF3D7_0512000 (PfPFD6) interacts with α-tubulin-I in P. falciparum, as shown by immunoprecipitation MS/MS; this interaction, along with the PfPFD6–MSP-1 interaction, is inhibited by the FDA-approved drug Biperiden, which disrupts prefoldin complex formation.\",\n      \"method\": \"Immunoprecipitation coupled MS/MS; drug inhibition assay with Biperiden\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — IP-MS identification of substrate plus pharmacological disruption in two parasite strains, single lab\",\n      \"pmids\": [\"38925325\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"3D7\"}\n      ]\n    }\n  ],\n  \"current_model\": \"PF3D7_0512000 (PfPFD6) is a beta subunit of the P. falciparum heterohexameric prefoldin co-chaperone complex that is expressed predominantly at trophozoite and schizont stages; it physically interacts with MSP-1 and α-tubulin-I (likely as substrates for folding/trafficking) and with Kelch13 (linking it to artemisinin resistance), and its functional expression in yeast PFD6 mutants restores an artemisinin-resistance phenotype, establishing a causative role in the unfolded protein response pathway underlying artemisinin resistance.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"PF3D7_0512000 (PfPFD6) is a subunit of the P. falciparum prefoldin co-chaperone system, participating in formation of the heterohexameric prefoldin complex together with the other five parasite prefoldin subunits (PFD1–5) [#3]. Consistent with a chaperone role, PfPFD6 physically engages client proteins including merozoite surface protein-1 (MSP-1) [#0] and α-tubulin-I [#5], interactions that are disrupted by the FDA-approved drug Biperiden, which blocks prefoldin complex assembly [#5]. PfPFD6 also interacts with Kelch13 in intraerythrocytic parasites, and heterologous expression of PfPFD6 in yeast PFD6 mutants confers an artemisinin-resistance phenotype, establishing a causative functional link between PfPFD6 and the artemisinin resistance mechanism [#2, #4]. PfPFD6 is expressed predominantly at the trophozoite and schizont stages of the asexual intraerythrocytic cycle [#1]. Beyond these interaction, complementation, and expression findings, no further mechanistic detail (e.g. structure or folding kinetics) has been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2022,\n      \"claim\": \"To ask whether PfPFD6 has identifiable client proteins, its physical association with a candidate parasite substrate was tested, establishing MSP-1 as a binding partner.\",\n      \"evidence\": \"Pull-down assay with in silico interaction analysis in P. falciparum\",\n      \"pmids\": [\"33145997\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Single Co-IP/pull-down without reciprocal validation or functional rescue\",\n        \"Does not demonstrate that PfPFD6 actually folds or traffics MSP-1\",\n        \"Interaction shown for PfPFD6 monomer, not within the assembled complex\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"To place PfPFD6 in the parasite life cycle, its stage-specific expression was profiled, showing enrichment at trophozoite and schizont stages.\",\n      \"evidence\": \"Stage-specific expression analysis in P. falciparum\",\n      \"pmids\": [\"33145997\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"Limited methodological detail reported for the expression assay\",\n        \"No quantification of protein versus transcript levels\",\n        \"Does not address subcellular localization\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"To establish whether PfPFD6 assembles into a functional co-chaperone, systematic subunit interaction analysis confirmed it participates in the heterohexameric prefoldin complex with PFD1–5.\",\n      \"evidence\": \"Systematic pairwise biophysical interaction assays across all six subunits in P. falciparum\",\n      \"pmids\": [\"38925325\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No structural model of the assembled complex\",\n        \"Stoichiometry and quaternary architecture not resolved\",\n        \"Single lab\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"To connect PfPFD6 to drug resistance, IP-MS in parasites and cross-species complementation tested its relationship to Kelch13 and artemisinin resistance, showing PfPFD6 binds Kelch13 and that its expression confers resistance in yeast PFD6 mutants.\",\n      \"evidence\": \"Immunoprecipitation coupled MS/MS in P. falciparum 3D7 plus heterologous complementation and ring survival assays in yeast PFD6 mutants\",\n      \"pmids\": [\"38925325\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Direct genetic manipulation of PfPFD6 in the parasite not shown\",\n        \"Mechanistic link between prefoldin folding activity and resistance not resolved\",\n        \"Single lab\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"3D7\"}]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"To identify additional clients and a pharmacological handle, IP-MS identified α-tubulin-I as a PfPFD6 partner and showed Biperiden disrupts both PfPFD6–α-tubulin-I and PfPFD6–MSP-1 interactions by blocking complex formation.\",\n      \"evidence\": \"Immunoprecipitation coupled MS/MS and Biperiden inhibition assay in P. falciparum\",\n      \"pmids\": [\"38925325\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Whether Biperiden acts directly on PfPFD6 versus another subunit not resolved\",\n        \"Folding outcome for α-tubulin-I not measured\",\n        \"Single lab\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"3D7\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How PfPFD6 mechanistically contributes within the prefoldin complex to client folding/trafficking and to artemisinin resistance in the parasite itself remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No direct genetic knockout/knockdown of PfPFD6 in P. falciparum reported\",\n        \"No structural characterization of PfPFD6 or its client-bound complex\",\n        \"Causal chain from prefoldin folding activity to Kelch13-mediated resistance not defined\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0051082\", \"supporting_discovery_ids\": [0, 5]},\n      {\"term_id\": \"GO:0005515\", \"supporting_discovery_ids\": [0, 2, 3, 5]}\n    ],\n    \"localization\": [],\n    \"pathway\": [\n      {\"term_id\": \"GO:0006457\", \"supporting_discovery_ids\": [0, 5]}\n    ],\n    \"complexes\": [\n      \"Heterohexameric prefoldin complex (PFD1-6)\"\n    ],\n    \"partners\": [\n      \"MSP-1 (merozoite surface protein-1)\",\n      \"alpha-tubulin-I\",\n      \"Kelch13\",\n      \"Prefoldin subunits PFD1-5\"\n    ],\n    \"other_free_text\": [\n      \"Expressed predominantly at trophozoite and schizont stages of the asexual intraerythrocytic cycle [#1]\",\n      \"PfPFD6 interactions with MSP-1 and alpha-tubulin-I are disrupted by the FDA-approved drug Biperiden [#5]\",\n      \"Expression of PfPFD6 in yeast PFD6 mutants confers an artemisinin-resistance phenotype [#4]\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_0512000","name":null,"product":"prefoldin subunit 6","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_1111600","name":null,"product":"prefoldin subunit 6, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_1021600","name":null,"product":"prefoldin subunit 6, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"PFD6","evaluation":null}