{"gene":"PF3D7_0823600","run_date":"2026-09-08T12:51:27","timeline":{"discoveries":[{"year":2004,"finding":"LipB (lipoyl-ACP:protein N-lipoyl transferase / octanoyl-ACP:protein N-octanoyltransferase) localizes to the apicoplast of P. falciparum intraerythrocytic stages, as demonstrated by GFP-fusion overexpression of its N-terminal targeting sequence. Functional activity was confirmed by complementation of E. coli lipB-deficient mutants. LipB constitutes part of the apicoplast-specific de novo lipoic acid synthesis pathway, distinct from the mitochondrial lipoic acid salvage pathway.","method":"GFP-fusion live imaging (N-terminal targeting sequence), bacterial complementation of lipB-deficient E. coli, Northern and Western blot","journal":"Molecular microbiology","confidence":"High","confidence_rationale":"Tier 2 / Strong — direct localization by GFP imaging plus functional complementation assay, two orthogonal methods in a single study","pmids":["15225307"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2007,"finding":"Disruption of the LipB gene in P. falciparum did not negatively affect asexual blood-stage parasite growth despite causing a >90% loss of lipoic acid in the apicoplast, demonstrating that LipB is not essential for intraerythrocytic development. Residual lipoylation of the apicoplast-located pyruvate dehydrogenase was attributed to the dual-targeted lipoate protein ligase LplA2, indicating functional redundancy in the apicoplast lipoylation pathway.","method":"Gene disruption (knockout), lipoic acid quantification, immunofluorescence/Western blot for lipoylation status","journal":"PLoS pathogens","confidence":"High","confidence_rationale":"Tier 2 / Strong — clean gene disruption with defined phenotypic readout (growth and lipoylation status), multiple orthogonal methods, independently consistent with PMID:23490300","pmids":["18069893"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2013,"finding":"LipB-deficient P. berghei sporozoites showed markedly attenuated infectivity in mice and arrested at a very late liver stage shortly before final intra-hepatic maturation, establishing that LipB is essential for liver stage development. LipB-deficient asexual blood-stage parasites grew normally under standard conditions but showed reduced growth under lipid-restricted conditions (treatment with 8-bromo-octanoate or clofibrate).","method":"Gene knockout in P. berghei, mouse infection assays, in vitro liver-stage development assay, growth assays under lipid-restricted conditions","journal":"Cellular microbiology","confidence":"High","confidence_rationale":"Tier 2 / Strong — clean knockout with in vivo and in vitro phenotypic readouts across multiple life stages, replicated across conditions","pmids":["23490300"],"is_preprint":false,"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2021,"finding":"Deletion of LipB in P. falciparum 3D7 altered expression of redox regulators in both the apicoplast and cytosol, and changed central carbon metabolism including glycolysis and TCA cycle activity. In the NF54 strain, LipB deletion prevented completion of sporogony in Anopheles mosquitoes, with no infectious sporozoites detectable, establishing LipB as essential for transmission.","method":"Gene knockout (lipB deletion), metabolomics, redox regulator expression profiling, mosquito infection assays","journal":"International journal for parasitology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — clean knockout with multiple metabolic readouts (metabolomics + gene expression) and mosquito stage phenotype, single lab","pmids":["33713652"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":"3D7"},{"species":"Plasmodium falciparum","strain":"NF54"}]}],"current_model":"LipB (PF3D7_0823600) is an apicoplast-localized octanoyl-ACP:protein N-octanoyltransferase that catalyzes de novo lipoic acid attachment to the apicoplast pyruvate dehydrogenase complex; it is dispensable for intraerythrocytic blood-stage growth (due to functional redundancy with the dual-targeted LplA2) but is required for normal liver-stage maturation in rodent malaria and for completion of sporogony in P. falciparum, and its loss alters apicoplast and cytosolic redox regulation as well as central carbon metabolism."},"narrative":{"mechanistic_narrative":"LipB (PF3D7_0823600) is an apicoplast-localized octanoyl-ACP:protein N-octanoyltransferase that catalyzes the first committed step of de novo lipoic acid synthesis, attaching the lipoyl/octanoyl moiety to apicoplast target proteins including the apicoplast pyruvate dehydrogenase complex [PMID:15225307, PMID:18069893]. Its apicoplast targeting was established by GFP-fusion imaging of its N-terminal targeting sequence, and its enzymatic activity was confirmed by complementation of E. coli lipB-deficient mutants, placing it in the apicoplast de novo lipoic acid synthesis pathway distinct from the mitochondrial salvage route [PMID:15225307]. In P. falciparum intraerythrocytic stages LipB is dispensable: its disruption abolishes >90% of apicoplast lipoic acid without impairing asexual growth, with residual lipoylation attributed to the dual-targeted ligase LplA2, indicating functional redundancy in apicoplast lipoylation [PMID:18069893]. LipB becomes functionally important in other life stages and under metabolic stress: in P. berghei it is required for late liver-stage maturation and sporozoite infectivity, and blood-stage growth of LipB-deficient parasites is reduced under lipid-restricted conditions [PMID:23490300]; in P. falciparum, LipB deletion alters apicoplast and cytosolic redox regulator expression and reshapes central carbon metabolism (glycolysis and TCA cycle), and prevents completion of sporogony in Anopheles, abolishing infectious sporozoite production [PMID:33713652].","teleology":[{"year":2004,"claim":"Establishing where LipB acts and whether it is a functional lipoic acid synthesis enzyme was the first step in defining a distinct apicoplast lipoylation pathway in Plasmodium.","evidence":"GFP-fusion live imaging of the N-terminal targeting sequence plus bacterial complementation of lipB-deficient E. coli in P. falciparum","pmids":["15225307"],"confidence":"High","gaps":["Enzymatic mechanism and endogenous substrate spectrum not directly resolved in the parasite","Overexpressed targeting-sequence fusion rather than endogenous protein localization"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2007,"claim":"Whether LipB is essential for blood-stage parasites was resolved, revealing that de novo apicoplast lipoylation is buffered by redundancy despite LipB supplying most apicoplast lipoic acid.","evidence":"Gene disruption in P. falciparum with lipoic acid quantification and lipoylation-status assays","pmids":["18069893"],"confidence":"High","gaps":["Molecular basis and regulation of LplA2 compensation not defined","Does not address other life stages"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2013,"claim":"The stage-specific requirement for LipB was defined, showing it is dispensable in blood stages but essential for liver-stage maturation and sporozoite infectivity, and conditionally important under lipid restriction.","evidence":"P. berghei knockout with mouse infection assays, in vitro liver-stage development, and growth under lipid-restricted conditions (8-bromo-octanoate, clofibrate)","pmids":["23490300"],"confidence":"High","gaps":["Which liver-stage substrates depend on LipB not identified","Mechanistic link between lipoylation loss and late liver-stage arrest not established"],"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2021,"claim":"The downstream metabolic and transmission consequences of losing LipB were mapped, connecting its loss to altered redox regulation, central carbon metabolism, and a block in sporogony.","evidence":"P. falciparum 3D7/NF54 knockout with metabolomics, redox regulator expression profiling, and mosquito infection assays","pmids":["33713652"],"confidence":"Medium","gaps":["Causal chain from lipoylation loss to redox and carbon-metabolism changes not resolved","Single lab; mechanism of sporogony arrest not defined"],"attribution":[{"species":"Plasmodium falciparum","strain":"3D7"},{"species":"Plasmodium falciparum","strain":"NF54"}]},{"year":null,"claim":"How LipB and the redundant ligase LplA2 partition apicoplast lipoylation, and the direct enzyme-substrate mechanism by which LipB modifies its targets in the parasite, remain unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No structural model of LipB in Plasmodium","Direct in-parasite substrate profiling absent","Mechanism of LplA2 functional overlap unknown"],"attribution":[]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":[],"partners":[],"other_free_text":["Supplies >90% of apicoplast lipoic acid; loss compensated at blood stage by dual-targeted ligase LplA2 [#1]","Lipoylates the apicoplast pyruvate dehydrogenase complex [#1]","Dispensable for P. falciparum asexual blood-stage growth [#1]","Required for P. berghei liver-stage maturation and sporozoite infectivity; conditionally important under lipid restriction [#2]","Deletion alters apicoplast and cytosolic redox regulator expression and central carbon metabolism (glycolysis, TCA cycle) in P. falciparum [#3]","Required for completion of sporogony in Anopheles (P. falciparum NF54); loss abolishes infectious sporozoites [#3]"]}},"prefetch_data":{},"corpus_meta":[{"pmid":"15225307","id":"PMC_15225307","title":"The human malaria parasite Plasmodium falciparum has distinct organelle-specific lipoylation pathways.","date":"2004","source":"Molecular microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/15225307","citation_count":64,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["LipB"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"18069893","id":"PMC_18069893","title":"Apicoplast lipoic acid protein ligase B is not essential for Plasmodium falciparum.","date":"2007","source":"PLoS pathogens","url":"https://pubmed.ncbi.nlm.nih.gov/18069893","citation_count":42,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["LipB"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"22128915","id":"PMC_22128915","title":"Mitochondrial lipoic acid scavenging is essential for Plasmodium berghei liver stage development.","date":"2012","source":"Cellular microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/22128915","citation_count":38,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"23490300","id":"PMC_23490300","title":"A key role for lipoic acid synthesis during Plasmodium liver stage development.","date":"2013","source":"Cellular microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/23490300","citation_count":32,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["LipB"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"22607141","id":"PMC_22607141","title":"Lipoic acid metabolism of Plasmodium--a suitable drug target.","date":"2012","source":"Current pharmaceutical design","url":"https://pubmed.ncbi.nlm.nih.gov/22607141","citation_count":31,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["LipB"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"19434237","id":"PMC_19434237","title":"Knockout studies reveal an important role of Plasmodium lipoic acid protein ligase A1 for asexual blood stage parasite survival.","date":"2009","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/19434237","citation_count":26,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["LipB"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"33713652","id":"PMC_33713652","title":"Plasmodium falciparum LipB mutants display altered redox and carbon metabolism in asexual stages and cannot complete sporogony in Anopheles mosquitoes.","date":"2021","source":"International journal for parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/33713652","citation_count":10,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["LipB"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"28655332","id":"PMC_28655332","title":"Conditional knock-out of lipoic acid protein ligase 1 reveals redundancy pathway for lipoic acid metabolism in Plasmodium berghei malaria parasite.","date":"2017","source":"Parasites & vectors","url":"https://pubmed.ncbi.nlm.nih.gov/28655332","citation_count":4,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["LipB"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":6978,"output_tokens":1360,"usd":0.020667,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6273,"output_tokens":2310,"usd":0.044557,"stage2_stop_reason":"end_turn"},"total_usd":0.065224,"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\": 2004,\n      \"finding\": \"LipB (lipoyl-ACP:protein N-lipoyl transferase / octanoyl-ACP:protein N-octanoyltransferase) localizes to the apicoplast of P. falciparum intraerythrocytic stages, as demonstrated by GFP-fusion overexpression of its N-terminal targeting sequence. Functional activity was confirmed by complementation of E. coli lipB-deficient mutants. LipB constitutes part of the apicoplast-specific de novo lipoic acid synthesis pathway, distinct from the mitochondrial lipoic acid salvage pathway.\",\n      \"method\": \"GFP-fusion live imaging (N-terminal targeting sequence), bacterial complementation of lipB-deficient E. coli, Northern and Western blot\",\n      \"journal\": \"Molecular microbiology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — direct localization by GFP imaging plus functional complementation assay, two orthogonal methods in a single study\",\n      \"pmids\": [\"15225307\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2007,\n      \"finding\": \"Disruption of the LipB gene in P. falciparum did not negatively affect asexual blood-stage parasite growth despite causing a >90% loss of lipoic acid in the apicoplast, demonstrating that LipB is not essential for intraerythrocytic development. Residual lipoylation of the apicoplast-located pyruvate dehydrogenase was attributed to the dual-targeted lipoate protein ligase LplA2, indicating functional redundancy in the apicoplast lipoylation pathway.\",\n      \"method\": \"Gene disruption (knockout), lipoic acid quantification, immunofluorescence/Western blot for lipoylation status\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — clean gene disruption with defined phenotypic readout (growth and lipoylation status), multiple orthogonal methods, independently consistent with PMID:23490300\",\n      \"pmids\": [\"18069893\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2013,\n      \"finding\": \"LipB-deficient P. berghei sporozoites showed markedly attenuated infectivity in mice and arrested at a very late liver stage shortly before final intra-hepatic maturation, establishing that LipB is essential for liver stage development. LipB-deficient asexual blood-stage parasites grew normally under standard conditions but showed reduced growth under lipid-restricted conditions (treatment with 8-bromo-octanoate or clofibrate).\",\n      \"method\": \"Gene knockout in P. berghei, mouse infection assays, in vitro liver-stage development assay, growth assays under lipid-restricted conditions\",\n      \"journal\": \"Cellular microbiology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — clean knockout with in vivo and in vitro phenotypic readouts across multiple life stages, replicated across conditions\",\n      \"pmids\": [\"23490300\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium berghei\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"Deletion of LipB in P. falciparum 3D7 altered expression of redox regulators in both the apicoplast and cytosol, and changed central carbon metabolism including glycolysis and TCA cycle activity. In the NF54 strain, LipB deletion prevented completion of sporogony in Anopheles mosquitoes, with no infectious sporozoites detectable, establishing LipB as essential for transmission.\",\n      \"method\": \"Gene knockout (lipB deletion), metabolomics, redox regulator expression profiling, mosquito infection assays\",\n      \"journal\": \"International journal for parasitology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — clean knockout with multiple metabolic readouts (metabolomics + gene expression) and mosquito stage phenotype, single lab\",\n      \"pmids\": [\"33713652\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"3D7\"},\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"NF54\"}\n      ]\n    }\n  ],\n  \"current_model\": \"LipB (PF3D7_0823600) is an apicoplast-localized octanoyl-ACP:protein N-octanoyltransferase that catalyzes de novo lipoic acid attachment to the apicoplast pyruvate dehydrogenase complex; it is dispensable for intraerythrocytic blood-stage growth (due to functional redundancy with the dual-targeted LplA2) but is required for normal liver-stage maturation in rodent malaria and for completion of sporogony in P. falciparum, and its loss alters apicoplast and cytosolic redox regulation as well as central carbon metabolism.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"LipB (PF3D7_0823600) is an apicoplast-localized octanoyl-ACP:protein N-octanoyltransferase that catalyzes the first committed step of de novo lipoic acid synthesis, attaching the lipoyl/octanoyl moiety to apicoplast target proteins including the apicoplast pyruvate dehydrogenase complex [#0, #1]. Its apicoplast targeting was established by GFP-fusion imaging of its N-terminal targeting sequence, and its enzymatic activity was confirmed by complementation of E. coli lipB-deficient mutants, placing it in the apicoplast de novo lipoic acid synthesis pathway distinct from the mitochondrial salvage route [#0]. In P. falciparum intraerythrocytic stages LipB is dispensable: its disruption abolishes >90% of apicoplast lipoic acid without impairing asexual growth, with residual lipoylation attributed to the dual-targeted ligase LplA2, indicating functional redundancy in apicoplast lipoylation [#1]. LipB becomes functionally important in other life stages and under metabolic stress: in P. berghei it is required for late liver-stage maturation and sporozoite infectivity, and blood-stage growth of LipB-deficient parasites is reduced under lipid-restricted conditions [#2]; in P. falciparum, LipB deletion alters apicoplast and cytosolic redox regulator expression and reshapes central carbon metabolism (glycolysis and TCA cycle), and prevents completion of sporogony in Anopheles, abolishing infectious sporozoite production [#3].\",\n  \"teleology\": [\n    {\n      \"year\": 2004,\n      \"claim\": \"Establishing where LipB acts and whether it is a functional lipoic acid synthesis enzyme was the first step in defining a distinct apicoplast lipoylation pathway in Plasmodium.\",\n      \"evidence\": \"GFP-fusion live imaging of the N-terminal targeting sequence plus bacterial complementation of lipB-deficient E. coli in P. falciparum\",\n      \"pmids\": [\"15225307\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Enzymatic mechanism and endogenous substrate spectrum not directly resolved in the parasite\", \"Overexpressed targeting-sequence fusion rather than endogenous protein localization\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2007,\n      \"claim\": \"Whether LipB is essential for blood-stage parasites was resolved, revealing that de novo apicoplast lipoylation is buffered by redundancy despite LipB supplying most apicoplast lipoic acid.\",\n      \"evidence\": \"Gene disruption in P. falciparum with lipoic acid quantification and lipoylation-status assays\",\n      \"pmids\": [\"18069893\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Molecular basis and regulation of LplA2 compensation not defined\", \"Does not address other life stages\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2013,\n      \"claim\": \"The stage-specific requirement for LipB was defined, showing it is dispensable in blood stages but essential for liver-stage maturation and sporozoite infectivity, and conditionally important under lipid restriction.\",\n      \"evidence\": \"P. berghei knockout with mouse infection assays, in vitro liver-stage development, and growth under lipid-restricted conditions (8-bromo-octanoate, clofibrate)\",\n      \"pmids\": [\"23490300\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Which liver-stage substrates depend on LipB not identified\", \"Mechanistic link between lipoylation loss and late liver-stage arrest not established\"],\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"The downstream metabolic and transmission consequences of losing LipB were mapped, connecting its loss to altered redox regulation, central carbon metabolism, and a block in sporogony.\",\n      \"evidence\": \"P. falciparum 3D7/NF54 knockout with metabolomics, redox regulator expression profiling, and mosquito infection assays\",\n      \"pmids\": [\"33713652\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Causal chain from lipoylation loss to redox and carbon-metabolism changes not resolved\", \"Single lab; mechanism of sporogony arrest not defined\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"3D7\"}, {\"species\": \"Plasmodium falciparum\", \"strain\": \"NF54\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How LipB and the redundant ligase LplA2 partition apicoplast lipoylation, and the direct enzyme-substrate mechanism by which LipB modifies its targets in the parasite, remain unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No structural model of LipB in Plasmodium\", \"Direct in-parasite substrate profiling absent\", \"Mechanism of LplA2 functional overlap unknown\"],\n      \"attribution\": []\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0033819\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0020011\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0009107\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"complexes\": [],\n    \"partners\": [],\n    \"other_free_text\": [\n      \"Supplies >90% of apicoplast lipoic acid; loss compensated at blood stage by dual-targeted ligase LplA2 [#1]\",\n      \"Lipoylates the apicoplast pyruvate dehydrogenase complex [#1]\",\n      \"Dispensable for P. falciparum asexual blood-stage growth [#1]\",\n      \"Required for P. berghei liver-stage maturation and sporozoite infectivity; conditionally important under lipid restriction [#2]\",\n      \"Deletion alters apicoplast and cytosolic redox regulator expression and central carbon metabolism (glycolysis, TCA cycle) in P. falciparum [#3]\",\n      \"Required for completion of sporogony in Anopheles (P. falciparum NF54); loss abolishes infectious sporozoites [#3]\"\n    ]\n  }\n}\n```","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_0823600","name":null,"product":"lipoate-protein ligase B","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_0707000","name":null,"product":"lipoate-protein ligase B","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_1317600","name":null,"product":"lipoate-protein ligase B, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"LipB","evaluation":null}