{"gene":"PF3D7_0317100","run_date":"2026-09-07T10:55:51","timeline":{"discoveries":[{"year":2014,"finding":"B9 is translationally repressed in sporozoites and is expressed after hepatocyte invasion, where it localizes to the parasite plasma membrane. Loss of B9 in P. berghei, P. yoelii, and P. falciparum causes developmental arrest in hepatocytes associated with a compromised parasitophorous vacuole membrane (PVM), indicating B9 is required for establishment and maintenance of the parasitophorous vacuole during liver-stage development.","method":"RT-PCR, immunofluorescence assay, gene knockout in P. berghei, P. yoelii, and P. falciparum with in vivo (BALB/c, C57BL6 mice) and in vitro (Huh7 hepatoma cells, primary human hepatocytes) phenotypic readout","journal":"FASEB journal : official publication of the Federation of American Societies for Experimental Biology","confidence":"High","confidence_rationale":"Tier 2 / Strong — clean KO with defined cellular phenotype across three Plasmodium species and multiple host systems, replicated in vivo and in vitro with direct localization data","pmids":["24509910"],"is_preprint":false,"attribution":[{"species":"Plasmodium berghei","strain":""},{"species":"Plasmodium yoelii","strain":""},{"species":"Plasmodium falciparum","strain":""}]},{"year":2014,"finding":"Deletion of b9 (together with slarp) in P. falciparum produces sporozoites that are infective to human hepatocytes in vitro and in humanized mice but completely abort liver-stage development after infection, confirming B9 governs an independent and critical process for successful liver-stage development.","method":"Gene knockout (double deletion of b9 and slarp) in P. falciparum; infectivity tested in vitro in human hepatocytes and in vivo in humanized mice engrafted with human hepatocytes","journal":"eLife","confidence":"High","confidence_rationale":"Tier 2 / Strong — clean KO with defined developmental-arrest phenotype confirmed in both in vitro and in vivo human hepatocyte systems","pmids":["25407681"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""},{"species":"Plasmodium berghei","strain":""}]},{"year":2023,"finding":"B9 is secreted from sporozoite micronemes and is required for productive invasion of hepatocytes. The N-terminus of B9 forms a beta-propeller domain structurally related to CyRPA. This beta-propeller domain is essential for sporozoite infectivity and interacts with the 6-cysteine proteins P36 and P52 in a heterologous expression system.","method":"Structural determination of B9 N-terminal domain (beta-propeller), heterologous expression system interaction assays (B9 with P36 and P52), genetic loss-of-function, localization to micronemes","journal":"iScience","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — structural domain identification plus interaction assay in heterologous system plus genetic KO phenotype, but interaction shown only in heterologous system (not native parasite co-IP)","pmids":["36761022"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2022,"finding":"B9 (in combination with other sporozoite-expressed 6-cysteine proteins) is responsible for the ability of sporozoites to commit to hepatocyte infection. Double knockouts of B9 and SPECT2 (essential for sporozoite migration through hepatocytes) showed parasites lacked the capacity to stop migration, suggesting B9 mediates recognition of hepatocyte-specific cell surface ligands that trigger the transition from migration to infection mode.","method":"Double gene knockout of B9 and SPECT2 in Plasmodium; behavioral assay measuring sporozoite migration vs. infection commitment","journal":"Parasitology international","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — genetic epistasis via double KO with defined behavioral phenotype, single lab, single method","pmids":["36403748"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"B9 (PF3D7_0317100) is a 6-cysteine family protein that is translationally repressed in sporozoites, secreted from micronemes upon hepatocyte contact, and localizes to the parasite plasma membrane during liver-stage development; its N-terminal beta-propeller domain interacts with 6-cysteine proteins P36 and P52, and B9 is essential for productive hepatocyte invasion and for the establishment and maintenance of the parasitophorous vacuole membrane, with loss of B9 causing complete developmental arrest at the liver stage across multiple Plasmodium species."},"narrative":{"mechanistic_narrative":"B9 (PF3D7_0317100) is a 6-cysteine family protein that governs the transition of Plasmodium sporozoites from migratory behavior to productive hepatocyte infection and the subsequent establishment of the intracellular liver stage [PMID:24509910, PMID:36403748]. B9 transcript is translationally repressed in sporozoites and the protein is expressed after hepatocyte invasion, localizing to the parasite plasma membrane, where loss of B9 in P. berghei, P. yoelii, and P. falciparum causes developmental arrest associated with a compromised parasitophorous vacuole membrane, establishing B9 as required for establishment and maintenance of the parasitophorous vacuole [PMID:24509910]. In P. falciparum, B9 is secreted from sporozoite micronemes and is required for productive invasion; its N-terminal beta-propeller domain is essential for infectivity and mediates interaction with the 6-cysteine proteins P36 and P52 in a heterologous system [PMID:36761022]. Consistent with a role in triggering infection commitment, B9 contributes to the sporozoite's ability to stop migrating and commit to invasion, implicating it in recognition of hepatocyte surface ligands [PMID:36403748]. Deletion of b9 yields sporozoites that invade but completely abort liver-stage development in human hepatocytes in vitro and in humanized mice, confirming an independent and critical function in liver-stage progression [PMID:25407681].","teleology":[{"year":2014,"claim":"Established that B9 is a stage-specific liver-stage effector rather than a constitutive sporozoite protein, and that it is essential for building the parasitophorous vacuole that shelters the developing parasite.","evidence":"RT-PCR and immunofluorescence for expression/localization plus gene knockout across three Plasmodium species with in vivo and in vitro hepatocyte readouts","pmids":["24509910"],"confidence":"High","gaps":["Molecular mechanism by which B9 stabilizes the PVM is undefined","No binding partners identified in this study","How translational repression is imposed and released is not addressed"],"attribution":[{"species":"Plasmodium berghei","strain":""},{"species":"Plasmodium yoelii","strain":""},{"species":"Plasmodium falciparum","strain":""}]},{"year":2014,"claim":"Showed B9's function is post-invasion and independent, since b9-deleted sporozoites retain hepatocyte infectivity but abort development, distinguishing invasion competence from liver-stage progression.","evidence":"Double knockout of b9 and slarp in P. falciparum with infectivity tested in human hepatocytes in vitro and in humanized mice","pmids":["25407681"],"confidence":"High","gaps":["Individual contribution of b9 versus slarp to arrest not fully resolved","Precise developmental stage of arrest not mechanistically dissected","No molecular effectors of the arrested phenotype identified"],"attribution":[{"species":"Plasmodium falciparum","strain":""},{"species":"Plasmodium berghei","strain":""}]},{"year":2022,"claim":"Placed B9 in the decision to convert from cell-traversal to infection mode, addressing how sporozoites sense that they have reached a suitable hepatocyte.","evidence":"Double knockout of B9 and SPECT2 in Plasmodium with a behavioral assay of migration versus infection commitment","pmids":["36403748"],"confidence":"Medium","gaps":["Hepatocyte-specific ligand recognized by B9 not identified","Single lab, single behavioral method","Direct receptor-binding evidence lacking"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2023,"claim":"Defined the structural basis and binding partners of B9, revealing an N-terminal beta-propeller domain structurally related to CyRPA that engages the 6-cysteine proteins P36 and P52 and is required for infectivity.","evidence":"Structural determination of the B9 N-terminal domain, heterologous-expression interaction assays with P36 and P52, microneme localization, and genetic loss-of-function in P. falciparum","pmids":["36761022"],"confidence":"Medium","gaps":["Interactions shown only in heterologous system, not by native parasite co-IP","Stoichiometry and architecture of any B9-P36-P52 complex unresolved","Host receptor engaged by the beta-propeller not identified"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"The molecular mechanism linking B9's beta-propeller/P36-P52 interactions to PVM establishment and the identity of the hepatocyte surface ligand triggering infection commitment remain unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No native-parasite validation of the B9-P36-P52 complex","Host receptor for B9 unidentified","Mechanistic link between invasion-triggering and PVM biogenesis not established"],"attribution":[]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["B9 N-terminal beta-propeller interacts with 6-cysteine proteins P36 and P52 (heterologous expression system) [#2]"],"partners":["P36","P52"],"other_free_text":["Translationally repressed in sporozoites; expressed after hepatocyte invasion [#0]","Secreted from sporozoite micronemes [#2]","Loss of B9 compromises the parasitophorous vacuole membrane and causes liver-stage developmental arrest in P. berghei, P. yoelii, and P. falciparum [#0]","N-terminal beta-propeller domain structurally related to CyRPA and essential for sporozoite infectivity [#2]","Contributes to the migration-to-infection commitment of sporozoites, implicated in recognition of hepatocyte surface ligands [#3]"]}},"prefetch_data":{},"corpus_meta":[{"pmid":"24509910","id":"PMC_24509910","title":"Two Plasmodium 6-Cys family-related proteins have distinct and critical roles in liver-stage development.","date":"2014","source":"FASEB journal : official publication of the Federation of American Societies for Experimental Biology","url":"https://pubmed.ncbi.nlm.nih.gov/24509910","citation_count":74,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"25407681","id":"PMC_25407681","title":"A genetically attenuated malaria vaccine candidate based on P. falciparum b9/slarp gene-deficient sporozoites.","date":"2014","source":"eLife","url":"https://pubmed.ncbi.nlm.nih.gov/25407681","citation_count":74,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"27899328","id":"PMC_27899328","title":"The s48/45 six-cysteine proteins: mediators of interaction throughout the Plasmodium life cycle.","date":"2016","source":"International journal for parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/27899328","citation_count":51,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"35899047","id":"PMC_35899047","title":"Plasmodium 6-Cysteine Proteins: Functional Diversity, Transmission-Blocking Antibodies and Structural Scaffolds.","date":"2022","source":"Frontiers in cellular and infection microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/35899047","citation_count":20,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["6-cysteine protein"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"36761022","id":"PMC_36761022","title":"Plasmodium sporozoites require the protein B9 to invade hepatocytes.","date":"2023","source":"iScience","url":"https://pubmed.ncbi.nlm.nih.gov/36761022","citation_count":5,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"36403748","id":"PMC_36403748","title":"Plasmodium 6-cysteine proteins determine the commitment of sporozoites to liver-infection.","date":"2022","source":"Parasitology international","url":"https://pubmed.ncbi.nlm.nih.gov/36403748","citation_count":1,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["6-cysteine protein"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"26469720","id":"PMC_26469720","title":"Progress with Plasmodium falciparum sporozoite (PfSPZ)-based malaria vaccines.","date":"2015","source":"Vaccine","url":"https://pubmed.ncbi.nlm.nih.gov/26469720","citation_count":136,"is_preprint":false,"source_species":["Pf"],"role":"citation_expansion","match_terms":["fwd_cite"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"37571809","id":"PMC_37571809","title":"Sporozoite immunization: innovative translational science to support the fight against malaria.","date":"2023","source":"Expert review of vaccines","url":"https://pubmed.ncbi.nlm.nih.gov/37571809","citation_count":45,"is_preprint":false,"source_species":["Pf"],"role":"citation_expansion","match_terms":["fwd_cite"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"35308105","id":"PMC_35308105","title":"Structure of the Pf12 and Pf41 heterodimeric complex of Plasmodium falciparum 6-cysteine proteins.","date":"2022","source":"FEMS microbes","url":"https://pubmed.ncbi.nlm.nih.gov/35308105","citation_count":14,"is_preprint":false,"source_species":["Pf"],"role":"citation_expansion","match_terms":["fwd_cite"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":7166,"output_tokens":1390,"usd":0.021174,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6319,"output_tokens":2420,"usd":0.046047,"stage2_stop_reason":"end_turn"},"total_usd":0.067221,"stage1_batch_id":"msgbatch_01DbiymDmubkPpYvdbAu5a7V","stage2_batch_id":"msgbatch_012TbrWvMRH129T7PQ4SmvrJ","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2014,\n      \"finding\": \"B9 is translationally repressed in sporozoites and is expressed after hepatocyte invasion, where it localizes to the parasite plasma membrane. Loss of B9 in P. berghei, P. yoelii, and P. falciparum causes developmental arrest in hepatocytes associated with a compromised parasitophorous vacuole membrane (PVM), indicating B9 is required for establishment and maintenance of the parasitophorous vacuole during liver-stage development.\",\n      \"method\": \"RT-PCR, immunofluorescence assay, gene knockout in P. berghei, P. yoelii, and P. falciparum with in vivo (BALB/c, C57BL6 mice) and in vitro (Huh7 hepatoma cells, primary human hepatocytes) phenotypic readout\",\n      \"journal\": \"FASEB journal : official publication of the Federation of American Societies for Experimental Biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — clean KO with defined cellular phenotype across three Plasmodium species and multiple host systems, replicated in vivo and in vitro with direct localization data\",\n      \"pmids\": [\"24509910\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium berghei\", \"strain\": \"\"},\n        {\"species\": \"Plasmodium yoelii\", \"strain\": \"\"},\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"Deletion of b9 (together with slarp) in P. falciparum produces sporozoites that are infective to human hepatocytes in vitro and in humanized mice but completely abort liver-stage development after infection, confirming B9 governs an independent and critical process for successful liver-stage development.\",\n      \"method\": \"Gene knockout (double deletion of b9 and slarp) in P. falciparum; infectivity tested in vitro in human hepatocytes and in vivo in humanized mice engrafted with human hepatocytes\",\n      \"journal\": \"eLife\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — clean KO with defined developmental-arrest phenotype confirmed in both in vitro and in vivo human hepatocyte systems\",\n      \"pmids\": [\"25407681\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"},\n        {\"species\": \"Plasmodium berghei\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"B9 is secreted from sporozoite micronemes and is required for productive invasion of hepatocytes. The N-terminus of B9 forms a beta-propeller domain structurally related to CyRPA. This beta-propeller domain is essential for sporozoite infectivity and interacts with the 6-cysteine proteins P36 and P52 in a heterologous expression system.\",\n      \"method\": \"Structural determination of B9 N-terminal domain (beta-propeller), heterologous expression system interaction assays (B9 with P36 and P52), genetic loss-of-function, localization to micronemes\",\n      \"journal\": \"iScience\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — structural domain identification plus interaction assay in heterologous system plus genetic KO phenotype, but interaction shown only in heterologous system (not native parasite co-IP)\",\n      \"pmids\": [\"36761022\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"B9 (in combination with other sporozoite-expressed 6-cysteine proteins) is responsible for the ability of sporozoites to commit to hepatocyte infection. Double knockouts of B9 and SPECT2 (essential for sporozoite migration through hepatocytes) showed parasites lacked the capacity to stop migration, suggesting B9 mediates recognition of hepatocyte-specific cell surface ligands that trigger the transition from migration to infection mode.\",\n      \"method\": \"Double gene knockout of B9 and SPECT2 in Plasmodium; behavioral assay measuring sporozoite migration vs. infection commitment\",\n      \"journal\": \"Parasitology international\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — genetic epistasis via double KO with defined behavioral phenotype, single lab, single method\",\n      \"pmids\": [\"36403748\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    }\n  ],\n  \"current_model\": \"B9 (PF3D7_0317100) is a 6-cysteine family protein that is translationally repressed in sporozoites, secreted from micronemes upon hepatocyte contact, and localizes to the parasite plasma membrane during liver-stage development; its N-terminal beta-propeller domain interacts with 6-cysteine proteins P36 and P52, and B9 is essential for productive hepatocyte invasion and for the establishment and maintenance of the parasitophorous vacuole membrane, with loss of B9 causing complete developmental arrest at the liver stage across multiple Plasmodium species.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"B9 (PF3D7_0317100) is a 6-cysteine family protein that governs the transition of Plasmodium sporozoites from migratory behavior to productive hepatocyte infection and the subsequent establishment of the intracellular liver stage [#0, #3]. B9 transcript is translationally repressed in sporozoites and the protein is expressed after hepatocyte invasion, localizing to the parasite plasma membrane, where loss of B9 in P. berghei, P. yoelii, and P. falciparum causes developmental arrest associated with a compromised parasitophorous vacuole membrane, establishing B9 as required for establishment and maintenance of the parasitophorous vacuole [#0]. In P. falciparum, B9 is secreted from sporozoite micronemes and is required for productive invasion; its N-terminal beta-propeller domain is essential for infectivity and mediates interaction with the 6-cysteine proteins P36 and P52 in a heterologous system [#2]. Consistent with a role in triggering infection commitment, B9 contributes to the sporozoite's ability to stop migrating and commit to invasion, implicating it in recognition of hepatocyte surface ligands [#3]. Deletion of b9 yields sporozoites that invade but completely abort liver-stage development in human hepatocytes in vitro and in humanized mice, confirming an independent and critical function in liver-stage progression [#1].\",\n  \"teleology\": [\n    {\n      \"year\": 2014,\n      \"claim\": \"Established that B9 is a stage-specific liver-stage effector rather than a constitutive sporozoite protein, and that it is essential for building the parasitophorous vacuole that shelters the developing parasite.\",\n      \"evidence\": \"RT-PCR and immunofluorescence for expression/localization plus gene knockout across three Plasmodium species with in vivo and in vitro hepatocyte readouts\",\n      \"pmids\": [\"24509910\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Molecular mechanism by which B9 stabilizes the PVM is undefined\", \"No binding partners identified in this study\", \"How translational repression is imposed and released is not addressed\"],\n      \"attribution\": [\n        {\"species\": \"Plasmodium berghei\", \"strain\": \"\"},\n        {\"species\": \"Plasmodium yoelii\", \"strain\": \"\"},\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2014,\n      \"claim\": \"Showed B9's function is post-invasion and independent, since b9-deleted sporozoites retain hepatocyte infectivity but abort development, distinguishing invasion competence from liver-stage progression.\",\n      \"evidence\": \"Double knockout of b9 and slarp in P. falciparum with infectivity tested in human hepatocytes in vitro and in humanized mice\",\n      \"pmids\": [\"25407681\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Individual contribution of b9 versus slarp to arrest not fully resolved\", \"Precise developmental stage of arrest not mechanistically dissected\", \"No molecular effectors of the arrested phenotype identified\"],\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"},\n        {\"species\": \"Plasmodium berghei\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Placed B9 in the decision to convert from cell-traversal to infection mode, addressing how sporozoites sense that they have reached a suitable hepatocyte.\",\n      \"evidence\": \"Double knockout of B9 and SPECT2 in Plasmodium with a behavioral assay of migration versus infection commitment\",\n      \"pmids\": [\"36403748\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Hepatocyte-specific ligand recognized by B9 not identified\", \"Single lab, single behavioral method\", \"Direct receptor-binding evidence lacking\"],\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Defined the structural basis and binding partners of B9, revealing an N-terminal beta-propeller domain structurally related to CyRPA that engages the 6-cysteine proteins P36 and P52 and is required for infectivity.\",\n      \"evidence\": \"Structural determination of the B9 N-terminal domain, heterologous-expression interaction assays with P36 and P52, microneme localization, and genetic loss-of-function in P. falciparum\",\n      \"pmids\": [\"36761022\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Interactions shown only in heterologous system, not by native parasite co-IP\", \"Stoichiometry and architecture of any B9-P36-P52 complex unresolved\", \"Host receptor engaged by the beta-propeller not identified\"],\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The molecular mechanism linking B9's beta-propeller/P36-P52 interactions to PVM establishment and the identity of the hepatocyte surface ligand triggering infection commitment remain unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No native-parasite validation of the B9-P36-P52 complex\", \"Host receptor for B9 unidentified\", \"Mechanistic link between invasion-triggering and PVM biogenesis not established\"],\n      \"attribution\": []\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0005515\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005886\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0020009\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0044409\", \"supporting_discovery_ids\": [0, 1, 2, 3]}\n    ],\n    \"complexes\": [\n      \"B9 N-terminal beta-propeller interacts with 6-cysteine proteins P36 and P52 (heterologous expression system) [#2]\"\n    ],\n    \"partners\": [\n      \"P36\",\n      \"P52\"\n    ],\n    \"other_free_text\": [\n      \"Translationally repressed in sporozoites; expressed after hepatocyte invasion [#0]\",\n      \"Secreted from sporozoite micronemes [#2]\",\n      \"Loss of B9 compromises the parasitophorous vacuole membrane and causes liver-stage developmental arrest in P. berghei, P. yoelii, and P. falciparum [#0]\",\n      \"N-terminal beta-propeller domain structurally related to CyRPA and essential for sporozoite infectivity [#2]\",\n      \"Contributes to the migration-to-infection commitment of sporozoites, implicated in recognition of hepatocyte surface ligands [#3]\"\n    ]\n  }\n}","audit_flag":{"gene":"PF3D7_0317100","tier":"IDENTITY_CHECK","verdict":"identity unverified","subtype":"names_other_cards","uniprot_band":"","rules_fired":"R12","issue":"No cited paper names this card; 3 of 4 cited papers name other catalogue genes (PF3D7_0404400, PF3D7_0404500, PF3D7_0408700). The summary may describe one of those genes."},"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_0317100","name":null,"product":"6-cysteine protein B9","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_0808100","name":null,"product":"6-cysteine protein","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_0824700","name":null,"product":"6-cysteine protein","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"B9","evaluation":null}