{"gene":"PF3D7_1006800","run_date":"2026-09-08T12:51:27","timeline":{"discoveries":[{"year":2022,"finding":"PfGBP2 (PF3D7_1006800) binds specifically to G-rich telomere repeats in G-quadruplex (G4) form in vitro, and can also bind to G-rich RNA in vitro. In vivo, PfGBP2 partially co-localises with the known telomeric protein HP1 but is also found in the cytoplasm, consistent with RNA binding. Its interactome includes numerous RNA-associated proteins.","method":"Proteomics of Isolated Chromatin fragments (PICh), in vitro binding assays, immunofluorescence co-localisation with HP1, mass spectrometry interactome","journal":"Frontiers in cellular and infection microbiology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — in vitro binding assays, in vivo localisation with co-localisation controls, and interactome MS from a single lab with multiple orthogonal methods","pmids":["35273922"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2021,"finding":"PfGBP2 (PF3D7_1006800) binds to a stable G-quadruplex-forming sequence (AP2_G4) as identified by DNA pull-down assay followed by LC-MS/MS, and this interaction was validated in vitro and in vivo. Gene knockout of PfGBP2 affects the expression of var genes, implicating PfGBP2 in regulation of G4-related functions including virulence gene regulation. PfGBP2 is essential for parasite survival in the presence of the G4-stabilising ligand pyridostatin.","method":"DNA pull-down assay with LC-MS/MS, in vitro and in vivo G4-binding validation, gene knockout with var gene expression analysis, pyridostatin sensitivity assay","journal":"Cellular microbiology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — multiple orthogonal methods (pull-down, MS, KO, drug sensitivity) from a single lab","pmids":["33340385"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2020,"finding":"GBP2 (PF3D7_1006800 ortholog) is required for normal asexual development and gametocyte (sexual) development in P. berghei; deletion of gbp2 delays asexual growth and significantly reduces production of both male and female gametocytes. Comparative proteomics of Δgbp2 parasites revealed elevated levels of adenosine deaminase (ADA), purine nucleoside phosphorylase (PNP), and hypoxanthine-guanine phosphoribosyltransferase (HGPRT), suggesting involvement of purine nucleotide biosynthesis in GBP2 function. GBP2 protein levels are markedly reduced under purine starvation (Δnt1 parasites), placing GBP2 downstream of purine availability.","method":"Gene deletion (Δgbp2), comparative proteomic analysis, genetic epistasis with Δnt1 (purine transporter knockout)","journal":"Parasitology international","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — clean KO with defined phenotypic readouts plus proteomic follow-up and genetic epistasis, single lab","pmids":["31958569"],"is_preprint":false,"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2021,"finding":"In P. berghei, GBP2 (PF3D7_1006800 ortholog) localises to both the nucleus and cytoplasm. Immunoprecipitation coupled to mass spectrometry (IP-MS) identified ALBA4, DOZI, and CITH (translational repression complex components) as GBP2 interactors, and also identified a PHAX domain-containing protein (an exportin-1 adaptor) as a GBP2 interactor, implicating GBP2 in mRNA export via the PHAX domain-containing protein pathway. GBP2 (but not NPL3) is required for male and female gametocyte production in P. berghei asexual development, while NAB2 (not GBP2) is essential for asexual blood-stage growth.","method":"Live-cell fluorescence imaging, immunoprecipitation coupled to mass spectrometry (IP-MS), gene deletion phenotypic analysis","journal":"Frontiers in cellular and infection microbiology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal-style IP-MS with live imaging and KO phenotype, single lab, multiple orthogonal methods","pmids":["34604117"],"is_preprint":false,"attribution":[{"species":"Plasmodium berghei","strain":""}]}],"current_model":"PF3D7_1006800 (GBP2) is a multifunctional G-quadruplex DNA/RNA-binding protein that localises to both the nucleus and cytoplasm of Plasmodium parasites, associates with telomeric chromatin and the known telomere protein HP1, regulates var gene expression, interacts with translational repression complex components (ALBA4, DOZI, CITH) and a PHAX domain-containing mRNA export adaptor, and is required in P. berghei for normal gametocyte development and asexual growth, with its function linked to purine nucleotide availability."},"narrative":{"mechanistic_narrative":"PF3D7_1006800 (GBP2) is a G-quadruplex-binding protein of Plasmodium that couples recognition of G-rich nucleic acid structures to virulence gene regulation and RNA metabolism [PMID:35273922, PMID:33340385]. In vitro it binds specifically to G-rich telomere repeats folded as G-quadruplexes and to a stable G4-forming sequence (AP2_G4), and it also binds G-rich RNA [PMID:35273922, PMID:33340385]. Consistent with this dual DNA/RNA activity, GBP2 partially co-localises with the telomeric protein HP1 while also occupying the cytoplasm, and its interactome is enriched for RNA-associated proteins [PMID:35273922]. Functionally, knockout of GBP2 alters var gene expression and renders parasites unable to survive exposure to the G4-stabilising ligand pyridostatin, linking its G4-binding activity to regulation of variant surface antigen genes [PMID:33340385]. In P. berghei, GBP2 localises to both nucleus and cytoplasm and interacts with translational repression complex components ALBA4, DOZI, and CITH and with a PHAX-domain exportin-1 adaptor, implicating it in mRNA export and translational control [PMID:34604117]. Deletion of gbp2 in P. berghei delays asexual growth and sharply reduces male and female gametocyte production, and GBP2 abundance is governed by purine availability, being reduced under purine starvation and associated with altered levels of purine-salvage enzymes [PMID:31958569, PMID:34604117]. Beyond these findings, the structural basis of G4 recognition and the direct mRNA targets of GBP2 have not been characterized in the available corpus.","teleology":[{"year":2020,"claim":"Establishing whether GBP2 has a biological role required a loss-of-function test; deletion showed it is needed for both asexual and sexual development and tied its abundance to purine metabolism.","evidence":"gbp2 gene deletion with phenotypic scoring, comparative proteomics, and genetic epistasis with a purine transporter knockout in P. berghei","pmids":["31958569"],"confidence":"Medium","gaps":["How purine availability mechanistically controls GBP2 levels is unresolved","Whether the purine-enzyme changes are direct GBP2 targets or downstream effects is not established","Molecular activity underlying the developmental phenotype not defined in this study"],"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2021,"claim":"To connect GBP2 to a molecular substrate, DNA pull-down and knockout linked its G4-binding activity to virulence gene regulation, showing G4 recognition has functional consequences for var expression.","evidence":"AP2_G4 DNA pull-down with LC-MS/MS, in vitro/in vivo G4-binding validation, knockout var-gene analysis, and pyridostatin sensitivity in P. falciparum","pmids":["33340385"],"confidence":"Medium","gaps":["Whether GBP2 directly binds var-locus G4s in vivo versus acting indirectly is unclear","No structural model of the G4-GBP2 interaction","Genome-wide G4 occupancy not mapped"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2021,"claim":"Defining GBP2's protein partners clarified its cytoplasmic role, placing it with translational repression machinery and an mRNA-export adaptor and distinguishing its developmental requirement from related family members.","evidence":"IP-MS, live-cell imaging, and comparative gene-deletion phenotyping in P. berghei","pmids":["34604117"],"confidence":"Medium","gaps":["Direct mRNA cargo of GBP2 not identified","Whether GBP2 acts within a stable complex or transiently with ALBA4/DOZI/CITH is unresolved","Functional contribution of the PHAX-domain adaptor interaction to export not tested directly"],"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2022,"claim":"Resolving the nature of GBP2's nucleic acid targets, chromatin proteomics and binding assays showed it recognises telomeric G-quadruplexes and G-rich RNA and partly co-localises with the telomere protein HP1.","evidence":"PICh, in vitro DNA/RNA G4-binding assays, HP1 co-localisation immunofluorescence, and interactome MS in P. falciparum","pmids":["35273922"],"confidence":"Medium","gaps":["Functional role of GBP2 at telomeres versus var loci not disentangled","Relative in vivo occupancy of DNA versus RNA targets unquantified","Whether HP1 co-localisation reflects direct interaction is not shown"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"The structural basis of G4 discrimination and the direct in vivo DNA and mRNA targets that mediate GBP2's effects on var expression and gametocytogenesis remain unknown.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No structure of GBP2 or its G4-bound complex","Direct mRNA cargo and genome-wide binding sites uncharacterized","Mechanism linking purine availability to GBP2 abundance undefined"],"attribution":[]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["Translational repression complex (ALBA4, DOZI, CITH) — GBP2 interactor in P. berghei [#3]"],"partners":["HP1 (PARTIAL CO-LOCALISATION, P. FALCIPARUM) [#0]","ALBA4 [#3]","DOZI [#3]","CITH [#3]","PHAX-DOMAIN-CONTAINING EXPORTIN-1 ADAPTOR [#3]"],"other_free_text":["GBP2 knockout alters var gene expression and confers sensitivity to the G4 ligand pyridostatin in P. falciparum [#1]","In P. berghei, gbp2 deletion delays asexual growth and reduces male and female gametocyte production [#2, #3]","GBP2 abundance is reduced under purine starvation and correlates with altered purine-salvage enzyme levels (ADA, PNP, HGPRT) in P. berghei [#2]"]}},"prefetch_data":{},"corpus_meta":[{"pmid":"35273922","id":"PMC_35273922","title":"Plasmodium falciparum GBP2 Is a Telomere-Associated Protein That Binds to G-Quadruplex DNA and RNA.","date":"2022","source":"Frontiers in cellular and infection microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/35273922","citation_count":14,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["GBP2","PfGBP2"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"31958569","id":"PMC_31958569","title":"G-strand binding protein 2 is involved in asexual and sexual development of Plasmodium berghei.","date":"2020","source":"Parasitology international","url":"https://pubmed.ncbi.nlm.nih.gov/31958569","citation_count":9,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["G-strand-binding protein 2","GBP2"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"33340385","id":"PMC_33340385","title":"PfGBP2 is a novel G-quadruplex binding protein in Plasmodium falciparum.","date":"2021","source":"Cellular microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/33340385","citation_count":6,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["G-strand-binding protein 2","PfGBP2"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"34604117","id":"PMC_34604117","title":"Roles and Cellular Localization of GBP2 and NAB2 During the Blood Stage of Malaria Parasites.","date":"2021","source":"Frontiers in cellular and infection microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/34604117","citation_count":6,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["G-strand-binding protein 2","GBP2"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":5159,"output_tokens":1521,"usd":0.019146,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6464,"output_tokens":2740,"usd":0.05041,"stage2_stop_reason":"end_turn"},"total_usd":0.069556,"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\": 2022,\n      \"finding\": \"PfGBP2 (PF3D7_1006800) binds specifically to G-rich telomere repeats in G-quadruplex (G4) form in vitro, and can also bind to G-rich RNA in vitro. In vivo, PfGBP2 partially co-localises with the known telomeric protein HP1 but is also found in the cytoplasm, consistent with RNA binding. Its interactome includes numerous RNA-associated proteins.\",\n      \"method\": \"Proteomics of Isolated Chromatin fragments (PICh), in vitro binding assays, immunofluorescence co-localisation with HP1, mass spectrometry interactome\",\n      \"journal\": \"Frontiers in cellular and infection microbiology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — in vitro binding assays, in vivo localisation with co-localisation controls, and interactome MS from a single lab with multiple orthogonal methods\",\n      \"pmids\": [\"35273922\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"PfGBP2 (PF3D7_1006800) binds to a stable G-quadruplex-forming sequence (AP2_G4) as identified by DNA pull-down assay followed by LC-MS/MS, and this interaction was validated in vitro and in vivo. Gene knockout of PfGBP2 affects the expression of var genes, implicating PfGBP2 in regulation of G4-related functions including virulence gene regulation. PfGBP2 is essential for parasite survival in the presence of the G4-stabilising ligand pyridostatin.\",\n      \"method\": \"DNA pull-down assay with LC-MS/MS, in vitro and in vivo G4-binding validation, gene knockout with var gene expression analysis, pyridostatin sensitivity assay\",\n      \"journal\": \"Cellular microbiology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — multiple orthogonal methods (pull-down, MS, KO, drug sensitivity) from a single lab\",\n      \"pmids\": [\"33340385\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"GBP2 (PF3D7_1006800 ortholog) is required for normal asexual development and gametocyte (sexual) development in P. berghei; deletion of gbp2 delays asexual growth and significantly reduces production of both male and female gametocytes. Comparative proteomics of Δgbp2 parasites revealed elevated levels of adenosine deaminase (ADA), purine nucleoside phosphorylase (PNP), and hypoxanthine-guanine phosphoribosyltransferase (HGPRT), suggesting involvement of purine nucleotide biosynthesis in GBP2 function. GBP2 protein levels are markedly reduced under purine starvation (Δnt1 parasites), placing GBP2 downstream of purine availability.\",\n      \"method\": \"Gene deletion (Δgbp2), comparative proteomic analysis, genetic epistasis with Δnt1 (purine transporter knockout)\",\n      \"journal\": \"Parasitology international\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — clean KO with defined phenotypic readouts plus proteomic follow-up and genetic epistasis, single lab\",\n      \"pmids\": [\"31958569\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"In P. berghei, GBP2 (PF3D7_1006800 ortholog) localises to both the nucleus and cytoplasm. Immunoprecipitation coupled to mass spectrometry (IP-MS) identified ALBA4, DOZI, and CITH (translational repression complex components) as GBP2 interactors, and also identified a PHAX domain-containing protein (an exportin-1 adaptor) as a GBP2 interactor, implicating GBP2 in mRNA export via the PHAX domain-containing protein pathway. GBP2 (but not NPL3) is required for male and female gametocyte production in P. berghei asexual development, while NAB2 (not GBP2) is essential for asexual blood-stage growth.\",\n      \"method\": \"Live-cell fluorescence imaging, immunoprecipitation coupled to mass spectrometry (IP-MS), gene deletion phenotypic analysis\",\n      \"journal\": \"Frontiers in cellular and infection microbiology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal-style IP-MS with live imaging and KO phenotype, single lab, multiple orthogonal methods\",\n      \"pmids\": [\"34604117\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"PF3D7_1006800 (GBP2) is a multifunctional G-quadruplex DNA/RNA-binding protein that localises to both the nucleus and cytoplasm of Plasmodium parasites, associates with telomeric chromatin and the known telomere protein HP1, regulates var gene expression, interacts with translational repression complex components (ALBA4, DOZI, CITH) and a PHAX domain-containing mRNA export adaptor, and is required in P. berghei for normal gametocyte development and asexual growth, with its function linked to purine nucleotide availability.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"PF3D7_1006800 (GBP2) is a G-quadruplex-binding protein of Plasmodium that couples recognition of G-rich nucleic acid structures to virulence gene regulation and RNA metabolism [#0, #1]. In vitro it binds specifically to G-rich telomere repeats folded as G-quadruplexes and to a stable G4-forming sequence (AP2_G4), and it also binds G-rich RNA [#0, #1]. Consistent with this dual DNA/RNA activity, GBP2 partially co-localises with the telomeric protein HP1 while also occupying the cytoplasm, and its interactome is enriched for RNA-associated proteins [#0]. Functionally, knockout of GBP2 alters var gene expression and renders parasites unable to survive exposure to the G4-stabilising ligand pyridostatin, linking its G4-binding activity to regulation of variant surface antigen genes [#1]. In P. berghei, GBP2 localises to both nucleus and cytoplasm and interacts with translational repression complex components ALBA4, DOZI, and CITH and with a PHAX-domain exportin-1 adaptor, implicating it in mRNA export and translational control [#3]. Deletion of gbp2 in P. berghei delays asexual growth and sharply reduces male and female gametocyte production, and GBP2 abundance is governed by purine availability, being reduced under purine starvation and associated with altered levels of purine-salvage enzymes [#2, #3]. Beyond these findings, the structural basis of G4 recognition and the direct mRNA targets of GBP2 have not been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2020,\n      \"claim\": \"Establishing whether GBP2 has a biological role required a loss-of-function test; deletion showed it is needed for both asexual and sexual development and tied its abundance to purine metabolism.\",\n      \"evidence\": \"gbp2 gene deletion with phenotypic scoring, comparative proteomics, and genetic epistasis with a purine transporter knockout in P. berghei\",\n      \"pmids\": [\"31958569\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"How purine availability mechanistically controls GBP2 levels is unresolved\",\n        \"Whether the purine-enzyme changes are direct GBP2 targets or downstream effects is not established\",\n        \"Molecular activity underlying the developmental phenotype not defined in this study\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"To connect GBP2 to a molecular substrate, DNA pull-down and knockout linked its G4-binding activity to virulence gene regulation, showing G4 recognition has functional consequences for var expression.\",\n      \"evidence\": \"AP2_G4 DNA pull-down with LC-MS/MS, in vitro/in vivo G4-binding validation, knockout var-gene analysis, and pyridostatin sensitivity in P. falciparum\",\n      \"pmids\": [\"33340385\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Whether GBP2 directly binds var-locus G4s in vivo versus acting indirectly is unclear\",\n        \"No structural model of the G4-GBP2 interaction\",\n        \"Genome-wide G4 occupancy not mapped\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Defining GBP2's protein partners clarified its cytoplasmic role, placing it with translational repression machinery and an mRNA-export adaptor and distinguishing its developmental requirement from related family members.\",\n      \"evidence\": \"IP-MS, live-cell imaging, and comparative gene-deletion phenotyping in P. berghei\",\n      \"pmids\": [\"34604117\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Direct mRNA cargo of GBP2 not identified\",\n        \"Whether GBP2 acts within a stable complex or transiently with ALBA4/DOZI/CITH is unresolved\",\n        \"Functional contribution of the PHAX-domain adaptor interaction to export not tested directly\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Resolving the nature of GBP2's nucleic acid targets, chromatin proteomics and binding assays showed it recognises telomeric G-quadruplexes and G-rich RNA and partly co-localises with the telomere protein HP1.\",\n      \"evidence\": \"PICh, in vitro DNA/RNA G4-binding assays, HP1 co-localisation immunofluorescence, and interactome MS in P. falciparum\",\n      \"pmids\": [\"35273922\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Functional role of GBP2 at telomeres versus var loci not disentangled\",\n        \"Relative in vivo occupancy of DNA versus RNA targets unquantified\",\n        \"Whether HP1 co-localisation reflects direct interaction is not shown\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The structural basis of G4 discrimination and the direct in vivo DNA and mRNA targets that mediate GBP2's effects on var expression and gametocytogenesis remain unknown.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No structure of GBP2 or its G4-bound complex\",\n        \"Direct mRNA cargo and genome-wide binding sites uncharacterized\",\n        \"Mechanism linking purine availability to GBP2 abundance undefined\"\n      ],\n      \"attribution\": []\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0051880\", \"supporting_discovery_ids\": [0, 1]},\n      {\"term_id\": \"GO:0003723\", \"supporting_discovery_ids\": [0, 3]},\n      {\"term_id\": \"GO:0003677\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005634\", \"supporting_discovery_ids\": [0, 3]},\n      {\"term_id\": \"GO:0005737\", \"supporting_discovery_ids\": [0, 3]},\n      {\"term_id\": \"GO:0000781\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0016441\", \"supporting_discovery_ids\": [3]},\n      {\"term_id\": \"GO:0006406\", \"supporting_discovery_ids\": [3]},\n      {\"term_id\": \"GO:0060968\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"complexes\": [\n      \"Translational repression complex (ALBA4, DOZI, CITH) — GBP2 interactor in P. berghei [#3]\"\n    ],\n    \"partners\": [\n      \"HP1 (partial co-localisation, P. falciparum) [#0]\",\n      \"ALBA4 [#3]\",\n      \"DOZI [#3]\",\n      \"CITH [#3]\",\n      \"PHAX-domain-containing exportin-1 adaptor [#3]\"\n    ],\n    \"other_free_text\": [\n      \"GBP2 knockout alters var gene expression and confers sensitivity to the G4 ligand pyridostatin in P. falciparum [#1]\",\n      \"In P. berghei, gbp2 deletion delays asexual growth and reduces male and female gametocyte production [#2, #3]\",\n      \"GBP2 abundance is reduced under purine starvation and correlates with altered purine-salvage enzyme levels (ADA, PNP, HGPRT) in P. berghei [#2]\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_1006800","name":null,"product":"G-strand-binding protein 2","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_1205000","name":null,"product":"G-strand-binding protein 2","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_0805600","name":null,"product":"G-strand-binding protein 2, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"GBP2","evaluation":null}