{"gene":"TG_248880","gene_symbol":"RAB7","run_date":"2026-09-08T12:58:25","timeline":{"discoveries":[{"year":1997,"finding":"Toxoplasma-containing phagosomes (formed by phagocytosis of dead/opsonized parasites) sequentially acquire host Rab7, consistent with normal late-endosomal fusion; in contrast, parasitophorous vacuoles formed by active parasite invasion fail to acquire Rab7 or any other endocytic fusion proteins, indicating that exclusion of Rab7 is a key mechanism by which actively invading Toxoplasma evades lysosomal degradation.","method":"Immunofluorescence localization of endogenous endocytic markers (including Rab7) in pulse-infected bone marrow-derived macrophages; comparison of phagocytosis vs. active invasion modes","journal":"Journal of Immunology","confidence":"High","confidence_rationale":"Tier 2 / Strong — direct comparative localization experiment with multiple endocytic markers and two well-defined entry modes; mechanistic conclusion about Rab7 exclusion replicated across conditions within a rigorous study","pmids":["9379044"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2006,"finding":"CD40 stimulation of macrophages infected with T. gondii triggers autophagy-dependent fusion of parasitophorous vacuoles with late endosomes/lysosomes; pharmacological and genetic impairment of Rab7 (alongside PIK3C3, vacuolar ATPase, and lysosomal enzymes) blocked this vacuole/lysosome fusion and abolished CD40-induced antimicrobial activity, placing Rab7 as a required effector in this pathway.","method":"Genetic (Rab7 dominant-negative/knockdown) and pharmacological approaches combined with immunofluorescence colocalization and antimicrobial activity assays in human and mouse macrophages","journal":"The Journal of Clinical Investigation","confidence":"High","confidence_rationale":"Tier 2 / Strong — multiple orthogonal methods (genetic, pharmacological, colocalization, functional killing assay) in both human and mouse macrophages; Rab7 requirement demonstrated alongside mechanistic autophagy pathway placement","pmids":["16955139"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2010,"finding":"In intracellular T. gondii tachyzoites, a novel plant vacuole-like organelle fragments during intracellular growth, with some of its markers colocalizing with the late-endosomal marker Rab7, suggesting involvement of Rab7-positive compartments in the endocytic-like pathway associated with this organelle.","method":"Immunofluorescence colocalization of organelle markers with Rab7 in intracellular tachyzoites; electron tomography","journal":"Molecular Microbiology","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single colocalization observation, no functional perturbation of Rab7 itself; mechanistic link to Rab7 function is inferential","pmids":["20398214"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2017,"finding":"During Toxoplasma infection, host lipid droplets (LD) internalized within the parasitophorous vacuole remain associated with Rab7 and become wrapped by the intravacuolar network of membranes (IVN); this Rab7-associated LD pool is implicated in parasite lipid scavenging, as mutant parasites lacking IVN formation or an IVN-localized phospholipase A2 show diminished lipid uptake from host LD.","method":"Immunofluorescence and live imaging of Rab7-associated LD in infected cells; genetic loss-of-function (IVN-deficient mutants, phospholipase A2 knockout) with lipid uptake assays","journal":"PLoS Pathogens","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — Rab7 colocalization with internalized LD supported by genetic mutants showing functional consequences; single lab, but two orthogonal approaches (imaging + genetics)","pmids":["28570716"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2013,"finding":"Rab7, a classical marker of late endocytic compartments, decorates endomembranous structures in T. gondii, suggesting operation of an endosomal-like system that has been evolutionarily repurposed for trafficking and sorting proteins to apical secretory organelles (rhoptries and micronemes) via the ER and Golgi.","method":"Review/synthesis of existing localization data on Rab5 and Rab7 in T. gondii; no new primary experiments reported","journal":"International Journal for Parasitology","confidence":"Low","confidence_rationale":"Tier 4 / Weak — review paper synthesizing prior localization observations without new functional experiments on Rab7 itself","pmids":["24211609"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"current_model":"In Toxoplasma gondii, host-cell Rab7 is excluded from the parasitophorous vacuole formed during active invasion (a key evasion mechanism), but is required for CD40-triggered autophagy-dependent rerouting of the vacuole to lysosomes in macrophages; within the parasite, Rab7 marks late-endosomal-like compartments associated with internalized host lipid droplets and a plant vacuole-like organelle, implicating it in an endosomal-like system used for nutrient scavenging and potentially for apical organelle biogenesis."},"narrative":{"mechanistic_narrative":"Rab7 functions in the Toxoplasma gondii host-parasite interface both as a host-cell late-endosomal marker exploited during infection and as a parasite-encoded marker of an endosomal-like membrane system [PMID:9379044, PMID:24211609]. On the host side, actively invading tachyzoites establish a parasitophorous vacuole that fails to acquire Rab7 or other endocytic fusion proteins, whereas phagosomes containing dead or opsonized parasites recruit Rab7 normally — establishing Rab7 exclusion as a mechanism by which invading parasites evade lysosomal fusion [PMID:9379044]. This exclusion can be overridden: CD40 stimulation of infected macrophages triggers autophagy-dependent fusion of the parasitophorous vacuole with late endosomes/lysosomes, and impairing Rab7 blocks this fusion and abolishes CD40-induced antimicrobial killing, placing Rab7 as a required effector of this pathway [PMID:16955139]. Within the parasite, Rab7 decorates late-endosomal-like endomembranes: it associates with host lipid droplets internalized into the vacuole that become wrapped by the intravacuolar network and feed parasite lipid scavenging [PMID:28570716], and marks compartments linked to a fragmenting plant vacuole-like organelle [PMID:20398214]. Beyond these localization and infection-model findings, the biochemical regulation of Rab7 in this system has not been characterized in the available corpus.","teleology":[{"year":1997,"claim":"It was unknown why actively invading Toxoplasma escapes lysosomal degradation; comparing entry modes established that exclusion of host Rab7 (and other endocytic fusion proteins) from the parasitophorous vacuole is a key evasion mechanism.","evidence":"Immunofluorescence of endogenous endocytic markers in pulse-infected bone marrow-derived macrophages, comparing phagocytosis vs. active invasion","pmids":["9379044"],"confidence":"High","gaps":["Does not identify the parasite factor that mediates Rab7 exclusion","Mechanism of selective marker exclusion at the vacuolar membrane not defined"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2006,"claim":"It was unknown how host immune signaling could redirect the evasion-competent vacuole to lysosomes; CD40 stimulation was shown to drive autophagy-dependent vacuole/lysosome fusion requiring Rab7, defining Rab7 as an effector of CD40-induced antimicrobial activity.","evidence":"Genetic (Rab7 dominant-negative/knockdown) and pharmacological perturbation with colocalization and antimicrobial killing assays in human and mouse macrophages","pmids":["16955139"],"confidence":"High","gaps":["Does not resolve how CD40 signaling overcomes the Rab7 exclusion seen during active invasion","Direct Rab7 effector interactions in the fusion step not defined"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2010,"claim":"Whether the parasite's own endomembrane system uses Rab7-positive compartments was unclear; colocalization of markers from a fragmenting plant vacuole-like organelle with Rab7 implicated Rab7 compartments in a parasite endocytic-like pathway.","evidence":"Immunofluorescence colocalization of organelle markers with Rab7 and electron tomography in intracellular tachyzoites","pmids":["20398214"],"confidence":"Low","gaps":["Single colocalization observation without functional perturbation of Rab7","Causal role of Rab7 in organelle dynamics not tested"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2013,"claim":"Synthesis of prior localization data framed parasite Rab7 as part of an evolutionarily repurposed endosomal-like system trafficking proteins to apical secretory organelles.","evidence":"Review synthesizing existing Rab5/Rab7 localization data; no new primary experiments","pmids":["24211609"],"confidence":"Low","gaps":["No new functional data on Rab7","Direct role of Rab7 in rhoptry/microneme biogenesis not experimentally demonstrated"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2017,"claim":"How the parasite scavenges host lipids was addressed by showing host lipid droplets internalized into the vacuole remain Rab7-associated and are wrapped by the intravacuolar network, feeding parasite lipid uptake.","evidence":"Immunofluorescence and live imaging of Rab7-associated lipid droplets plus IVN-deficient and phospholipase A2 knockout mutants with lipid uptake assays","pmids":["28570716"],"confidence":"Medium","gaps":["Whether Rab7 itself is functionally required for lipid droplet internalization vs. being a passive marker not resolved","Single-lab findings"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":null,"claim":"The biochemical regulation of Rab7 in this system — its GEFs, GAPs, effectors, and the parasite factors that mediate its exclusion or recruitment — remains uncharacterized.","evidence":"","pmids":[],"confidence":"Low","gaps":["No Rab7 regulators or effectors identified in the corpus","Direct causal role of parasite Rab7 in apical organelle biogenesis untested"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":[],"partners":[],"other_free_text":["Host Rab7 is excluded from parasitophorous vacuoles formed by active invasion but recruited to phagosomes of dead/opsonized parasites [#0].","Required effector of CD40-induced, autophagy-dependent fusion of the parasitophorous vacuole with late endosomes/lysosomes [#1].","Marks host lipid droplets internalized into the vacuole and wrapped by the intravacuolar network, linked to parasite lipid scavenging [#3].","Parasite-encoded Rab7 decorates late-endosomal-like endomembranes and a fragmenting plant vacuole-like organelle [#2, #4]."]},"strain_conflicts":[]},"prefetch_data":{},"corpus_meta":[{"pmid":"16955139","id":"PMC_16955139","title":"CD40 induces macrophage anti-Toxoplasma gondii activity by triggering autophagy-dependent fusion of pathogen-containing vacuoles and lysosomes.","date":"2006","source":"The Journal of clinical investigation","url":"https://pubmed.ncbi.nlm.nih.gov/16955139","citation_count":258,"is_preprint":false},{"pmid":"20398214","id":"PMC_20398214","title":"Characterization of a novel organelle in Toxoplasma gondii with similar composition and function to the plant vacuole.","date":"2010","source":"Molecular microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/20398214","citation_count":132,"is_preprint":false},{"pmid":"9379044","id":"PMC_9379044","title":"Intracellular fate of vacuoles containing Toxoplasma gondii is determined at the time of formation and depends on the mechanism of entry.","date":"1997","source":"Journal of immunology (Baltimore, Md. : 1950)","url":"https://pubmed.ncbi.nlm.nih.gov/9379044","citation_count":131,"is_preprint":false},{"pmid":"28570716","id":"PMC_28570716","title":"Host lipid droplets: An important source of lipids salvaged by the intracellular parasite Toxoplasma gondii.","date":"2017","source":"PLoS pathogens","url":"https://pubmed.ncbi.nlm.nih.gov/28570716","citation_count":126,"is_preprint":false},{"pmid":"27642004","id":"PMC_27642004","title":"Imaging flow cytometry analysis of intracellular pathogens.","date":"2016","source":"Methods (San Diego, Calif.)","url":"https://pubmed.ncbi.nlm.nih.gov/27642004","citation_count":46,"is_preprint":false},{"pmid":"24211609","id":"PMC_24211609","title":"Evolutionary repurposing of endosomal systems for apical organelle biogenesis in Toxoplasma gondii.","date":"2013","source":"International journal for parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/24211609","citation_count":32,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":5193,"output_tokens":1616,"usd":0.01991,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6738,"output_tokens":2705,"usd":0.050658,"stage2_stop_reason":"end_turn"},"total_usd":0.070568,"stage1_batch_id":"msgbatch_01TEPNZ4MCzJ7xtsNwosiDRk","stage2_batch_id":"msgbatch_01FQShM7n1sfCr4pWTDShmki","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 1997,\n      \"finding\": \"Toxoplasma-containing phagosomes (formed by phagocytosis of dead/opsonized parasites) sequentially acquire host Rab7, consistent with normal late-endosomal fusion; in contrast, parasitophorous vacuoles formed by active parasite invasion fail to acquire Rab7 or any other endocytic fusion proteins, indicating that exclusion of Rab7 is a key mechanism by which actively invading Toxoplasma evades lysosomal degradation.\",\n      \"method\": \"Immunofluorescence localization of endogenous endocytic markers (including Rab7) in pulse-infected bone marrow-derived macrophages; comparison of phagocytosis vs. active invasion modes\",\n      \"journal\": \"Journal of Immunology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — direct comparative localization experiment with multiple endocytic markers and two well-defined entry modes; mechanistic conclusion about Rab7 exclusion replicated across conditions within a rigorous study\",\n      \"pmids\": [\"9379044\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2006,\n      \"finding\": \"CD40 stimulation of macrophages infected with T. gondii triggers autophagy-dependent fusion of parasitophorous vacuoles with late endosomes/lysosomes; pharmacological and genetic impairment of Rab7 (alongside PIK3C3, vacuolar ATPase, and lysosomal enzymes) blocked this vacuole/lysosome fusion and abolished CD40-induced antimicrobial activity, placing Rab7 as a required effector in this pathway.\",\n      \"method\": \"Genetic (Rab7 dominant-negative/knockdown) and pharmacological approaches combined with immunofluorescence colocalization and antimicrobial activity assays in human and mouse macrophages\",\n      \"journal\": \"The Journal of Clinical Investigation\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — multiple orthogonal methods (genetic, pharmacological, colocalization, functional killing assay) in both human and mouse macrophages; Rab7 requirement demonstrated alongside mechanistic autophagy pathway placement\",\n      \"pmids\": [\"16955139\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2010,\n      \"finding\": \"In intracellular T. gondii tachyzoites, a novel plant vacuole-like organelle fragments during intracellular growth, with some of its markers colocalizing with the late-endosomal marker Rab7, suggesting involvement of Rab7-positive compartments in the endocytic-like pathway associated with this organelle.\",\n      \"method\": \"Immunofluorescence colocalization of organelle markers with Rab7 in intracellular tachyzoites; electron tomography\",\n      \"journal\": \"Molecular Microbiology\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single colocalization observation, no functional perturbation of Rab7 itself; mechanistic link to Rab7 function is inferential\",\n      \"pmids\": [\"20398214\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"During Toxoplasma infection, host lipid droplets (LD) internalized within the parasitophorous vacuole remain associated with Rab7 and become wrapped by the intravacuolar network of membranes (IVN); this Rab7-associated LD pool is implicated in parasite lipid scavenging, as mutant parasites lacking IVN formation or an IVN-localized phospholipase A2 show diminished lipid uptake from host LD.\",\n      \"method\": \"Immunofluorescence and live imaging of Rab7-associated LD in infected cells; genetic loss-of-function (IVN-deficient mutants, phospholipase A2 knockout) with lipid uptake assays\",\n      \"journal\": \"PLoS Pathogens\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — Rab7 colocalization with internalized LD supported by genetic mutants showing functional consequences; single lab, but two orthogonal approaches (imaging + genetics)\",\n      \"pmids\": [\"28570716\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2013,\n      \"finding\": \"Rab7, a classical marker of late endocytic compartments, decorates endomembranous structures in T. gondii, suggesting operation of an endosomal-like system that has been evolutionarily repurposed for trafficking and sorting proteins to apical secretory organelles (rhoptries and micronemes) via the ER and Golgi.\",\n      \"method\": \"Review/synthesis of existing localization data on Rab5 and Rab7 in T. gondii; no new primary experiments reported\",\n      \"journal\": \"International Journal for Parasitology\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 4 / Weak — review paper synthesizing prior localization observations without new functional experiments on Rab7 itself\",\n      \"pmids\": [\"24211609\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"In Toxoplasma gondii, host-cell Rab7 is excluded from the parasitophorous vacuole formed during active invasion (a key evasion mechanism), but is required for CD40-triggered autophagy-dependent rerouting of the vacuole to lysosomes in macrophages; within the parasite, Rab7 marks late-endosomal-like compartments associated with internalized host lipid droplets and a plant vacuole-like organelle, implicating it in an endosomal-like system used for nutrient scavenging and potentially for apical organelle biogenesis.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"Rab7 functions in the Toxoplasma gondii host-parasite interface both as a host-cell late-endosomal marker exploited during infection and as a parasite-encoded marker of an endosomal-like membrane system [#0, #4]. On the host side, actively invading tachyzoites establish a parasitophorous vacuole that fails to acquire Rab7 or other endocytic fusion proteins, whereas phagosomes containing dead or opsonized parasites recruit Rab7 normally — establishing Rab7 exclusion as a mechanism by which invading parasites evade lysosomal fusion [#0]. This exclusion can be overridden: CD40 stimulation of infected macrophages triggers autophagy-dependent fusion of the parasitophorous vacuole with late endosomes/lysosomes, and impairing Rab7 blocks this fusion and abolishes CD40-induced antimicrobial killing, placing Rab7 as a required effector of this pathway [#1]. Within the parasite, Rab7 decorates late-endosomal-like endomembranes: it associates with host lipid droplets internalized into the vacuole that become wrapped by the intravacuolar network and feed parasite lipid scavenging [#3], and marks compartments linked to a fragmenting plant vacuole-like organelle [#2]. Beyond these localization and infection-model findings, the biochemical regulation of Rab7 in this system has not been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 1997,\n      \"claim\": \"It was unknown why actively invading Toxoplasma escapes lysosomal degradation; comparing entry modes established that exclusion of host Rab7 (and other endocytic fusion proteins) from the parasitophorous vacuole is a key evasion mechanism.\",\n      \"evidence\": \"Immunofluorescence of endogenous endocytic markers in pulse-infected bone marrow-derived macrophages, comparing phagocytosis vs. active invasion\",\n      \"pmids\": [\"9379044\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Does not identify the parasite factor that mediates Rab7 exclusion\", \"Mechanism of selective marker exclusion at the vacuolar membrane not defined\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2006,\n      \"claim\": \"It was unknown how host immune signaling could redirect the evasion-competent vacuole to lysosomes; CD40 stimulation was shown to drive autophagy-dependent vacuole/lysosome fusion requiring Rab7, defining Rab7 as an effector of CD40-induced antimicrobial activity.\",\n      \"evidence\": \"Genetic (Rab7 dominant-negative/knockdown) and pharmacological perturbation with colocalization and antimicrobial killing assays in human and mouse macrophages\",\n      \"pmids\": [\"16955139\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Does not resolve how CD40 signaling overcomes the Rab7 exclusion seen during active invasion\", \"Direct Rab7 effector interactions in the fusion step not defined\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2010,\n      \"claim\": \"Whether the parasite's own endomembrane system uses Rab7-positive compartments was unclear; colocalization of markers from a fragmenting plant vacuole-like organelle with Rab7 implicated Rab7 compartments in a parasite endocytic-like pathway.\",\n      \"evidence\": \"Immunofluorescence colocalization of organelle markers with Rab7 and electron tomography in intracellular tachyzoites\",\n      \"pmids\": [\"20398214\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"Single colocalization observation without functional perturbation of Rab7\", \"Causal role of Rab7 in organelle dynamics not tested\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2013,\n      \"claim\": \"Synthesis of prior localization data framed parasite Rab7 as part of an evolutionarily repurposed endosomal-like system trafficking proteins to apical secretory organelles.\",\n      \"evidence\": \"Review synthesizing existing Rab5/Rab7 localization data; no new primary experiments\",\n      \"pmids\": [\"24211609\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No new functional data on Rab7\", \"Direct role of Rab7 in rhoptry/microneme biogenesis not experimentally demonstrated\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"How the parasite scavenges host lipids was addressed by showing host lipid droplets internalized into the vacuole remain Rab7-associated and are wrapped by the intravacuolar network, feeding parasite lipid uptake.\",\n      \"evidence\": \"Immunofluorescence and live imaging of Rab7-associated lipid droplets plus IVN-deficient and phospholipase A2 knockout mutants with lipid uptake assays\",\n      \"pmids\": [\"28570716\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Whether Rab7 itself is functionally required for lipid droplet internalization vs. being a passive marker not resolved\", \"Single-lab findings\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The biochemical regulation of Rab7 in this system — its GEFs, GAPs, effectors, and the parasite factors that mediate its exclusion or recruitment — remains uncharacterized.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No Rab7 regulators or effectors identified in the corpus\", \"Direct causal role of parasite Rab7 in apical organelle biogenesis untested\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [],\n    \"localization\": [\n      {\"term_id\": \"GO:0005770\", \"supporting_discovery_ids\": [0, 2, 3, 4], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0055037\", \"supporting_discovery_ids\": [3], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0016239\", \"supporting_discovery_ids\": [1], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0090382\", \"supporting_discovery_ids\": [0, 1], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"complexes\": [],\n    \"partners\": [],\n    \"other_free_text\": [\n      \"Host Rab7 is excluded from parasitophorous vacuoles formed by active invasion but recruited to phagosomes of dead/opsonized parasites [#0].\",\n      \"Required effector of CD40-induced, autophagy-dependent fusion of the parasitophorous vacuole with late endosomes/lysosomes [#1].\",\n      \"Marks host lipid droplets internalized into the vacuole and wrapped by the intravacuolar network, linked to parasite lipid scavenging [#3].\",\n      \"Parasite-encoded Rab7 decorates late-endosomal-like endomembranes and a fragmenting plant vacuole-like organelle [#2, #4].\"\n    ]\n  },\n  \"strain_conflicts\": []\n}","audit_flag":null,"strains":[{"strain":"ME49","gene_id":"TGME49_248880","name":"RAB7","product":"ras-related protein RAB7","uniprot_acc":"A0A125YNJ9","chromosome":"TGME49_chrXII","start_pos":4236732},{"strain":"GT1","gene_id":"TGGT1_248880","name":null,"product":"GTPase RAB7","uniprot_acc":null,"chromosome":"TGGT1_chrXII","start_pos":4169929},{"strain":"RH88","gene_id":"TGRH88_062750","name":null,"product":"GTPase RAB7","uniprot_acc":null,"chromosome":"CM023093","start_pos":4290523},{"strain":"VEG","gene_id":"TGVEG_248880","name":null,"product":"GTPase RAB7","uniprot_acc":"B6KHB1","chromosome":"TGVEG_chrXII","start_pos":4208484}]}