{"gene":"PF3D7_1334800","run_date":"2026-09-08T14:19:06","timeline":{"discoveries":[{"year":2010,"finding":"MSRP2 (PF3D7_1334800) protein is detectable by specific antibodies in P. falciparum asexual blood stages; sequential proteolytic cleavages produce 28- and 25-kDa forms. Notably, MSRP2 is absent from mature merozoites; instead, the 25-kDa form (MSRP2(25)) is soluble and secreted upon merozoite egress rather than residing on the merozoite surface.","method":"Immunoblot with antibodies to recombinant MSRP2, fractionation of merozoite lysate vs. culture supernatant","journal":"Eukaryotic cell","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct protein detection by specific antibody, fractionation demonstrating secretion vs. surface absence, single lab with two orthogonal methods (immunoblot + subcellular fractionation)","pmids":["20472690"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":"3D7"}]},{"year":2011,"finding":"MSRP2 (PF3D7_1334800) is a substrate of PfSUB1: bioinformatic and proteomic analysis of the late asexual blood stage proteome identified MSRP2 among proteins proteolytically processed by the subtilisin-like protease PfSUB1 prior to merozoite egress.","method":"Proteomics (mass spectrometry of late-stage blood-stage proteome) combined with bioinformatic prediction of PfSUB1 cleavage sites","journal":"Infection and immunity","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — proteomic identification in a global substrate screen, single lab, supported by bioinformatic corroboration but no in vitro cleavage reconstitution reported in abstract","pmids":["21220481"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2002,"finding":"MSRP2 (referred to as MSRP-2 in P. falciparum and its P. yoelii homologue) binds the amino-terminal region of MSP-1 in vitro. Yeast two-hybrid isolation using P. yoelii MSP-1 N-terminus as bait recovered the P. yoelii MSRP-2 homologue, and in vitro binding experiments confirmed interaction between P. falciparum MSRP-2 and the amino-terminal region of P. falciparum MSP-1.","method":"Yeast two-hybrid screen; in vitro binding assay","journal":"Eukaryotic cell","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — yeast two-hybrid plus in vitro binding assay confirm interaction, single lab, two complementary methods","pmids":["12477792"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""},{"species":"Plasmodium yoelii","strain":""}]},{"year":2004,"finding":"P. yoelii MSRP-2 (the rodent-parasite homologue of PF3D7_1334800) is expressed on the surface of schizonts, co-localises with the amino-terminal portion of MSP-1 and with MSP-7, and is released from the parasite into culture supernatants. Immunoprecipitation from parasite lysates and culture supernatants with anti-MSRP-2 antibodies confirmed its presence in both compartments.","method":"Immunofluorescence; immunoprecipitation from parasite lysate and culture supernatant","journal":"Infection and immunity","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — reciprocal localization and immunoprecipitation from two fractions, single lab, two orthogonal methods","pmids":["14742548"],"is_preprint":false,"attribution":[{"species":"Plasmodium yoelii","strain":"17XL"}]},{"year":2013,"finding":"Members of the MSP7-related protein (MSRP) family, which includes MSRP2 (PF3D7_1334800), were identified as PEXEL/HT-negative exported proteins (PNEPs) in P. falciparum, indicating that MSRP2 is exported into the host erythrocyte by a mechanism independent of the classical PEXEL/HT export signal, and that this export requires protein translocation across the parasitophorous vacuole membrane.","method":"Fluorescent reporter fusion assays; live imaging of exported GFP-tagged proteins","journal":"PLoS pathogens","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reporter export assays with live imaging establishing PNEP export, single lab; MSRP family identified as PNEPs but individual gene-level functional follow-up limited in abstract","pmids":["23950716"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2010,"finding":"Deletion of msrp2 (and other msrp genes) in P. falciparum 3D7 by targeted disruption produced no detectable growth or invasion phenotype; only deletion of msp7 (a distinct family member) led to a detectable phenotype. Thus MSRP2 is individually dispensable for asexual blood-stage growth in vitro.","method":"Targeted gene disruption confirmed by Southern hybridization; growth and invasion assays","journal":"Eukaryotic cell","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — clean knockout with confirmed ablation and quantitative growth/invasion readout, single lab","pmids":["20472690"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":"3D7"}]},{"year":2015,"finding":"P. berghei MSRP2 (PbMSRP2, ortholog of PF3D7_1334800) binds directly to mouse P-selectin, as shown by a systematic extracellular protein interaction screen. The interaction was confirmed biochemically and, when complexed with MSP7 family members, P-selectin could no longer bind its endogenous carbohydrate ligand Sialyl-Lewis(X), suggesting a possible immune-modulatory mechanism.","method":"Extracellular protein interaction screen (AVEXIS or equivalent); biochemical binding characterization; competition assay with Sialyl-Lewis(X)","journal":"Malaria journal","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, interaction screen with biochemical follow-up but the MSRP2-specific contribution is noted alongside another family member (MSRP1); limited orthogonal validation for MSRP2 specifically","pmids":["26045295"],"is_preprint":false,"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2015,"finding":"In P. berghei, a triple knockout of msp7/mspr1/mspr2 (the latter being the P. berghei homologue of MSRP2) showed no impairment of life cycle progression, indicating that MSRP2 ortholog is dispensable for completion of the life cycle including gametogenesis in the rodent malaria model.","method":"Triple gene deletion (msp7−/mspr1−/mspr2−) in P. berghei; life cycle progression assay","journal":"Molecular and biochemical parasitology","confidence":"Low","confidence_rationale":"Tier 2 / Weak — clean triple knockout with life cycle readout, but the MSRP2 contribution cannot be separated from the triple mutant context; single lab","pmids":["26222913"],"is_preprint":false,"attribution":[{"species":"Plasmodium berghei","strain":""}]}],"current_model":"MSRP2 (PF3D7_1334800) is a secreted, soluble member of the P. falciparum MSP7-related protein family that binds the N-terminal region of MSP-1, undergoes sequential PfSUB1-mediated proteolytic processing to 28- and 25-kDa forms, and is released into the parasitophorous vacuole/culture supernatant upon merozoite egress rather than remaining surface-associated; it is also exported into the host erythrocyte as a PEXEL-negative exported protein (PNEP), and its rodent ortholog (PbMSRP2) can bind host P-selectin, but individual deletion of MSRP2 produces no detectable growth or invasion phenotype in vitro."},"narrative":{"mechanistic_narrative":"MSRP2 (PF3D7_1334800) is a secreted member of the P. falciparum MSP7-related protein (MSRP) family that acts in the asexual blood stage in association with the MSP-1 complex rather than as a surface-resident merozoite protein [PMID:20472690, PMID:12477792]. It binds the amino-terminal region of MSP-1, an interaction first captured through the P. yoelii homologue and confirmed biochemically for P. falciparum MSRP2 [PMID:12477792]. During schizont maturation MSRP2 undergoes sequential proteolytic cleavage—it is a substrate of the subtilisin-like protease PfSUB1—generating 28- and 25-kDa forms, and the soluble 25-kDa form is released into the culture supernatant upon merozoite egress rather than remaining on the merozoite surface [PMID:20472690, PMID:21220481]. MSRP2 is also exported into the host erythrocyte as a PEXEL/HT-negative exported protein (PNEP), placing it in a translocation pathway independent of the classical PEXEL export signal [PMID:23950716]. Despite these interactions and processing events, targeted disruption of msrp2 in P. falciparum 3D7 produces no detectable growth or invasion phenotype in vitro, so its precise cellular function during blood-stage development is not established in the available corpus [PMID:20472690]. In the rodent parasite P. berghei, the ortholog PbMSRP2 binds host P-selectin, hinting at a possible host-interaction role, but the P. berghei ortholog is also dispensable for life-cycle progression [PMID:26045295, PMID:26222913].","teleology":[{"year":2002,"claim":"Establishing a binding partner was the first step in placing MSRP2 in a functional context; the question was whether it associates with any known merozoite protein.","evidence":"Yeast two-hybrid screen with P. yoelii MSP-1 N-terminus as bait plus in vitro binding assay with P. falciparum MSRP2","pmids":["12477792"],"confidence":"Medium","gaps":["Binding region on MSRP2 not mapped","Functional consequence of the MSRP2–MSP-1 interaction not defined","Interaction not confirmed in vivo in the parasite"],"attribution":[{"species":"Plasmodium falciparum","strain":""},{"species":"Plasmodium yoelii","strain":""}]},{"year":2004,"claim":"The localization and fate of MSRP2 was addressed in the rodent homologue, testing whether it behaves as a surface protein of the MSP-1/MSP-7 complex.","evidence":"Immunofluorescence and immunoprecipitation from lysate and supernatant of P. yoelii schizonts","pmids":["14742548"],"confidence":"Medium","gaps":["Shown in P. yoelii, not P. falciparum","Mechanism of release not defined","Does not establish a role for the released protein"],"attribution":[{"species":"Plasmodium yoelii","strain":"17XL"}]},{"year":2010,"claim":"The processing and secretory fate of P. falciparum MSRP2, and its functional requirement, were directly tested to determine whether it is a surface merozoite protein essential for growth.","evidence":"Immunoblot with anti-MSRP2 antibodies, subcellular fractionation, and targeted gene disruption with growth/invasion assays in P. falciparum 3D7","pmids":["20472690"],"confidence":"Medium","gaps":["No detectable knockout phenotype leaves function unexplained","Redundancy with other MSRP members not tested","Identity of the proteases generating the 28/25-kDa forms not resolved here"],"attribution":[{"species":"Plasmodium falciparum","strain":"3D7"}]},{"year":2011,"claim":"The protease responsible for MSRP2 maturation was identified, linking its cleavage to the egress protease cascade.","evidence":"Mass spectrometry of the late blood-stage proteome combined with bioinformatic prediction of PfSUB1 cleavage sites","pmids":["21220481"],"confidence":"Medium","gaps":["No in vitro cleavage reconstitution with purified PfSUB1","Functional consequence of cleavage unknown","Cleavage site positions not experimentally verified"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2013,"claim":"The trafficking of MSRP2 beyond the parasite was addressed, asking whether it reaches the host cell and by what route.","evidence":"Fluorescent reporter fusion assays and live imaging identifying MSRP family members as PEXEL/HT-negative exported proteins in P. falciparum","pmids":["23950716"],"confidence":"Medium","gaps":["Export shown at family level; MSRP2-specific export signal not mapped","Function of exported MSRP2 in the erythrocyte unknown","Translocation machinery not identified"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2015,"claim":"A candidate host-directed activity was tested by asking whether the MSRP2 ortholog engages a host receptor.","evidence":"Extracellular protein interaction screen with biochemical binding and Sialyl-Lewis(X) competition assay showing PbMSRP2 binds mouse P-selectin","pmids":["26045295"],"confidence":"Low","gaps":["MSRP2-specific contribution reported alongside MSRP1","Shown in P. berghei, not P. falciparum","In vivo immune-modulatory consequence not demonstrated"],"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2015,"claim":"The requirement of the MSRP2 ortholog across the full life cycle was tested to determine whether family redundancy masks an essential role.","evidence":"Triple gene deletion (msp7/mspr1/mspr2) in P. berghei with life-cycle progression assay","pmids":["26222913"],"confidence":"Low","gaps":["MSRP2 contribution cannot be isolated in the triple mutant","Shown in P. berghei rodent model","No phenotype leaves function undefined"],"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":null,"claim":"The core function of MSRP2 remains undefined: it binds MSP-1, is PfSUB1-processed, secreted and exported, yet no loss-of-function phenotype has been assigned in either P. falciparum or P. berghei.","evidence":"","pmids":[],"confidence":"Low","gaps":["No causal role for MSRP2 in invasion, egress, or host modulation established","Functional redundancy among MSRP members untested at the level of MSRP2-specific complementation","P-selectin engagement not tested for P. falciparum MSRP2"],"attribution":[]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["MSP-1 N-terminal complex (via binding)"],"partners":["MSP-1 (AMINO-TERMINAL REGION)","PFSUB1 (PROTEASE)","MSP-7 (CO-LOCALIZATION IN P. YOELII)","HOST P-SELECTIN (PBMSRP2 ORTHOLOG)"],"other_free_text":["Sequential proteolytic processing yields 28- and 25-kDa forms; the 25-kDa form is soluble and secreted at merozoite egress rather than surface-associated [#0].","PEXEL/HT-negative exported protein (PNEP) exported into the host erythrocyte independently of the classical PEXEL signal [#4].","Individually dispensable for asexual growth/invasion in P. falciparum 3D7 [#5] and, as part of a triple deletion, for P. berghei life-cycle progression [#7].","P-selectin binding and function characterized only for the P. berghei ortholog and partly alongside MSRP1 [#6]."]}},"prefetch_data":{},"corpus_meta":[{"pmid":"23950716","id":"PMC_23950716","title":"Identification of new PNEPs indicates a substantial non-PEXEL exportome and underpins common features in Plasmodium falciparum protein export.","date":"2013","source":"PLoS 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Notably, MSRP2 is absent from mature merozoites; instead, the 25-kDa form (MSRP2(25)) is soluble and secreted upon merozoite egress rather than residing on the merozoite surface.\",\n      \"method\": \"Immunoblot with antibodies to recombinant MSRP2, fractionation of merozoite lysate vs. culture supernatant\",\n      \"journal\": \"Eukaryotic cell\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct protein detection by specific antibody, fractionation demonstrating secretion vs. surface absence, single lab with two orthogonal methods (immunoblot + subcellular fractionation)\",\n      \"pmids\": [\"20472690\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"3D7\"}]\n    },\n    {\n      \"year\": 2011,\n      \"finding\": \"MSRP2 (PF3D7_1334800) is a substrate of PfSUB1: bioinformatic and proteomic analysis of the late asexual blood stage proteome identified MSRP2 among proteins proteolytically processed by the subtilisin-like protease PfSUB1 prior to merozoite egress.\",\n      \"method\": \"Proteomics (mass spectrometry of late-stage blood-stage proteome) combined with bioinformatic prediction of PfSUB1 cleavage sites\",\n      \"journal\": \"Infection and immunity\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — proteomic identification in a global substrate screen, single lab, supported by bioinformatic corroboration but no in vitro cleavage reconstitution reported in abstract\",\n      \"pmids\": [\"21220481\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2002,\n      \"finding\": \"MSRP2 (referred to as MSRP-2 in P. falciparum and its P. yoelii homologue) binds the amino-terminal region of MSP-1 in vitro. Yeast two-hybrid isolation using P. yoelii MSP-1 N-terminus as bait recovered the P. yoelii MSRP-2 homologue, and in vitro binding experiments confirmed interaction between P. falciparum MSRP-2 and the amino-terminal region of P. falciparum MSP-1.\",\n      \"method\": \"Yeast two-hybrid screen; in vitro binding assay\",\n      \"journal\": \"Eukaryotic cell\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — yeast two-hybrid plus in vitro binding assay confirm interaction, single lab, two complementary methods\",\n      \"pmids\": [\"12477792\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"},\n        {\"species\": \"Plasmodium yoelii\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2004,\n      \"finding\": \"P. yoelii MSRP-2 (the rodent-parasite homologue of PF3D7_1334800) is expressed on the surface of schizonts, co-localises with the amino-terminal portion of MSP-1 and with MSP-7, and is released from the parasite into culture supernatants. Immunoprecipitation from parasite lysates and culture supernatants with anti-MSRP-2 antibodies confirmed its presence in both compartments.\",\n      \"method\": \"Immunofluorescence; immunoprecipitation from parasite lysate and culture supernatant\",\n      \"journal\": \"Infection and immunity\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — reciprocal localization and immunoprecipitation from two fractions, single lab, two orthogonal methods\",\n      \"pmids\": [\"14742548\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium yoelii\", \"strain\": \"17XL\"}]\n    },\n    {\n      \"year\": 2013,\n      \"finding\": \"Members of the MSP7-related protein (MSRP) family, which includes MSRP2 (PF3D7_1334800), were identified as PEXEL/HT-negative exported proteins (PNEPs) in P. falciparum, indicating that MSRP2 is exported into the host erythrocyte by a mechanism independent of the classical PEXEL/HT export signal, and that this export requires protein translocation across the parasitophorous vacuole membrane.\",\n      \"method\": \"Fluorescent reporter fusion assays; live imaging of exported GFP-tagged proteins\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reporter export assays with live imaging establishing PNEP export, single lab; MSRP family identified as PNEPs but individual gene-level functional follow-up limited in abstract\",\n      \"pmids\": [\"23950716\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2010,\n      \"finding\": \"Deletion of msrp2 (and other msrp genes) in P. falciparum 3D7 by targeted disruption produced no detectable growth or invasion phenotype; only deletion of msp7 (a distinct family member) led to a detectable phenotype. Thus MSRP2 is individually dispensable for asexual blood-stage growth in vitro.\",\n      \"method\": \"Targeted gene disruption confirmed by Southern hybridization; growth and invasion assays\",\n      \"journal\": \"Eukaryotic cell\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — clean knockout with confirmed ablation and quantitative growth/invasion readout, single lab\",\n      \"pmids\": [\"20472690\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"3D7\"}]\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"P. berghei MSRP2 (PbMSRP2, ortholog of PF3D7_1334800) binds directly to mouse P-selectin, as shown by a systematic extracellular protein interaction screen. The interaction was confirmed biochemically and, when complexed with MSP7 family members, P-selectin could no longer bind its endogenous carbohydrate ligand Sialyl-Lewis(X), suggesting a possible immune-modulatory mechanism.\",\n      \"method\": \"Extracellular protein interaction screen (AVEXIS or equivalent); biochemical binding characterization; competition assay with Sialyl-Lewis(X)\",\n      \"journal\": \"Malaria journal\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, interaction screen with biochemical follow-up but the MSRP2-specific contribution is noted alongside another family member (MSRP1); limited orthogonal validation for MSRP2 specifically\",\n      \"pmids\": [\"26045295\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"In P. berghei, a triple knockout of msp7/mspr1/mspr2 (the latter being the P. berghei homologue of MSRP2) showed no impairment of life cycle progression, indicating that MSRP2 ortholog is dispensable for completion of the life cycle including gametogenesis in the rodent malaria model.\",\n      \"method\": \"Triple gene deletion (msp7−/mspr1−/mspr2−) in P. berghei; life cycle progression assay\",\n      \"journal\": \"Molecular and biochemical parasitology\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 2 / Weak — clean triple knockout with life cycle readout, but the MSRP2 contribution cannot be separated from the triple mutant context; single lab\",\n      \"pmids\": [\"26222913\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"MSRP2 (PF3D7_1334800) is a secreted, soluble member of the P. falciparum MSP7-related protein family that binds the N-terminal region of MSP-1, undergoes sequential PfSUB1-mediated proteolytic processing to 28- and 25-kDa forms, and is released into the parasitophorous vacuole/culture supernatant upon merozoite egress rather than remaining surface-associated; it is also exported into the host erythrocyte as a PEXEL-negative exported protein (PNEP), and its rodent ortholog (PbMSRP2) can bind host P-selectin, but individual deletion of MSRP2 produces no detectable growth or invasion phenotype in vitro.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"MSRP2 (PF3D7_1334800) is a secreted member of the P. falciparum MSP7-related protein (MSRP) family that acts in the asexual blood stage in association with the MSP-1 complex rather than as a surface-resident merozoite protein [#0, #2]. It binds the amino-terminal region of MSP-1, an interaction first captured through the P. yoelii homologue and confirmed biochemically for P. falciparum MSRP2 [#2]. During schizont maturation MSRP2 undergoes sequential proteolytic cleavage—it is a substrate of the subtilisin-like protease PfSUB1—generating 28- and 25-kDa forms, and the soluble 25-kDa form is released into the culture supernatant upon merozoite egress rather than remaining on the merozoite surface [#0, #1]. MSRP2 is also exported into the host erythrocyte as a PEXEL/HT-negative exported protein (PNEP), placing it in a translocation pathway independent of the classical PEXEL export signal [#4]. Despite these interactions and processing events, targeted disruption of msrp2 in P. falciparum 3D7 produces no detectable growth or invasion phenotype in vitro, so its precise cellular function during blood-stage development is not established in the available corpus [#5]. In the rodent parasite P. berghei, the ortholog PbMSRP2 binds host P-selectin, hinting at a possible host-interaction role, but the P. berghei ortholog is also dispensable for life-cycle progression [#6, #7].\",\n  \"teleology\": [\n    {\n      \"year\": 2002,\n      \"claim\": \"Establishing a binding partner was the first step in placing MSRP2 in a functional context; the question was whether it associates with any known merozoite protein.\",\n      \"evidence\": \"Yeast two-hybrid screen with P. yoelii MSP-1 N-terminus as bait plus in vitro binding assay with P. falciparum MSRP2\",\n      \"pmids\": [\"12477792\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Binding region on MSRP2 not mapped\", \"Functional consequence of the MSRP2\\u2013MSP-1 interaction not defined\", \"Interaction not confirmed in vivo in the parasite\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}, {\"species\": \"Plasmodium yoelii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2004,\n      \"claim\": \"The localization and fate of MSRP2 was addressed in the rodent homologue, testing whether it behaves as a surface protein of the MSP-1/MSP-7 complex.\",\n      \"evidence\": \"Immunofluorescence and immunoprecipitation from lysate and supernatant of P. yoelii schizonts\",\n      \"pmids\": [\"14742548\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Shown in P. yoelii, not P. falciparum\", \"Mechanism of release not defined\", \"Does not establish a role for the released protein\"],\n      \"attribution\": [{\"species\": \"Plasmodium yoelii\", \"strain\": \"17XL\"}]\n    },\n    {\n      \"year\": 2010,\n      \"claim\": \"The processing and secretory fate of P. falciparum MSRP2, and its functional requirement, were directly tested to determine whether it is a surface merozoite protein essential for growth.\",\n      \"evidence\": \"Immunoblot with anti-MSRP2 antibodies, subcellular fractionation, and targeted gene disruption with growth/invasion assays in P. falciparum 3D7\",\n      \"pmids\": [\"20472690\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No detectable knockout phenotype leaves function unexplained\", \"Redundancy with other MSRP members not tested\", \"Identity of the proteases generating the 28/25-kDa forms not resolved here\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"3D7\"}]\n    },\n    {\n      \"year\": 2011,\n      \"claim\": \"The protease responsible for MSRP2 maturation was identified, linking its cleavage to the egress protease cascade.\",\n      \"evidence\": \"Mass spectrometry of the late blood-stage proteome combined with bioinformatic prediction of PfSUB1 cleavage sites\",\n      \"pmids\": [\"21220481\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No in vitro cleavage reconstitution with purified PfSUB1\", \"Functional consequence of cleavage unknown\", \"Cleavage site positions not experimentally verified\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2013,\n      \"claim\": \"The trafficking of MSRP2 beyond the parasite was addressed, asking whether it reaches the host cell and by what route.\",\n      \"evidence\": \"Fluorescent reporter fusion assays and live imaging identifying MSRP family members as PEXEL/HT-negative exported proteins in P. falciparum\",\n      \"pmids\": [\"23950716\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Export shown at family level; MSRP2-specific export signal not mapped\", \"Function of exported MSRP2 in the erythrocyte unknown\", \"Translocation machinery not identified\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"A candidate host-directed activity was tested by asking whether the MSRP2 ortholog engages a host receptor.\",\n      \"evidence\": \"Extracellular protein interaction screen with biochemical binding and Sialyl-Lewis(X) competition assay showing PbMSRP2 binds mouse P-selectin\",\n      \"pmids\": [\"26045295\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"MSRP2-specific contribution reported alongside MSRP1\", \"Shown in P. berghei, not P. falciparum\", \"In vivo immune-modulatory consequence not demonstrated\"],\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2015,\n      \"claim\": \"The requirement of the MSRP2 ortholog across the full life cycle was tested to determine whether family redundancy masks an essential role.\",\n      \"evidence\": \"Triple gene deletion (msp7/mspr1/mspr2) in P. berghei with life-cycle progression assay\",\n      \"pmids\": [\"26222913\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"MSRP2 contribution cannot be isolated in the triple mutant\", \"Shown in P. berghei rodent model\", \"No phenotype leaves function undefined\"],\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The core function of MSRP2 remains undefined: it binds MSP-1, is PfSUB1-processed, secreted and exported, yet no loss-of-function phenotype has been assigned in either P. falciparum or P. berghei.\",\n      \"evidence\": null,\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No causal role for MSRP2 in invasion, egress, or host modulation established\", \"Functional redundancy among MSRP members untested at the level of MSRP2-specific complementation\", \"P-selectin engagement not tested for P. falciparum MSRP2\"],\n      \"attribution\": []\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0005515\", \"supporting_discovery_ids\": [2, 6]},\n      {\"term_id\": \"GO:0008233\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005576\", \"supporting_discovery_ids\": [0, 3]},\n      {\"term_id\": \"GO:0020002\", \"supporting_discovery_ids\": [4]},\n      {\"term_id\": \"GO:0020030\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0006508\", \"supporting_discovery_ids\": [0, 1]},\n      {\"term_id\": \"GO:0046903\", \"supporting_discovery_ids\": [0, 3]}\n    ],\n    \"complexes\": [\"MSP-1 N-terminal complex (via binding)\"],\n    \"partners\": [\"MSP-1 (amino-terminal region)\", \"PfSUB1 (protease)\", \"MSP-7 (co-localization in P. yoelii)\", \"host P-selectin (PbMSRP2 ortholog)\"],\n    \"other_free_text\": [\n      \"Sequential proteolytic processing yields 28- and 25-kDa forms; the 25-kDa form is soluble and secreted at merozoite egress rather than surface-associated [#0].\",\n      \"PEXEL/HT-negative exported protein (PNEP) exported into the host erythrocyte independently of the classical PEXEL signal [#4].\",\n      \"Individually dispensable for asexual growth/invasion in P. falciparum 3D7 [#5] and, as part of a triple deletion, for P. berghei life-cycle progression [#7].\",\n      \"P-selectin binding and function characterized only for the P. berghei ortholog and partly alongside MSRP1 [#6].\"\n    ]\n  }\n}","audit_flag":{"gene":"PF3D7_1334800","tier":"IDENTITY_CHECK","verdict":"identity unverified","subtype":"names_other_cards","uniprot_band":"","rules_fired":"R12","issue":"No cited paper names this card; 5 of 7 cited papers name other catalogue genes (PF3D7_0930300, PF3D7_0507500, PF3D7_1410400). The summary may describe one of those genes."},"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_1334800","name":null,"product":"MSP7-like protein","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_1349100","name":null,"product":"MSP7-like protein","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_1266000","name":null,"product":"merozoite surface protein 7D","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"MSP7","evaluation":null}