{"gene":"PF3D7_1451600","run_date":"2026-09-08T14:19:07","timeline":{"discoveries":[{"year":2013,"finding":"LAP5 (PF3D7_1451600) protein is not detected in gametocytes of P. berghei despite prominent transcription of its gene in sexual blood stage parasites, indicating that translational repression controls its expression. GFP-tagging showed LAP5 (PbLAP5) is associated with crystalloids in the ookinete/early oocyst stage, consistent with post-transcriptional regulation delaying protein accumulation until after gametogenesis.","method":"GFP-tagging of PbLAP5 in transgenic P. berghei; fluorescence microscopy for protein localization; comparison of transcript and protein expression levels","journal":"Molecular and biochemical parasitology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct GFP localization experiment with functional interpretation, single lab, two orthogonal methods (fluorescence microscopy + transcript analysis)","pmids":["23684590"],"is_preprint":false,"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2017,"finding":"LAP5 (PbLAP5) is recruited into the LAP protein complex after fertilization (i.e., in the ookinete stage), joining the pre-formed LAP1/LAP2/LAP3 gametocyte complex. This recruitment is facilitated chiefly by LAP1 through its scavenger receptor cysteine-rich (SRCR) modules, as established by affinity purification and quantitative mass spectrometry of reporter-tagged LAP lines.","method":"Affinity purification of reporter-tagged LAPs combined with high-accuracy label-free quantitative mass spectrometry in transgenic P. berghei","journal":"Molecular and biochemical parasitology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — affinity purification with MS quantification, single lab, multiple LAP parasite lines compared","pmids":["28414172"],"is_preprint":false,"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2020,"finding":"LAP5 (PbLAP5) is part of an extended LAP interactome of ~50 proteins identified by GFP affinity pulldown and high-accuracy mass spectrometry from LAP3-GFP-expressing parasites; this interactome includes members of CPW-WPC and pleckstrin homology-like domain protein families, indicating LAP5 (as a LAP complex member) participates in a larger molecular assembly that facilitates crystalloid targeting and biogenesis.","method":"GFP affinity pulldown of LAP3::GFP combined with high-accuracy mass spectrometry in transgenic P. berghei; fluorescence microscopy for crystalloid co-localization","journal":"Journal of proteomics","confidence":"Low","confidence_rationale":"Tier 3 / Weak — LAP5 is identified as a complex member by mass spectrometry but no direct functional experiment was performed specifically on LAP5 itself in this study","pmids":["32736136"],"is_preprint":false,"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2009,"finding":"LAP5 (a member of the LCCL protein family) is targeted to the crystalloid organelle in P. berghei ookinetes and early oocysts, as shown by fluorescent protein tagging, extending the crystalloid localization previously established for PbSR (LAP3) to additional LAP family members.","method":"Fluorescent protein tagging and live-cell fluorescence microscopy in transgenic P. berghei","journal":"Molecular and biochemical parasitology","confidence":"Low","confidence_rationale":"Tier 3 / Weak — direct localization experiment by GFP tagging, single lab, single method; LAP5 mentioned as one of two additional family members without individual functional follow-up","pmids":["19932717"],"is_preprint":false,"attribution":[{"species":"Plasmodium berghei","strain":""}]}],"current_model":"LAP5 (PF3D7_1451600) is a member of the six-protein LCCL lectin adhesive-like protein (LAP) complex in Plasmodium; its mRNA is transcribed in gametocytes but its protein expression is subject to translational repression, delaying accumulation until after fertilization, whereupon it is recruited to the pre-formed LAP1/LAP2/LAP3 sub-complex (via LAP1 SRCR modules) and localises to the crystalloid organelle in ookinetes and early oocysts, where the LAP complex as a whole is required for crystalloid biogenesis, oocyst cell division, and sporozoite formation."},"narrative":{"mechanistic_narrative":"LAP5 (PF3D7_1451600) is a member of the LCCL lectin adhesive-like protein (LAP) complex of Plasmodium that functions in the crystalloid organelle during the mosquito-stage transition of the parasite [PMID:23684590, PMID:19932717]. In P. berghei, LAP5 mRNA is transcribed in sexual blood-stage (gametocyte) parasites, but its protein is not detected at that stage, indicating that translational repression delays LAP5 protein accumulation until after gametogenesis [PMID:23684590]. Following fertilization, in the ookinete and early oocyst stages, LAP5 is recruited into the LAP complex, joining the pre-formed LAP1/LAP2/LAP3 sub-complex chiefly through the SRCR modules of LAP1, and localizes to the crystalloid organelle [PMID:28414172, PMID:23684590, PMID:19932717]. Beyond its membership in this complex and its crystalloid targeting, no LAP5-specific molecular activity or phenotype has been characterized in the available corpus; the wider ~50-protein LAP interactome and the complex's role in crystalloid biogenesis are established at the level of other LAP members rather than through direct functional study of LAP5 itself [PMID:32736136].","teleology":[{"year":2009,"claim":"Establishing where LAP5 acts within the parasite was the first requirement for placing it in a cellular process; tagging showed LAP5 is targeted to the crystalloid organelle in ookinetes and early oocysts.","evidence":"Fluorescent protein tagging and live-cell microscopy in transgenic P. berghei","pmids":["19932717"],"confidence":"Low","gaps":["LAP5 mentioned as one of two additional family members without individual functional follow-up","No functional consequence of crystalloid localization tested for LAP5 specifically","Mechanism of crystalloid targeting not defined"],"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2013,"claim":"The disconnect between LAP5 transcript and protein levels answered how its expression is timed: translational repression withholds LAP5 protein in gametocytes and delays accumulation until the crystalloid-forming stages.","evidence":"GFP-tagging of PbLAP5 with fluorescence microscopy plus transcript-versus-protein comparison in transgenic P. berghei","pmids":["23684590"],"confidence":"Medium","gaps":["The molecular machinery mediating LAP5 translational repression is not identified","No demonstration of a LAP5 loss-of-function phenotype","Timing of protein onset defined by localization rather than quantitative protein kinetics"],"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2017,"claim":"How LAP5 assembles into the complex was resolved by showing it is recruited post-fertilization into a pre-formed LAP1/LAP2/LAP3 sub-complex, chiefly via LAP1 SRCR modules, ordering the assembly hierarchy.","evidence":"Affinity purification of reporter-tagged LAPs with label-free quantitative mass spectrometry in transgenic P. berghei","pmids":["28414172"],"confidence":"Medium","gaps":["Direct LAP1-LAP5 binding interface not structurally mapped","Whether LAP5 recruitment is required for complex function untested","Contribution of LAP5 to complex stability not measured"],"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2020,"claim":"Broadening the complex context, LAP5 was placed within an extended ~50-protein interactome including CPW-WPC and pleckstrin homology-like domain proteins, situating the LAP complex in a larger assembly linked to crystalloid targeting and biogenesis.","evidence":"GFP affinity pulldown of LAP3::GFP with high-accuracy mass spectrometry and crystalloid co-localization microscopy in transgenic P. berghei","pmids":["32736136"],"confidence":"Low","gaps":["LAP5 identified only as a complex member; no direct functional experiment on LAP5 in this study","Interactome derived from LAP3-GFP pulldown, not LAP5 bait","Which interactome members contact LAP5 directly is unknown"],"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":null,"claim":"It remains unknown what LAP5 contributes to the LAP complex on its own — whether its loss affects crystalloid biogenesis, oocyst division, or sporozoite formation, and what its LCCL-domain-based molecular activity is.","evidence":"","pmids":[],"confidence":"Low","gaps":["No LAP5-specific gene disruption or phenotype reported in the corpus","No biochemical activity assigned to the LAP5 LCCL/lectin-like domains","All functional inference derives from other LAP members or the complex as a whole"],"attribution":[{"species":"Plasmodium berghei","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["LCCL lectin adhesive-like protein (LAP) complex","LAP1/LAP2/LAP3 sub-complex (LAP5 recruited post-fertilization)"],"partners":["LAP1 (RECRUITS LAP5 VIA SRCR MODULES)","LAP2","LAP3","EXTENDED LAP INTERACTOME INCLUDING CPW-WPC AND PLECKSTRIN HOMOLOGY-LIKE DOMAIN PROTEINS"],"other_free_text":["LAP5 mRNA transcribed in gametocytes but protein subject to translational repression, delaying accumulation until after fertilization [#0]","All direct evidence is from Plasmodium berghei orthologs; no P. falciparum-specific functional data in the corpus","No LAP5-specific loss-of-function phenotype established; functional roles attributed to the LAP complex as a whole"]}},"prefetch_data":{},"corpus_meta":[{"pmid":"10971586","id":"PMC_10971586","title":"The LCCL module.","date":"2000","source":"European journal of biochemistry","url":"https://pubmed.ncbi.nlm.nih.gov/10971586","citation_count":84,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["LCCL"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"12354219","id":"PMC_12354219","title":"A malaria scavenger receptor-like protein essential for parasite development.","date":"2002","source":"Molecular microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/12354219","citation_count":75,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["LCCL"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"17335349","id":"PMC_17335349","title":"Female inheritance of malarial lap genes is essential for mosquito transmission.","date":"2007","source":"PLoS pathogens","url":"https://pubmed.ncbi.nlm.nih.gov/17335349","citation_count":62,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["LCCL"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"11985859","id":"PMC_11985859","title":"PSLAP, a protein with multiple adhesive motifs, is expressed in Plasmodium falciparum gametocytes.","date":"2002","source":"Molecular and biochemical parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/11985859","citation_count":51,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["LCCL"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"19932717","id":"PMC_19932717","title":"Plasmodium berghei crystalloids contain multiple LCCL proteins.","date":"2009","source":"Molecular and biochemical parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/19932717","citation_count":39,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["LCCL"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"15562607","id":"PMC_15562607","title":"Functional characterization of an LCCL-lectin domain containing protein family in Plasmodium berghei.","date":"2004","source":"The Journal of parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/15562607","citation_count":38,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["LCCL"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"23684590","id":"PMC_23684590","title":"Translational repression controls temporal expression of the Plasmodium berghei LCCL protein complex.","date":"2013","source":"Molecular and biochemical parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/23684590","citation_count":33,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["LCCL","PbLAP5"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"25900212","id":"PMC_25900212","title":"Biogenesis of the crystalloid organelle in Plasmodium involves microtubule-dependent vesicle transport and assembly.","date":"2015","source":"International journal for parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/25900212","citation_count":22,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["LCCL"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"30367865","id":"PMC_30367865","title":"The Plasmodium LAP complex affects crystalloid biogenesis and oocyst cell division.","date":"2018","source":"International journal for parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/30367865","citation_count":16,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["LCCL"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"32736136","id":"PMC_32736136","title":"Plasmodium berghei LAPs form an extended protein complex that facilitates crystalloid targeting and biogenesis.","date":"2020","source":"Journal of proteomics","url":"https://pubmed.ncbi.nlm.nih.gov/32736136","citation_count":16,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["LCCL"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"28414172","id":"PMC_28414172","title":"LCCL protein complex formation in Plasmodium is critically dependent on LAP1.","date":"2017","source":"Molecular and biochemical parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/28414172","citation_count":15,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["LAP5","LCCL"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"33941493","id":"PMC_33941493","title":"Crystalloids: Fascinating Parasite Organelles Essential for Malaria Transmission.","date":"2021","source":"Trends in parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/33941493","citation_count":15,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["LCCL"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"22877575","id":"PMC_22877575","title":"Conformational co-dependence between Plasmodium berghei LCCL proteins promotes complex formation and stability.","date":"2012","source":"Molecular and biochemical parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/22877575","citation_count":11,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["LCCL"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"35394999","id":"PMC_35394999","title":"Comparison of PvLAP5 and Pvs25 qRT-PCR assays for the detection of Plasmodium vivax gametocytes in field samples preserved at ambient temperature from remote malaria endemic regions of Panama.","date":"2022","source":"PLoS neglected tropical diseases","url":"https://pubmed.ncbi.nlm.nih.gov/35394999","citation_count":7,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PvLAP5"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"38399683","id":"PMC_38399683","title":"The Multiple Roles of LCCL Domain-Containing Proteins for Malaria Parasite Transmission.","date":"2024","source":"Microorganisms","url":"https://pubmed.ncbi.nlm.nih.gov/38399683","citation_count":6,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["LCCL"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"30753856","id":"PMC_30753856","title":"Dysregulated gene expression in oocysts of Plasmodium berghei LAP mutants.","date":"2019","source":"Molecular and biochemical parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/30753856","citation_count":4,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["LCCL"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"35923798","id":"PMC_35923798","title":"The WD40-Protein PfWLP1 Ensures Stability of the PfCCp-Based Adhesion Protein Complex in Plasmodium falciparum Gametocytes.","date":"2022","source":"Frontiers in cellular and infection microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/35923798","citation_count":4,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["LCCL"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"30401681","id":"PMC_30401681","title":"Interaction with complement proteins and dendritic cells implicates LCCL domain-containing proteins (CCps) of malaria parasites in immunomodulation.","date":"2018","source":"The Biochemical journal","url":"https://pubmed.ncbi.nlm.nih.gov/30401681","citation_count":3,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["LCCL"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"38862023","id":"PMC_38862023","title":"Plasmodium LCCL domain-containing modular proteins have their origins in the ancestral alveolate.","date":"2024","source":"Open biology","url":"https://pubmed.ncbi.nlm.nih.gov/38862023","citation_count":1,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["LCCL"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":10850,"output_tokens":1309,"usd":0.026093,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6215,"output_tokens":2366,"usd":0.045112,"stage2_stop_reason":"end_turn"},"total_usd":0.071205,"stage1_batch_id":"msgbatch_011BPjN2BL33F8cJXD1r7V7T","stage2_batch_id":"msgbatch_01Qwg6vP7qxkpL6Gsc7tajsb","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2013,\n      \"finding\": \"LAP5 (PF3D7_1451600) protein is not detected in gametocytes of P. berghei despite prominent transcription of its gene in sexual blood stage parasites, indicating that translational repression controls its expression. GFP-tagging showed LAP5 (PbLAP5) is associated with crystalloids in the ookinete/early oocyst stage, consistent with post-transcriptional regulation delaying protein accumulation until after gametogenesis.\",\n      \"method\": \"GFP-tagging of PbLAP5 in transgenic P. berghei; fluorescence microscopy for protein localization; comparison of transcript and protein expression levels\",\n      \"journal\": \"Molecular and biochemical parasitology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct GFP localization experiment with functional interpretation, single lab, two orthogonal methods (fluorescence microscopy + transcript analysis)\",\n      \"pmids\": [\"23684590\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"LAP5 (PbLAP5) is recruited into the LAP protein complex after fertilization (i.e., in the ookinete stage), joining the pre-formed LAP1/LAP2/LAP3 gametocyte complex. This recruitment is facilitated chiefly by LAP1 through its scavenger receptor cysteine-rich (SRCR) modules, as established by affinity purification and quantitative mass spectrometry of reporter-tagged LAP lines.\",\n      \"method\": \"Affinity purification of reporter-tagged LAPs combined with high-accuracy label-free quantitative mass spectrometry in transgenic P. berghei\",\n      \"journal\": \"Molecular and biochemical parasitology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — affinity purification with MS quantification, single lab, multiple LAP parasite lines compared\",\n      \"pmids\": [\"28414172\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"LAP5 (PbLAP5) is part of an extended LAP interactome of ~50 proteins identified by GFP affinity pulldown and high-accuracy mass spectrometry from LAP3-GFP-expressing parasites; this interactome includes members of CPW-WPC and pleckstrin homology-like domain protein families, indicating LAP5 (as a LAP complex member) participates in a larger molecular assembly that facilitates crystalloid targeting and biogenesis.\",\n      \"method\": \"GFP affinity pulldown of LAP3::GFP combined with high-accuracy mass spectrometry in transgenic P. berghei; fluorescence microscopy for crystalloid co-localization\",\n      \"journal\": \"Journal of proteomics\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — LAP5 is identified as a complex member by mass spectrometry but no direct functional experiment was performed specifically on LAP5 itself in this study\",\n      \"pmids\": [\"32736136\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2009,\n      \"finding\": \"LAP5 (a member of the LCCL protein family) is targeted to the crystalloid organelle in P. berghei ookinetes and early oocysts, as shown by fluorescent protein tagging, extending the crystalloid localization previously established for PbSR (LAP3) to additional LAP family members.\",\n      \"method\": \"Fluorescent protein tagging and live-cell fluorescence microscopy in transgenic P. berghei\",\n      \"journal\": \"Molecular and biochemical parasitology\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — direct localization experiment by GFP tagging, single lab, single method; LAP5 mentioned as one of two additional family members without individual functional follow-up\",\n      \"pmids\": [\"19932717\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"LAP5 (PF3D7_1451600) is a member of the six-protein LCCL lectin adhesive-like protein (LAP) complex in Plasmodium; its mRNA is transcribed in gametocytes but its protein expression is subject to translational repression, delaying accumulation until after fertilization, whereupon it is recruited to the pre-formed LAP1/LAP2/LAP3 sub-complex (via LAP1 SRCR modules) and localises to the crystalloid organelle in ookinetes and early oocysts, where the LAP complex as a whole is required for crystalloid biogenesis, oocyst cell division, and sporozoite formation.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"LAP5 (PF3D7_1451600) is a member of the LCCL lectin adhesive-like protein (LAP) complex of Plasmodium that functions in the crystalloid organelle during the mosquito-stage transition of the parasite [#0, #3]. In P. berghei, LAP5 mRNA is transcribed in sexual blood-stage (gametocyte) parasites, but its protein is not detected at that stage, indicating that translational repression delays LAP5 protein accumulation until after gametogenesis [#0]. Following fertilization, in the ookinete and early oocyst stages, LAP5 is recruited into the LAP complex, joining the pre-formed LAP1/LAP2/LAP3 sub-complex chiefly through the SRCR modules of LAP1, and localizes to the crystalloid organelle [#1, #0, #3]. Beyond its membership in this complex and its crystalloid targeting, no LAP5-specific molecular activity or phenotype has been characterized in the available corpus; the wider ~50-protein LAP interactome and the complex's role in crystalloid biogenesis are established at the level of other LAP members rather than through direct functional study of LAP5 itself [#2].\",\n  \"teleology\": [\n    {\n      \"year\": 2009,\n      \"claim\": \"Establishing where LAP5 acts within the parasite was the first requirement for placing it in a cellular process; tagging showed LAP5 is targeted to the crystalloid organelle in ookinetes and early oocysts.\",\n      \"evidence\": \"Fluorescent protein tagging and live-cell microscopy in transgenic P. berghei\",\n      \"pmids\": [\"19932717\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"LAP5 mentioned as one of two additional family members without individual functional follow-up\",\n        \"No functional consequence of crystalloid localization tested for LAP5 specifically\",\n        \"Mechanism of crystalloid targeting not defined\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2013,\n      \"claim\": \"The disconnect between LAP5 transcript and protein levels answered how its expression is timed: translational repression withholds LAP5 protein in gametocytes and delays accumulation until the crystalloid-forming stages.\",\n      \"evidence\": \"GFP-tagging of PbLAP5 with fluorescence microscopy plus transcript-versus-protein comparison in transgenic P. berghei\",\n      \"pmids\": [\"23684590\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"The molecular machinery mediating LAP5 translational repression is not identified\",\n        \"No demonstration of a LAP5 loss-of-function phenotype\",\n        \"Timing of protein onset defined by localization rather than quantitative protein kinetics\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"How LAP5 assembles into the complex was resolved by showing it is recruited post-fertilization into a pre-formed LAP1/LAP2/LAP3 sub-complex, chiefly via LAP1 SRCR modules, ordering the assembly hierarchy.\",\n      \"evidence\": \"Affinity purification of reporter-tagged LAPs with label-free quantitative mass spectrometry in transgenic P. berghei\",\n      \"pmids\": [\"28414172\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Direct LAP1-LAP5 binding interface not structurally mapped\",\n        \"Whether LAP5 recruitment is required for complex function untested\",\n        \"Contribution of LAP5 to complex stability not measured\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"Broadening the complex context, LAP5 was placed within an extended ~50-protein interactome including CPW-WPC and pleckstrin homology-like domain proteins, situating the LAP complex in a larger assembly linked to crystalloid targeting and biogenesis.\",\n      \"evidence\": \"GFP affinity pulldown of LAP3::GFP with high-accuracy mass spectrometry and crystalloid co-localization microscopy in transgenic P. berghei\",\n      \"pmids\": [\"32736136\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"LAP5 identified only as a complex member; no direct functional experiment on LAP5 in this study\",\n        \"Interactome derived from LAP3-GFP pulldown, not LAP5 bait\",\n        \"Which interactome members contact LAP5 directly is unknown\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"It remains unknown what LAP5 contributes to the LAP complex on its own — whether its loss affects crystalloid biogenesis, oocyst division, or sporozoite formation, and what its LCCL-domain-based molecular activity is.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No LAP5-specific gene disruption or phenotype reported in the corpus\",\n        \"No biochemical activity assigned to the LAP5 LCCL/lectin-like domains\",\n        \"All functional inference derives from other LAP members or the complex as a whole\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [],\n    \"localization\": [\n      {\"term_id\": \"crystalloid organelle\", \"supporting_discovery_ids\": [0, 3]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"crystalloid biogenesis / mosquito-stage development\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"complexes\": [\n      \"LCCL lectin adhesive-like protein (LAP) complex\",\n      \"LAP1/LAP2/LAP3 sub-complex (LAP5 recruited post-fertilization)\"\n    ],\n    \"partners\": [\n      \"LAP1 (recruits LAP5 via SRCR modules)\",\n      \"LAP2\",\n      \"LAP3\",\n      \"extended LAP interactome including CPW-WPC and pleckstrin homology-like domain proteins\"\n    ],\n    \"other_free_text\": [\n      \"LAP5 mRNA transcribed in gametocytes but protein subject to translational repression, delaying accumulation until after fertilization [#0]\",\n      \"All direct evidence is from Plasmodium berghei orthologs; no P. falciparum-specific functional data in the corpus\",\n      \"No LAP5-specific loss-of-function phenotype established; functional roles attributed to the LAP complex as a whole\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_1451600","name":null,"product":"LCCL domain-containing protein","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_1315300","name":null,"product":"LCCL domain-containing protein","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_1230500","name":null,"product":"LCCL domain-containing protein, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"LAP5","evaluation":null}