{"doi":"10.1371/journal.ppat.1011449","title":"A malaria parasite phospholipase facilitates efficient asexual blood stage egress","abstract":"<jats:p>\n                    Malaria parasite release (egress) from host red blood cells involves parasite-mediated membrane poration and rupture, thought to involve membrane-lytic effector molecules such as perforin-like proteins and/or phospholipases. With the aim of identifying these effectors, we disrupted the expression of two\n                    <jats:italic>Plasmodium falciparum</jats:italic>\n                    perforin-like proteins simultaneously and showed that they have no essential roles during blood stage egress. Proteomic profiling of parasite proteins discharged into the parasitophorous vacuole (PV) just prior to egress detected the presence in the PV of a lecithin:cholesterol acyltransferase (LCAT; PF3D7_0629300). Conditional ablation of LCAT resulted in abnormal egress and a reduced replication rate. Lipidomic profiles of LCAT-null parasites showed drastic changes in several phosphatidylserine and acylphosphatidylglycerol species during egress. We thus show that, in addition to its previously demonstrated role in liver stage merozoite egress, LCAT is required to facilitate efficient egress in asexual blood stage malaria parasites.\n                  </jats:p>","journal":"PLOS Pathogens","year":2023,"id":674989,"datarank":0.42498200160843247,"base_score":2.833213344056216,"endowment":2.833213344056216,"self_citation_contribution":0.42498200160843247,"citation_network_contribution":0.0,"self_endowment_contribution":0.42498200160843247,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":16,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":725554,"name":"Paul-Christian Burda","orcid":"0000-0003-0461-4352","position":1,"is_corresponding":false},{"id":699700,"name":"Konstantinos Koussis","orcid":"0000-0002-6737-8724","position":2,"is_corresponding":false},{"id":743588,"name":"James A. Thomas","orcid":"0000-0002-2509-490X","position":3,"is_corresponding":false},{"id":725552,"name":"Emma Pietsch","orcid":"0000-0003-4744-1666","position":4,"is_corresponding":false},{"id":1763637,"name":"Enrica Calvani","orcid":null,"position":5,"is_corresponding":false},{"id":1763638,"name":"Steven A. Howell","orcid":null,"position":6,"is_corresponding":false},{"id":259747,"name":"James I. MacRae","orcid":"0000-0002-1464-8583","position":7,"is_corresponding":false},{"id":145294,"name":"Ambrosius P. Snijders","orcid":null,"position":8,"is_corresponding":false},{"id":1454024,"name":"Tim-Wolf Gilberger","orcid":null,"position":9,"is_corresponding":false},{"id":699702,"name":"Michael J. Blackman","orcid":"0000-0002-7442-3810","position":10,"is_corresponding":false},{"id":811329,"name":"Abhinay Ramaprasad","orcid":"0000-0001-9372-5526","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"A malaria parasite phospholipase facilitates efficient asexual blood stage egress","abstract":"<jats:p>\n                    Malaria parasite release (egress) from host red blood cells involves parasite-mediated membrane poration and rupture, thought to involve membrane-lytic effector molecules such as perforin-like proteins and/or phospholipases. With the aim of identifying these effectors, we disrupted the expression of two\n                    <jats:italic>Plasmodium falciparum</jats:italic>\n                    perforin-like proteins simultaneously and showed that they have no essential roles during blood stage egress. Proteomic profiling of parasite proteins discharged into the parasitophorous vacuole (PV) just prior to egress detected the presence in the PV of a lecithin:cholesterol acyltransferase (LCAT; PF3D7_0629300). Conditional ablation of LCAT resulted in abnormal egress and a reduced replication rate. Lipidomic profiles of LCAT-null parasites showed drastic changes in several phosphatidylserine and acylphosphatidylglycerol species during egress. We thus show that, in addition to its previously demonstrated role in liver stage merozoite egress, LCAT is required to facilitate efficient egress in asexual blood stage malaria parasites.\n                  </jats:p>","is_dataset_classified":null,"base_score":2.833213344056216,"endowment":2.833213344056216,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"37352369","pmcid":"PMC10325081","openalex_id":"https://openalex.org/W4381839338","authors":[],"funders":[{"funder_name":"H2020 Marie Skłodowska-Curie Actions","grant_id":"751865","title":"Role of perforin-like proteins and phospholipases in malaria parasite egress"},{"funder_name":"Wellcome Trust","grant_id":"220318/A/20/Z","title":null},{"funder_name":"Cancer Research UK","grant_id":"CC2129","title":null},{"funder_name":"Wellcome Trust","grant_id":"ISSF2","title":null},{"funder_name":"Deutsche Forschungsgemeinschaft","grant_id":"414222880","title":null},{"funder_name":"Deutsche Forschungsgemeinschaft","grant_id":"SPP2225","title":null},{"funder_name":"The Francis Crick Institute","grant_id":"CC1063","title":null},{"funder_name":"Deutsche Forschungsgemeinschaft","grant_id":"unidentified","title":"unidentified"},{"funder_name":"Wellcome Trust","grant_id":"220318","title":"Functional analysis of the downstream mediators of cyclic nucleotide signalling in malaria parasites"},{"funder_name":"Cancer Research UK","grant_id":"","title":null},{"funder_name":"Medical Research Council","grant_id":"","title":null},{"funder_name":"Medical Research Council","grant_id":"","title":null},{"funder_name":"Cancer Research UK","grant_id":"","title":null}],"total_grants":13,"fwci":3.5426,"citation_percentile":0.93069357,"influential_citations":0,"citation_trend":[{"year":2022,"count":1},{"year":2023,"count":4},{"year":2024,"count":5},{"year":2025,"count":4},{"year":2026,"count":2}],"oa_status":"gold","license":"cc-by","oa_locations":[{"url":"https://doi.org/10.1371/journal.ppat.1011449","host_type":"journal"},{"url":"https://doi.org/10.1371/journal.ppat.1011449","host_type":"publisher"},{"url":"https://dx.plos.org/10.1371/journal.ppat.1011449","host_type":"publisher"},{"url":"https://pubmed.ncbi.nlm.nih.gov/37352369","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/10325081","host_type":"repository"},{"url":"https://researchonline.lshtm.ac.uk/view/creators/ipmbjtho.html>;","host_type":"repository"},{"url":"https://doaj.org/article/729265df578440d2850076d88548b0c4","host_type":"repository"},{"url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC10325081/pdf/ppat.1011449.pdf","host_type":"repository"},{"url":"https://researchonline.lshtm.ac.uk/id/eprint/4670733/1/Ramaprasad-etal-2023-A-malaria-parasite-phospholipase-facilitates-efficient-asexual-blood-stage-egress.pdf","host_type":"repository"},{"url":"https://europepmc.org/articles/PMC10325081","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC10325081?pdf=render","host_type":"Europe_PMC"},{"url":"https://doi.org/10.1101/2023.03.13.532312","host_type":""},{"url":"https://dx.doi.org/10.3204/pubdb-2024-00265","host_type":""},{"url":"https://dx.doi.org/10.25418/crick.23675178","host_type":""},{"url":"https://dx.doi.org/10.25418/crick.23675178.v1","host_type":""},{"url":"http://dx.doi.org/10.1371/journal.ppat.1011449","host_type":""},{"url":"https://bib-pubdb1.desy.de/record/601556","host_type":""}],"fields_of_study":["Malaria Research and Control","Trypanosoma species research and implications","Research on Leishmaniasis Studies","03 medical and health sciences","0303 health sciences","Animals","Parasites","Phospholipases","Perforin","Proteomics","Erythrocytes","Plasmodium falciparum","Malaria","Protozoan Proteins","Malaria, Falciparum"],"mesh_terms":["Animals","Erythrocytes","Malaria","Parasites","Phospholipases","Plasmodium falciparum","Protozoan Proteins","Malaria, Falciparum","Proteomics","Perforin"],"keywords":["Biology","Parasite hosting","Effector","Cell biology","Proteome","Plasmodium falciparum","Plasmodium (life cycle)","Malaria","Secretion","Lytic cycle","Microbiology","Virology","Immunology","Biochemistry","Proteomics","Model organisms","Erythrocytes","QH301-705.5","Protozoan Proteins","610","Infectious Disease","Biochemistry &amp; Proteomics","Signalling &amp; Oncogenes","Animals","Parasites","Biology (General)","Malaria, Falciparum","info:eu-repo/classification/ddc/610","Computational &amp; Systems Biology","Chemical Biology &amp; High Throughput","Human Biology &amp; Physiology","Perforin","FOS: Clinical medicine","RC581-607","Tumour Biology","Metabolism","Phospholipases","Immunologic diseases. Allergy","Research Article","Developmental Biology","Structural Biology &amp; Biophysics"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Good health and well-being"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"gen"},{"name":"doi"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-16T19:18:03.660824Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}