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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>","DOI":"10.1371\/journal.ppat.1011449","type":"journal-article","created":{"date-parts":[[2023,6,24]],"date-time":"2023-06-24T19:29:34Z","timestamp":1687634974000},"page":"e1011449","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":16,"title":["A malaria parasite phospholipase facilitates efficient asexual blood stage 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