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@ARTICLE{Ramaprasad:601556,
      author       = {Ramaprasad, Abhinay and Burda, Paul-Christian and Koussis,
                      Konstantinos and Thomas, James A. and Pietsch, Emma and
                      Calvani, Enrica and Howell, Steven A. and MacRae, James I.
                      and Snijders, Ambrosius P. and Gilberger, Tim-Wolf and
                      Blackman, Michael J.},
      title        = {{A} malaria parasite phospholipase facilitates efficient
                      asexual blood stage egress},
      journal      = {PLoS pathogens},
      volume       = {19},
      number       = {6},
      issn         = {1553-7366},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {PUBDB-2024-00265},
      pages        = {e1011449},
      year         = {2023},
      abstract     = {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 Plasmodium falciparum 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.},
      cin          = {CSSB-BNITM-TG},
      ddc          = {610},
      cid          = {I:(DE-H253)CSSB-BNITM-TG-20210520},
      pnm          = {899 - ohne Topic (POF4-899) / MalariaEgress - Role of
                      perforin-like proteins and phospholipases in malaria
                      parasite egress (751865) / DFG project G:(GEPRIS)414222880 -
                      Funktionelle Charakterisierung der Phospholipasen im
                      Malariaerreger Plasmodium falciparum (414222880)},
      pid          = {G:(DE-HGF)POF4-899 / G:(EU-Grant)751865 /
                      G:(GEPRIS)414222880},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:37352369},
      UT           = {WOS:001016234800001},
      doi          = {10.1371/journal.ppat.1011449},
      url          = {https://bib-pubdb1.desy.de/record/601556},
}