Journal
SCIENCE
Volume 358, Issue 6362, Pages 522-+Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aaf8675
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Funding
- Nederlandse Organisatie voor Wetenschaopelijk Onderzoek (NWO) [175.010.2007.012]
- Carigest SA
- Swiss National Foundation [156825, 310030B_166678, 310030_159519, BSSGI0_155852]
- SystemsX.ch [51TRPO_151032]
- Academy of Finland [257537, 292718]
- European Research Council under European Union's Horizon 2020 Research and Innovation program [695596]
- Francis Crick Institute
- Wellcome Institutional Strategic Support Fund (ISSF2)
- The Francis Crick Institute [10043] Funding Source: researchfish
- Swiss National Science Foundation (SNF) [310030_159519, 310030B_166678, BSSGI0_155852] Funding Source: Swiss National Science Foundation (SNF)
- Academy of Finland (AKA) [292718, 257537, 257537, 292718] Funding Source: Academy of Finland (AKA)
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Regulated exocytosis by secretory organelles is important for malaria parasite invasion and egress. Many parasite effector proteins, including perforins, adhesins, and proteases, are extensively proteolytically processed both pre-and postexocytosis. Here we report the multistage antiplasmodial activity of the aspartic protease inhibitor hydroxyl-ethyl-amine-based scaffold compound 49c. This scaffold inhibits the preexocytosis processing of several secreted rhoptry and microneme proteins by targeting the corresponding maturases plasmepsins IX (PMIX) and X (PMX), respectively. Conditional excision of PMIX revealed its crucial role in invasion, and recombinantly active PMIX and PMX cleave egress and invasion factors in a 49c-sensitive manner.
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