ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2016
Plasmodium actin is incompletely folded by heterologous protein-folding machinery and likely requires the native Plasmodium chaperonin complex to enter a mature functional state.
Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 21 citations in OpenAlex.
- The malaria parasite chaperonin containing TCP-1 (CCT) complex: Data integration with other CCT proteomes.Frontiers in molecular biosciences · 2022Article
- The Impact of Nutritional Supplementation During Pregnancy on the Incidence of Gestational Diabetes and Glycaemia Control.Frontiers in nutrition · 2022Review
- TCP1γ Subunit Is Indispensable for Growth and Infectivity of Leishmania donovani.Antimicrobial agents and chemotherapy · 2020Article
- A Biosynthetic Platform for Antimalarial Drug Discovery.Antimicrobial agents and chemotherapy · 2020Article
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- Partners in Mischief: Functional Networks of Heat Shock Proteins ofBiomolecules · 2019Review
- Knockdown ofFrontiers in microbiology · 2019Article
- The substrate specificity of eukaryotic cytosolic chaperonin CCT.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- Characterization of a protozoan Phosducin-like protein-3 (PhLP-3) reveals conserved redox activity.PloS one · 2018Article
- Reconstitution of the core of the malaria parasite glideosome with recombinantThe Journal of biological chemistry · 2017Article
- Apicomplexan actin polymerization depends on nucleation.Scientific reports · 2017Article
- The Molecular Basis of Erythrocyte Invasion by Malaria Parasites.Cell host & microbe · 2017Review
- The chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosol.Cellular microbiology · 2017Article
- Article
- Surface attachment, promoted by the actomyosin system of Toxoplasma gondii is important for efficient gliding motility and invasion.BMC biology · 2017Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Actin filament turnover underpins several processes in the life cycle of the malaria parasite, Plasmodium falciparum. Polymerization and depolymerization are especially important for gliding motility, a substrate-dependent form of cell movement that underpins the protozoan parasite's ability to disseminate and invade host cells. To date, given difficulties in extraction of native actins directly from parasites, much of our biochemical understanding of malarial actin has instead relied on recombinant protein extracted and purified from heterologous protein expression systems. Here, using in vitro transcription-translation methodologies and quantitative protein-binding assays, we explored the folding state of heterologously expressed P. falciparum actin 1 (PfACTI) with the aim of assessing the reliability of current recombinant-protein-based data. We demonstrate that PfACTI, when expressed in non-native systems, is capable of binding to and release from bacterial, yeast, and mammalian chaperonin complexes but appears to be incompletely folded. Characterization of the native Plasmodium folding machinery in silico, the chaperonin containing t-complex protein-1 complex, highlights key divergences between the different chaperonin systems that likely underpins this incomplete folded state. These results highlight the importance of characterizing actin's folded state and raise concerns about the interpretation of actin polymerization kinetics based solely on protein derived from heterologous expression systems.
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