ArticleThe Biochemical journal2013
Specific phosphorylation of the PfRh2b invasion ligand of Plasmodium falciparum.
Article in The Biochemical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 14 citations in OpenAlex.
- N-terminal phosphorylation regulates the activity of glycogen synthase kinase 3 from Plasmodium falciparum.The Biochemical journal · 2022Article
- The catalytic subunit of Plasmodium falciparum casein kinase 2 is essential for gametocytogenesis.Communications biology · 2021Article
- Article
- The Molecular Basis of Erythrocyte Invasion by Malaria Parasites.Cell host & microbe · 2017Review
- Hierarchical phosphorylation of apical membrane antigen 1 is required for efficient red blood cell invasion by malaria parasites.Scientific reports · 2016Article
- Plasmodium vivax Reticulocyte Binding Proteins Are Key Targets of Naturally Acquired Immunity in Young Papua New Guinean Children.PLoS neglected tropical diseases · 2016Article
- The mechanics of malaria parasite invasion of the human erythrocyte - towards a reassessment of the host cell contribution.Cellular microbiology · 2016Review
- Quantitative phospho-proteomics reveals the Plasmodium merozoite triggers pre-invasion host kinase modification of the red cell cytoskeleton.Scientific reports · 2016Article
- The Binding of Plasmodium falciparum Adhesins and Erythrocyte Invasion Proteins to Aldolase Is Enhanced by Phosphorylation.PloS one · 2016Article
- Plasmodium falciparum Adhesins Play an Essential Role in Signalling and Activation of Invasion into Human Erythrocytes.PLoS pathogens · 2015Article
- Parasite Calcineurin Regulates Host Cell Recognition and Attachment by Apicomplexans.Cell host & microbe · 2015Article
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
Red blood cell invasion by the malaria parasite Plasmodium falciparum relies on a complex protein network that uses low and high affinity receptor-ligand interactions. Signal transduction through the action of specific kinases is a control mechanism for the orchestration of this process. In the present study we report on the phosphorylation of the CPD (cytoplasmic domain) of P. falciparum Rh2b (reticulocyte homologue protein 2b). First, we identified Ser3233 as the sole phospho-acceptor site in the CPD for in vitro phosphorylation by parasite extract. We provide several lines of evidence that this phosphorylation is mediated by PfCK2 (P. falciparum casein kinase 2): phosphorylation is cAMP independent, utilizes ATP as well as GTP as phosphate donors, is inhibited by heparin and tetrabromocinnamic acid, and is mediated by purified PfCK2. We raised a phospho-specific antibody and showed that Ser3233 phosphorylation occurs in the parasite prior to host cell egress. We analysed the spatiotemporal aspects of this phosphorylation using immunoprecipitated endogenous Rh2b and minigenes expressing the CPD either at the plasma or rhoptry membrane. Phosphorylation of Rh2b is not spatially restricted to either the plasma or rhoptry membrane and most probably occurs before Rh2b is translocated from the rhoptry neck to the plasma membrane.
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Registered trials
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