ArticleEukaryotic cell2013
A bacterial phosphatase-like enzyme of the malaria parasite Plasmodium falciparum possesses tyrosine phosphatase activity and is implicated in the regulation of band 3 dynamics during parasite invasion.
Article in Eukaryotic cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 24 citations in OpenAlex.
- Toxoplasma gondii PPM3H regulates the parasite virulence and modulates host immune and inflammatory responses in mice.Veterinary research · 2025Article
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- Deciphering the Role of Protein Phosphatases in Apicomplexa: The Future of Innovative Therapeutics?Microorganisms · 2022Review
- The Cellular and Molecular Interaction Between Erythrocytes andFrontiers in cellular and infection microbiology · 2022Review
- TheFrontiers in cellular and infection microbiology · 2021Article
- Functional Characterization of 17 Protein Serine/Threonine Phosphatases inFrontiers in cell and developmental biology · 2021Article
- Host Cytoskeleton Remodeling throughout the Blood Stages of Plasmodium falciparum.Microbiology and molecular biology reviews : MMBR · 2019Review
- The serine/threonine phosphatases of apicomplexan parasites.Molecular microbiology · 2017Review
- Article
- Mesangial proliferative glomerulonephritis in murine malaria parasite, Plasmodium chabaudi AS, infected NC mice.Clinical and experimental nephrology · 2017Article
- Shelph2, a bacterial-like phosphatase of the malaria parasite Plasmodium falciparum, is dispensable during asexual blood stage.PloS one · 2017Article
- Host-Parasite Interactions in Human Malaria: Clinical Implications of Basic Research.Frontiers in microbiology · 2017Review
- Rhizobiales-like Phosphatase 2 from Arabidopsis thaliana Is a Novel Phospho-tyrosine-specific Phospho-protein Phosphatase (PPP) Family Protein Phosphatase.The Journal of biological chemistry · 2016Article
- Genome wide in silico analysis of Plasmodium falciparum phosphatome.BMC genomics · 2014Article
- Genome-wide functional analysis of Plasmodium protein phosphatases reveals key regulators of parasite development and differentiation.Cell host & microbe · 2014Article
- A flow cytometric assay to quantify invasion of red blood cells by rodent Plasmodium parasites in vivo.Malaria journal · 2014Article
- PhosphoTyrosyl phosphatase activator of Plasmodium falciparum: identification of its residues involved in binding to and activation of PP2A.International journal of molecular sciences · 2014Article
- Homology Modeling and Docking Study ofJournal of pharmacy & bioallied sciencesArticle
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
Abstract
Eukaryotic parasites of the genus Plasmodium cause malaria by invading and developing within host erythrocytes. Here, we demonstrate that PfShelph2, a gene product of Plasmodium falciparum that belongs to the Shewanella-like phosphatase (Shelph) subfamily, selectively hydrolyzes phosphotyrosine, as shown for other previously studied Shelph family members. In the extracellular merozoite stage, PfShelph2 localizes to vesicles that appear to be distinct from those of rhoptry, dense granule, or microneme organelles. During invasion, PfShelph2 is released from these vesicles and exported to the host erythrocyte. In vitro, PfShelph2 shows tyrosine phosphatase activity against the host erythrocyte protein Band 3, which is the most abundant tyrosine-phosphorylated species of the erythrocyte. During P. falciparum invasion, Band 3 undergoes dynamic and rapid clearance from the invasion junction within 1 to 2 s of parasite attachment to the erythrocyte. Release of Pfshelph2 occurs after clearance of Band 3 from the parasite-host cell interface and when the parasite is nearly or completely enclosed in the nascent vacuole. We propose a model in which the phosphatase modifies Band 3 in time to restore its interaction with the cytoskeleton and thus reestablishes the erythrocyte cytoskeletal network at the end of the invasion process.
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