ArticleMolecular and biochemical parasitology2014
A conserved domain targets exported PHISTb family proteins to the periphery of Plasmodium infected erythrocytes.
Article in Molecular and biochemical parasitology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 49 citations in OpenAlex.
- Molecular Markers for Sensitive Detection ofThe American journal of tropical medicine and hygiene · 2017Trial
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- PlasmoFAB: a benchmark to foster machine learning for Plasmodium falciparum protein antigen candidate prediction.Bioinformatics (Oxford, England) · 2023Article
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- Antiparasitic Effects of Sulfated Polysaccharides from Marine Hydrobionts.Marine drugs · 2021Review
- In silico characterisation of putative Plasmodium falciparum vaccine candidates in African malaria populations.Scientific reports · 2021Article
- Characterisation of complexes formed by parasite proteins exported into the host cell compartment of Plasmodium falciparum infected red blood cells.Cellular microbiology · 2021Article
- The Role of Malaria Parasite Heat Shock Proteins in Protein Trafficking and Remodelling of Red Blood Cells.Advances in experimental medicine and biology · 2021Review
- Investigating a Plasmodium falciparum erythrocyte invasion phenotype switch at the whole transcriptome level.Scientific reports · 2020Article
- Characterization of sulfated polysaccharide activity against virulentF1000Research · 2020Article
- Interaction Analysis of aFrontiers in microbiology · 2020Article
- Host Cytoskeleton Remodeling throughout the Blood Stages of Plasmodium falciparum.Microbiology and molecular biology reviews : MMBR · 2019Review
- Plasmodium helical interspersed subtelomeric family-an enigmatic piece of the Plasmodium biology puzzle.Parasitology research · 2019Review
- Naturally acquired immunity against immatureScience translational medicine · 2019Article
- Plasmodium genomics: an approach for learning about and ending human malaria.Parasitology research · 2019Review
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
During blood-stage infection, malaria parasites export numerous proteins to the host erythrocyte. The Poly-Helical Interspersed Sub-Telomeric (PHIST) proteins are an exported family that share a common 'PRESAN' domain, and include numerous members in Plasmodium falciparum, Plasmodium vivax and Plasmodium knowlesi. In P. falciparum, PHIST proteins have been implicated in protein trafficking and intercellular communication. A number of PHIST proteins are essential for parasite survival. Here, we identify nine members of the PHISTb sub-class of PHIST proteins, including one protein known to be essential for parasite survival, that localise to the erythrocyte periphery. These proteins have solubility characteristics consistent with their association with the erythrocyte cytoskeleton. Together, an extended PRESAN domain, comprising the PRESAN domain and preceding sequence, form a novel targeting-domain that is sufficient to localise a protein to the erythrocyte periphery. We validate the role of this domain in RESA, thus identifying a cytoskeleton-binding domain in RESA that functions independently of its known spectrin-binding domain. Our data suggest that some PHISTb proteins may act as cross-linkers of the erythrocyte cytoskeleton. We also show for the first time that peripherally-localised PHISTb proteins are encoded in genomes of P. knowlesi and vivax indicating a conserved role for the extended PRESAN domain of these proteins in targeting to the erythrocyte periphery.
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