ArticleMalaria journal2015
A comparative study of the localization and membrane topology of members of the RIFIN, STEVOR and PfMC-2TM protein families in Plasmodium falciparum-infected erythrocytes.
Article in Malaria journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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36 citing papers in PubMed, 65 citations in OpenAlex.
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- Epigenetics of malaria parasite nutrient uptake, but why?Trends in parasitology · 2022Review
- Selective expression of variant surface antigens enables Plasmodium falciparum to evade immune clearance in vivo.Nature communications · 2022Article
- Neutrophils impose strong immune pressure against PfEMP1 variants implicated in cerebral malaria.EMBO reports · 2022Article
- PMRT1, amBio · 2022Article
- Mechanisms for Host Immune Evasion Mediated byFrontiers in immunology · 2022Review
- The Putative Bromodomain Protein PfBDP7 of the Human Malaria ParasiteFrontiers in cell and developmental biology · 2022Article
- Natural Killer Cell Antibody-Dependent Cellular Cytotoxicity (ADCC) Activity Against Plasmodium falciparum-Infected Red Blood Cells.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Characterization of Apicomplexan Amino Acid Transporters (ApiATs) in the Malaria Parasite Plasmodium falciparum.mSphere · 2021Article
- Trafficking and Association ofPathogens (Basel, Switzerland) · 2021Article
- Genome-Wide Scans for GhanaianFrontiers in cellular and infection microbiology · 2021Article
- Structure of theProceedings of the National Academy of Sciences of the United States of America · 2020Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundVariant surface antigens (VSA) exposed on the membrane of Plasmodium falciparum infected erythrocytes mediate immune evasion and are important pathogenicity factors in malaria disease. In addition to the well-studied PfEMP1, the small VSA families RIFIN, STEVOR and PfMC-2TM are assumed to play a role in this process.
methodsThis study presents a detailed comparative characterization of the localization, membrane topology and extraction profile across the life cycle of various members of these protein families employing confocal microscopy, immunoelectron microscopy and immunoblots.
resultsThe presented data reveal a clear association of variants of the RIFIN, STEVOR and PfMC-2TM proteins with the host cell membrane and topological studies indicate that the semi-conserved N-terminal region of RIFINs and some STEVOR proteins is exposed at the erythrocyte surface. At the Maurer's clefts, the semi-conserved N-terminal region as well as the variable stretch of RIFINs appears to point to the lumen away from the erythrocyte cytoplasm. These results challenge the previously proposed two transmembrane topology model for the RIFIN and STEVOR protein families and suggest that only one hydrophobic region spans the membrane. In contrast, PfMC-2TM proteins indeed seem to be anchored by two hydrophobic stretches in the host cell membrane exposing just a few, variable amino acids at the surface of the host cell.
conclusionTogether, the host cell surface exposure and topology of RIFIN and STEVOR proteins suggests members of these protein families may indeed be involved in immune evasion of the infected erythrocyte, whereas members of the PfMC-2TM family seem to bear different functions in parasite biology.
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