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Membrane integration and topology of RIFIN and STEVOR proteins of the Plasmodium falciparum parasite
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.ORCID iD: 0000-0003-0426-3716
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Stockholm University, Science for Life Laboratory (SciLifeLab).
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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Number of Authors: 142019 (English)In: The FEBS Journal, ISSN 1742-464X, E-ISSN 1742-4658Article in journal (Refereed) Epub ahead of print
Abstract [en]

The malarial parasite Plasmodium exports its own proteins to the cell surfaces of red blood cells (RBCs) during infection. Examples of exported proteins include members of the repetitive interspersed family (RIFIN) and subtelomeric variable open reading frame (STEVOR) family of proteins from Plasmodium falciparum. The presence of these parasite-derived proteins on surfaces of infected RBCs triggers the adhesion of infected cells to uninfected cells (rosetting) and to the vascular endothelium potentially obstructing blood flow. While there is a fair amount of information on the localization of these proteins on the cell surfaces of RBCs, less is known about how they can be exported to the membrane and the topologies they can adopt during the process. The first step of export is plausibly the cotranslational insertion of proteins into the endoplasmic reticulum (ER) of the parasite, and here, we investigate the insertion of three RIFIN and two STEVOR proteins into the ER membrane. We employ a well-established experimental system that uses N-linked glycosylation of sites within the protein as a measure to assess the extent of membrane insertion and the topology it assumes when inserted into the ER membrane. Our results indicate that for all the proteins tested, transmembranes (TMs) 1 and 3 integrate into the membrane, so that the protein assumes an overall topology of Ncyt-Ccyt. We also show that the segment predicted to be TM2 for each of the proteins likely does not reside in the membrane, but is translocated to the lumen.

Place, publisher, year, edition, pages
2019.
Keywords [en]
membrane protein topology, N-linked glycosylation, Plasmodium, RIFIN protein, STEVOR protein
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:su:diva-177797DOI: 10.1111/febs.15171ISI: 000504344200001PubMedID: 31821735OAI: oai:DiVA.org:su-177797DiVA, id: diva2:1387385
Available from: 2020-01-21 Created: 2020-01-21 Last updated: 2020-03-17

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Kudva, RenukaMagoulopoulou, AnastasiaLara, PatriciaHessa, Taravon Heijne, GunnarNilsson, IngMarie
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