ArticlePloS one2014
Characterization of the small exported Plasmodium falciparum membrane protein SEMP1.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 26 citations in OpenAlex.
- MAHRP2 is required for tether formation and cytoadherence inFrontiers in cellular and infection microbiology · 2026Article
- MAP-X reveals distinct protein complex dynamics across Plasmodium falciparum blood stages.Nature microbiology · 2025Article
- APEX2-based proximity proteomic analysis identifies candidate interactors for Plasmodium falciparum knob-associated histidine-rich protein in infected erythrocytes.Scientific reports · 2024Article
- Article
- Plasmodium falciparum formins are essential for invasion and sexual stage development.Communications biology · 2023Article
- Deletion of the Plasmodium falciparum exported protein PTP7 leads to Maurer's clefts vesiculation, host cell remodeling defects, and loss of surface presentation of EMP1.PLoS pathogens · 2022Article
- Directed evolution in mammalian cells.Nature methods · 2021Review
- Article
- A High-Resolution Map of SBP1 Interactomes in Plasmodium falciparum-infected Erythrocytes.iScience · 2019Article
- Article
- Proteomic analysis of extracellular vesicles from aWellcome open research · 2017Article
- Plasmodium Helical Interspersed Subtelomeric (PHIST) Proteins, at the Center of Host Cell Remodeling.Microbiology and molecular biology reviews : MMBR · 2016Review
- Plasmodium falciparum Plasmodium helical interspersed subtelomeric proteins contribute to cytoadherence and anchor P. falciparum erythrocyte membrane protein 1 to the host cell cytoskeleton.Cellular microbiology · 2016Article
- Plasmodium species: master renovators of their host cells.Nature reviews. Microbiology · 2016Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Survival and virulence of the human malaria parasite Plasmodium falciparum during the blood stage of infection critically depend on extensive host cell refurbishments mediated through export of numerous parasite proteins into the host cell. The parasite-derived membranous structures called Maurer's clefts (MC) play an important role in protein trafficking from the parasite to the red blood cell membrane. However, their specific function has yet to be determined. We identified and characterized a new MC membrane protein, termed small exported membrane protein 1 (SEMP1). Upon invasion it is exported into the RBC cytosol where it inserts into the MCs before it is partly translocated to the RBC membrane. Using conventional and conditional loss-of-function approaches we showed that SEMP1 is not essential for parasite survival, gametocytogenesis, or PfEMP1 export under culture conditions. Co-IP experiments identified several potential interaction partners, including REX1 and other membrane-associated proteins that were confirmed to co-localize with SEMP1 at MCs. Transcriptome analysis further showed that expression of a number of exported parasite proteins was up-regulated in SEMP1-depleted parasites. By using Co-IP and transcriptome analysis for functional characterization of an exported parasite protein we provide a new starting point for further detailed dissection and characterisation of MC-associated protein complexes.
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