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Related Experiment Videos

The Plasmodium selenoproteome.

Alexey V Lobanov1, Cesar Delgado, Stefan Rahlfs

  • 1Department of Biochemistry, University of Nebraska, Lincoln, NE 68588, USA.

Nucleic Acids Research
|January 24, 2006
PubMed
Summary
This summary is machine-generated.

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Parasitic Apicomplexa, including Plasmodium, utilize the 21st amino acid, selenocysteine (Sec). Researchers identified novel Plasmodium selenoprotein genes and functional SECIS elements, suggesting new antimalarial drug targets.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Parasitology

Background:

  • Selenocysteine (Sec) is the 21st amino acid, incorporated via a specific recoding mechanism.
  • While present in animals and algae, Sec utilization in other eukaryotes like Apicomplexa parasites was largely uncharacterized.
  • Previous studies indicated Sec's presence in some Apicomplexa, but specific selenoproteins remained unknown.

Purpose of the Study:

  • To investigate the presence and function of Sec insertion machinery and selenoproteins in Apicomplexa parasites.
  • To identify novel selenoprotein genes and selenocysteine insertion sequence (SECIS) elements in Plasmodium species.
  • To assess the functional conservation of Plasmodium SECIS elements and explore potential therapeutic strategies.

Main Methods:

Related Experiment Videos

  • Bioinformatic analysis to identify selenocysteine insertion sequence (SECIS) elements and potential selenoprotein genes.
  • Comparative genomics to assess the conservation of identified genes and elements across Plasmodia and other species.
  • In vitro expression studies in mammalian cells to validate the functionality of Plasmodium SECIS elements.

    • Main Results:

    • Plasmodium and Toxoplasma utilize Sec, while Cryptosporidium does not.
    • Four novel Plasmodium falciparum selenoprotein genes were identified, distinct from known eukaryotic selenoproteins.
    • Two Plasmodium SECIS elements were confirmed to be functional in supporting Sec insertion in mammalian cells.
    • Identified selenoproteins were conserved within Plasmodia but lacked homologs in other organisms.

    Conclusions:

    • Apicomplexa parasites, particularly Plasmodium, possess a unique selenoprotein system involving functional SECIS elements.
    • The identified Plasmodium selenoproteins represent novel targets for drug development.
    • The conservation of Sec insertion machinery highlights potential vulnerabilities in these parasites exploitable for therapeutic intervention.