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Related Experiment Videos

Acylation-dependent protein export in Leishmania.

P W Denny1, S Gokool, D G Russell

  • 1Wellcome Trust Laboratories for Molecular Parasitology, Department of Biochemistry, Imperial College of Science, Technology and Medicine, London SW7 2AZ, United Kingdom.

The Journal of Biological Chemistry
|February 7, 2001
PubMed
Summary
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Leishmania surface proteins are transported via a novel non-classical pathway. N-myristoylation and palmitoylation direct hydrophilic acylated surface proteins (HASPs) to the cell surface, even in mammalian cells.

Area of Science:

  • Cell Biology
  • Parasitology
  • Protein Trafficking

Background:

  • The protozoan parasite Leishmania surface is rich in glycosylphosphatidylinositol-anchored glycoconjugates and proteins.
  • Hydrophilic acylated surface proteins (HASPs) are found on the extracellular face of the plasma membrane in infective Leishmania stages.
  • HASPs lack typical signal sequences for secretion or membrane anchoring, suggesting unique transport mechanisms.

Purpose of the Study:

  • To investigate the transport and localization mechanisms of Hydrophilic Acylated Surface Proteins (HASPs) in Leishmania.
  • To identify the structural elements responsible for HASP localization to the cell surface.
  • To determine if the HASP export signal is recognized by higher eukaryotic export machinery.

Main Methods:

Related Experiment Videos

  • N-terminal domain analysis of HASPB to identify localization signals.
  • Site-directed mutagenesis of predicted acylation residues in HASPB.
  • Fusion of the HASPB N-terminal domain with Aequorea victoria green fluorescent protein (GFP) for cell surface targeting studies.
  • Expression of HASPB in transfected mammalian cells to assess cross-species export signal recognition.

    • Main Results:

    • The N-terminal domain of HASPB contains information for dual N-myristoylation and palmitoylation, crucial for plasma membrane localization.
    • The N-terminal 18 amino acids of HASPB are sufficient to direct GFP to the Leishmania cell surface.
    • Mutagenesis confirmed that both myristate and palmitate modifications are essential for correct HASPB trafficking.
    • HASPB was successfully translocated to the extracellular face of the plasma membrane in transfected mammalian cells.

    Conclusions:

    • HASPB represents a novel class of proteins exported via a non-classical pathway dependent on N-myristoylation and palmitoylation.
    • The N-terminal acylation signals of HASPB are conserved and recognized by export mechanisms in higher eukaryotes.
    • This study elucidates a unique protein export mechanism in Leishmania with implications for understanding eukaryotic cell surface protein targeting.