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Author Spotlight: Exploring Heat Shock Proteins in Malaria and Tuberculosis Infections
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Structure of the substrate-binding domain of Plasmodium falciparum heat-shock protein 70-x

Julia Schmidt1, Ioannis Vakonakis1

  • 1Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom.

Acta Crystallographica. Section F, Structural Biology Communications
|October 2, 2020
PubMed

Insights

Malaria parasite Plasmodium falciparum exports heat-shock 70 kDa protein x (PfHsp70-x) to aid growth. Its structure reveals similarities to human Hsp70, suggesting potential exploitation of host chaperones.

Area of Science:

  • Parasitology
  • Structural Biology
  • Molecular Medicine

Background:

  • Plasmodium falciparum modifies host erythrocytes by exporting proteins.
  • PfHsp70-x is a key exported protein supporting parasite growth during fever.
  • The ATP-binding domain of PfHsp70-x has druggable epitopes distinct from human Hsp70.

Purpose of the Study:

  • To determine the crystallographic structure of the substrate-binding domain (SBD) of PfHsp70-x.
  • To compare the SBD structure and substrate-binding mechanism with human Hsp70 chaperones.

Main Methods:

  • X-ray crystallography was used to resolve the structure of PfHsp70-x SBD.
  • The structure was determined in complex with a hydrophobic peptide.

Main Results:

  • The crystallographic structure of the PfHsp70-x SBD was determined.
  • The PfHsp70-x SBD shows high similarity to human erythrocytic Hsp70 chaperones.
  • Substrate binding occurs at a conserved interface between β-sandwich and α-helical subdomains.

Conclusions:

  • The substrate-binding domain of PfHsp70-x is structurally conserved with human Hsp70.
  • Plasmodium falciparum may exploit human chaperones for protein trafficking and proteome maintenance within erythrocytes.
Keywords:
PfEMP-1PfHsp70-xPlasmodium falciparumchaperonescomplexescrystallographyerythrocyte remodellingmalaria

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