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Plasmodium falciparum-encoded exported hsp70/hsp40 chaperone/co-chaperone complexes within the host erythrocyte

Simone Külzer1, Sarah Charnaud, Tal Dagan

  • 1Parasitology, Philipps University Marburg, Marburg, Germany.

Cellular Microbiology
|August 29, 2012
PubMed

Insights

Malaria parasites use a novel exported chaperone, PfHsp70-x, to modify host erythrocytes. This parasite protein, along with PfHsp40s, forms complexes in J-dots, impacting virulence factor presentation.

Area of Science:

  • Molecular parasitology
  • Host-pathogen interactions
  • Protein trafficking

Background:

  • Malaria parasites (Plasmodium falciparum) extensively modify mature human erythrocytes.
  • Parasite-encoded heat shock proteins (PfHsp40s) are exported to the erythrocyte and implicated in host cell modification.
  • Hsp40s typically function with Hsp70 chaperones, with human Hsp70 previously assumed as the interaction partner.

Purpose of the Study:

  • To identify and characterize parasite-encoded Hsp70s involved in host erythrocyte modification.
  • To investigate the interaction partners of exported PfHsp40s within the host cell.
  • To elucidate the role of parasite-derived chaperones in malaria pathogenesis.

Main Methods:

  • Identification and characterization of a novel exported parasite Hsp70 (PfHsp70-x).
  • Analysis of PfHsp70-x complex formation with PfHsp40s in structures called J-dots.
  • Investigation of PfHsp70-x association with Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1).

Main Results:

  • A novel parasite-exported Hsp70, PfHsp70-x, was identified and characterized.
  • PfHsp70-x forms complexes with PfHsp40s within the host erythrocyte, specifically in J-dots.
  • PfHsp70-x is closely associated with PfEMP1, a major virulence factor.
  • Hsp70-x is encoded by parasite species that export EMP1, suggesting a role in EMP1 surface presentation.

Conclusions:

  • Parasite-encoded chaperone/co-chaperone complexes (PfHsp70-x/PfHsp40s) exist within the host erythrocyte.
  • These complexes are involved in protein trafficking and modification of the host cell.
  • The host-pathogen interaction is more complex, involving parasite-encoded Hsp70-x in protein transport and virulence factor presentation.

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