African Journal of
Biochemistry Research

  • Abbreviation: Afr. J. Biochem. Res.
  • Language: English
  • ISSN: 1996-0778
  • DOI: 10.5897/AJBR
  • Start Year: 2007
  • Published Articles: 425

Full Length Research Paper

The Hsp40-Hsp70 chaperone machinery of Plasmodium falciparum

Eva-Rachele Pesce* and Gregory L. Blatch
Biomedical Biotechnology Research Unit, Department of Biochemistry, Microbiology and Biotechnology, Rhodes University, Grahamstown 6140, South Africa.
Email: [email protected]

  •  Accepted: 04 December 2008
  •  Published: 31 May 2009



Plasmodium falciparum is the protozoan parasite responsible for the most virulent form of malaria. The majority of the asexual stages of its life cycle occur in the human erythrocyte. Since the infected erythrocytes undergo dramatic structural and functional changes upon parasite infection, malaria research has been focusing on investigating the proteins potentially involved in host cell modifications. Molecular chaperones are believed to play an important role in erythrocyte remodelling as many of these proteins are predicted to be exported into the erythrocyte cytoplasm. A family of molecular chaperones that has recently received much attention is the heat shock protein family (Hsps), and in particular members belonging to the 40 and 70 kDa heat shock proteins classes (Hsp40s and Hsp70s). This review summarises the latest in silico and in vivo data available on Pfalciparum Hsp40s and Hsp70s.


Key words: Plasmodium falciparum, malaria, Hsp40s, Hsp70.