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© Thierry Blisnick & Philippe Bastin, Institut Pasteur
Bloodstream Trypanosoma brucei cell
Publication : Molecular and biochemical parasitology

Molecular characterization of the heat shock protein 90 gene of the human malaria parasite Plasmodium falciparum

Team: Trypanosome Cell Biology
Member: Serge Bonnefoy
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Molecular and biochemical parasitology - 01 Sep 1994

Bonnefoy S, Attal G, Langsley G, Tekaia F, Mercereau-Puijalon O

Link to Pubmed [PMID] – 7838176

Mol. Biochem. Parasitol. 1994 Sep;67(1):157-70

We report here the nucleotide sequence of hsp90 (heat shock protein 90) of Plasmodium falciparum. Computer analysis of the deduced protein sequence revealed an unusually large region of charged amino acids when compared to hsp90 from other species. This region shows striking homology to the calcium binding domain of calreticulin, the major calcium binding protein of endoplasmic reticulum. Phylogenetic tree analysis indicates that P. falciparum hsp90 is more closely related to hsp90 from plants than to hsp90 from vertebrates or other parasites. The malaria hsp90 is an ATP binding protein encoded by a single gene constitutively expressed in both asexual (trophozoite) and sexual (gametocyte) stage parasites. The hsp90 protein is homologous to a previously identified 90-kDa antigen strongly recognised by both sera from vaccinated monkeys and monoclonal antibody XIV/7.