Abstract
Plasmodium falciparum has the most adenine (A)- and thymine (T)-rich genome known to date, and 24-30% of the P. falciparum proteome contains asparagine (N) and glutamine (Q) residues. In general, asparagine repeats in proteins increase the propensity for aggregation, especially at elevated temperatures, which occur routinely in P. falciparum parasites during exoerythrocytic and erythrocytic developmental stages in a vertebrate host. The P. falciparum exported chaperone machinery is comprised of an exported PfHsp70-x protein and its co-chaperone PfHsp40-x1 in the host erythrocyte compartment, and PfHsp70-z and its co-chaperones in the parasite cytoplasm have been identified. In vitro assays reveal that these chaperone partners function in refolding of asparagine-rich polypeptides. The identification and chaperoning of exported poly-asparagine-containing proteins, and the biological roles and the protection mechanisms of P. falciparum during febrile conditions by the exported chaperone machinery are discussed.