Functional analysis of exported Plasmodium falciparum proteins by specific conditional regulation of protein transport

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During its intracellular development the malaria parasite Plasmodium falciparum exports a large number of proteins to the host cell, mature human erythrocytes. Some of these exported proteins mediate numerous essential functions including cytoadherence and evasion of the hosts immune system, that are directly linked to the severe pathology of the disease. However, the function of most exported proteins remains, to date, elusive as most of these proteins lack any known domain structures. In a recent study, we have identified members of the heat shock protein 40 (HSP40) family that is exported to the host cell, and implicated in transport of further parasite-encoded exported proteins. The exact function of this protein within the host cell remains elusive. The aim of this project is the development of a system to enable the functional analysis of exported proteins, using the previously identified HSP40 as a model protein. As many exported proteins are essential for the parasites survival, they are therefore not accessible to traditional gene inactivation and reverse genetic strategies. Studying the function of further exported proteins may allow the assignment of proteins that are important for pathogenesis and survival of the malaria parasite.