Konstruktion und Charakterisierung einer Mutante des GPI-Biosyntheseweges von Plasmodium falciparum

Glycosylphosphatidylinositol represents a complex glycolipid which plays an important role as anchoring molecule for cell surface proteins. The biosynthesis of these molecules is a complex process which involves step-by-step transfer of single sugar components to phosphytidylinositol. This work concentrates on dolichol phosphate mannose synthase of Plasmodium falciparum an enzyme which shows its activity in the ER compartment. The known sequences of dolichol phosphate mannose synthases (DPM1) are divided into two groups. To achieve further information about the DPM1-protein of P. falciparum, mutants of this organism were made which show different marker sequences at the DPM1 protein. The sequence analysis of this protein, the fact that a hydrophobic marker sequence seems to interfere with the hydrophilic DPM1-protein and the failing of finding homologous subunits to its human counterpart lead to the conclusion that the parasites protein is unique among the DPM-synthases and could open a new field of antimalarial therapy.