Untersuchung der Funktion der N-terminalen Verlängerung von GBP 130 von Plasmodium falciparum
Plasmodium falciparum exportiert Proteine in den Wirtserythrozyt, die die Wirtszelle morphologisch modifizieren. Eine wichtige Konsequenz dieser morphologischen Veränderung der Wirtszelle ist die Eigenschaft der infizierten Zellen an Rezeptoren im Endothel der Blutgefässe zu binden. Diese adhäsiven...
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Table of Contents: The initial stages of the P. falciparum secretory pathway appear to be similar to that in higher eukaryotes, but with some important differences. It has been noted that, although many P. falciparum proteins contain so-called “canonical” signal peptides (with a central hydrophobic region, a hydrophilic N-region and a C-terminal region), a number of secreted proteins contain an unusual N-terminal region prior to the hydrophobic signal peptide (recessed signal peptides). These N-terminal sequences appear to target proteins to the ER, but how exactly this occurs, and the function of the extension remains unknown. For reasons that are currently not well understood, recessed signal sequences are found mostly attached to proteins predicted to be transported to the cytosol of the host erythrocyte. These proteins underlie the pathology of malaria infection, as they confer novel properties to the infected host cell. In this PhD thesis, we aim to dissect such unusual secretory signal peptides, with a view to understanding their function. We shall use several P. falciparum N-terminal regions to this end, including classical signal peptides, as well as proteins containing recessed hydrophobic domains.