Plasmodium falciparum is the causative agent of the most severe form of malaria. This parasite drastically modifies its host cell, the erythrocyte, to create a hospitable environment for its growth and reproduction. In order for these modifications to occur, the parasite secretes proteins into the erythrocyte. While the secretion machinery is still unknown, many secreted proteins have been found to have a hydrophobic signal sequence and a novel host-targeting signal downstream of the hydrophobic sequence. A novel P. falciparum protein has been shown to be secreted from the parasitophorous vacuole, yet it lacks both a hydrophobic signal sequence and a host-targeting signal. It was hypothesized that this protein, Pfl2110c, must interact with other proteins as it migrates into the erythrocyte. Using immunofluorescence assays and co-immunoprecipitation experiments, I found that Pfl2110c interacts with several parasite proteins as well as with the erythrocyte cytoskeleton. Therefore, Pfl2110c was renamed skeleton-binding protein 2 (SBP-2).
| Identifer | oai:union.ndltd.org:vcu.edu/oai:scholarscompass.vcu.edu:etd-2693 |
| Date | 15 April 2009 |
| Creators | Zapata, Monica |
| Publisher | VCU Scholars Compass |
| Source Sets | Virginia Commonwealth University |
| Detected Language | English |
| Type | text |
| Format | application/pdf |
| Source | Theses and Dissertations |
| Rights | © The Author |
Page generated in 0.0015 seconds