Files and links (1)
PDFOpen Access (License Unspecified), Open Access
Dissertation
Characterization of proteins that interact with the amino-termius of the Plasmodium merozoite surface protein 1 (MSP-1)
Doctor of Philosophy (Ph.D.), Drexel University
Apr 2003
DOI:
https://doi.org/10.17918/00008044
Abstract
Merozoite surface protein 1 (MSP-1) is a large molecular weight protein expressed on the surface of the malaria merozoite in a non-covalent complex with other protein molecules. MSP-1 undergoes a series of proteolytic processing events but a precise biological role for the various proteolytic fragments of MSP-1 or for the additional proteins present in the complex is not known. Through the use of the yeast-two hybrid system, we have isolated genes encoding proteins that interact with a region of the amino terminal proteolytic fragment of MSP-1 from the mouse parasite Plasmodium yoelii. This analysis has led to the isolation of two sequence-related molecules, one of which is the P. yoelii homologue of MSP-7 originally described in Plasmodium falciparum. In P. yoelii we have designated these sequences PyMSP-7 and PyMSRP-2. Immunofluorescence studies co-localize these proteins with PyMSP-1 and each other to the surface of late stage P. yoelii 17XL parasites. Immunization with PyMSRP-2, but not PyMSP-7, can protect mice against P. yoelii 17XL lethal challenge even though RT-PCR data suggests there is 2 fold more message present for PyMSP-7 during infection. Blast analysis of the P. falciparum database has revealed that there are 6 related protein molecules present in this species encoded near each other on chromosome 13 and 3 related protein molecules in P. berghei. In P. falciparum , we have designated these molecules MSP-7 and MSRP 2-5. Analysis of the P. yoelii and P. berghei databases indicates a similar chromosomal organization for the genes in the mouse parasite species. The three P. falciparum sequences with the highest degree of homology to the P. yoelii sequences isolated in the two-hybrid screen have been characterized at the molecular level (MSRP 1-3). Expression analysis indicated that the mRNAs are expressed at varying levels in the different asexual stages. Immunofluorescence studies co-localized the expression of the MSRP molecules and the amino-terminal portion of MSP-1 to the surface of trophozoites and schizonts. In vitro binding experiments confirm the interaction between MSRP-1, MSRP-2, and the amino-terminal region of P. falciparum MSP-1.
Metrics
26 File views/ downloads
9 Record Views
Details
- Title
- Characterization of proteins that interact with the amino-termius of the Plasmodium merozoite surface protein 1 (MSP-1)
- Creators
- Kerrianne Mello
- Contributors
- Lawrence W. Bergman (Advisor) - Drexel University, Drexel University (1970-)
- Awarding Institution
- Drexel University
- Degree Awarded
- Doctor of Philosophy (Ph.D.)
- Publisher
- Drexel University; Philadelphia, Pennsylvania
- Number of pages
- x, 136 pages
- Resource Type
- Dissertation
- Language
- English
- Academic Unit
- College of Medicine; Drexel University
- Other Identifier
- 991021889115604721