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primary topic: The P. vivax merozoite surface protein 1 (MSP-1): Development of a recombinant protein production process and structural characterisation of MSP-1

The P. vivax merozoite surface protein 1 (MSP-1): Development of a recombinant protein production process and structural characterisation of MSP-1
type: Article
abstract: Malaria in humans is most often caused by either Plasmodium falciparum or P. vivax. Research efforts have mostly focused on P. falciparum, despite P. vivax being the most widespread Plasmodium species. This parasite species differs from P. falciparum in some key aspects like its ability to form dormant liver forms, an early appearance of gametocytes in the blood stream and its strict tropism to reticulocytes. Although P. vivax and P. falciparum invade different developmental stages of red blood cells, both express a highly abundant protein on the surface of their merozoites, the merozoite surface protein 1 (MSP-1). Initially expressed as a precursor protein, MSP-1 undergoes proteolytic processing and is cleaved into four processing fragments called p83, p30, p38 and p42. These fragments remain non-covalently associated and are attached to the surface of the merozoite via a GPI anchor at the C-terminal fragment p42. MSP-1 is considered a promising vaccine candidate and P. falciparum MSP-1D is currently tested as a vaccine in a clinical trial. However, no similar vaccine was developed for P. vivax yet. The establishment of a protein production process for P. vivax MSP-1 (PvMSP-1) was an essential part of this study. Two different methods were developed, which both use individually expressed fusion proteins to assemble the full length MSP-1 protein. One fusion protein consists of the fragments p83 and p30, the other includes p38 and p42. In the first approach, the two halves are refolded together and purified by ion exchange chromatography and size exclusion chromatography. This protocol was also applied to produce P. berghei MSP-1 and test whether the assembly of a hybrid protein consisting of one P. falciparum half and one P. vivax half is possible. In the second approach contaminants are first removed from the individual fusion proteins by high resolution ion exchange chromatography before reconstitution of MSP-1. Both techniques result in a pure MSP-1 preparation, …
date: 2018
author list: authors
type: EPrint
type: DoctoralThesisEPrint
is part of: repository
has document: The P. vivax merozoite surface protein 1 (MSP-1): Development of a recombinant protein production process and structural characterisation of MSP-1 (PDF)
has document: The P. vivax merozoite surface protein 1 (MSP-1): Development of a recombinant protein production process and structural characterisation of MSP-1 (Other)
subject: 570 Biowissenschaften, Biologie

The P. vivax merozoite surface protein 1 (MSP-1): Development of a recombinant protein production process and structural characterisation of MSP-1 (PDF)
type: Document
has file: Thesis_final.pdf
has part: Thesis_final.pdf

Tanja Marzluf
type: Person
given name: Tanja
family name: Marzluf

The P. vivax merozoite surface protein 1 (MSP-1): Development of a recombinant protein production process and structural characterisation of MSP-1 (Other)
type: Document
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primary topic: The P. vivax merozoite surface protein 1 (MSP-1): Development of a recombinant protein production process and structural characterisation of MSP-1

570 Biowissenschaften, Biologie
type: Concept
preferred label: 570 Life sciences @en