Structural studies of Immune Mapped Protein 1 (IMP1) homologues in apicomplexan parasites
File(s)
Author(s)
Benjamin, Stefi Victoria
Type
Thesis
Abstract
Apicomplexan parasites are responsible for causing a number of diseases in humans and animals. Toxoplasma gondii is known to cause toxoplasmosis in humans, Eimeria tenella is known to cause coccidiosis in chickens and Plasmodium falciparum is known to cause malaria in humans. These parasites place a huge burden on global health and on the global economy. Current methods of treatment are losing effectiveness, raising the need for new ways to combat these diseases. Identifying vaccine candidates against apicomplexan parasites has been the focus of recent research. Immune Mapped Protein 1 (IMP1) is a novel antigenic protein which was first identified in Eimeria maxima. Recent research has shown that immunisation with IMP1 raises immunity against the parasite in a species specific manner. However, the structure and function of IMP1 is not known.
Here we report the structure of the IMP homologue from Plasmodium falciparum (PfIMP2) solved using solution state Nuclear Magnetic Resonance (NMR). The structure of PfIMP2 has revealed that IMP homologues have a conserved C-terminal IMP domain. Recent research has also revealed that the IMP domain is the immune-dominant region in the IMP homologues. We also report that there are two classes of IMP homologues within apicomplexans. This redundancy of the protein within the parasites suggests that IMP homologues play an important role within the parasite. In vitro experiments performed to gain some insight on the functional role played by IMP proteins within the parasites are also reported. Although the function of the IMP homologues is yet to be deduced, the immunogenic nature of these homologues makes them interesting candidates to study.
Here we report the structure of the IMP homologue from Plasmodium falciparum (PfIMP2) solved using solution state Nuclear Magnetic Resonance (NMR). The structure of PfIMP2 has revealed that IMP homologues have a conserved C-terminal IMP domain. Recent research has also revealed that the IMP domain is the immune-dominant region in the IMP homologues. We also report that there are two classes of IMP homologues within apicomplexans. This redundancy of the protein within the parasites suggests that IMP homologues play an important role within the parasite. In vitro experiments performed to gain some insight on the functional role played by IMP proteins within the parasites are also reported. Although the function of the IMP homologues is yet to be deduced, the immunogenic nature of these homologues makes them interesting candidates to study.
Version
Open Access
Date Issued
2016-09
Date Awarded
2017-01
Copyright Statement
Attribution NoDerivatives 4.0 International Licence (CC BY-ND)
Advisor
Matthews, Steve J
Publisher Department
Life Sciences
Publisher Institution
Imperial College London
Qualification Level
Doctoral
Qualification Name
Doctor of Philosophy (PhD)