Functional insight the role of plasmodium falciparum reticulocyte blinding like protein homologues : RH2B and RH5 during merozoites invasion
The process of Plasmodium merozoites invasion is a complex multi-step process. In understanding the mechanisms leading to successful merozoites invasion, a group of proteins known as Plasmodium falciparum erythrocyte binding ligands as well as Plasmodium falciparum reticulocyte binding - like pro...
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| Format: | Theses and Dissertations |
| Language: | English |
| Published: |
2016
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| Online Access: | https://hdl.handle.net/10356/69419 |
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| Institution: | Nanyang Technological University |
| Language: | English |
| Summary: | The process of Plasmodium merozoites invasion is a complex multi-step process. In
understanding the mechanisms leading to successful merozoites invasion, a group of proteins
known as Plasmodium falciparum erythrocyte binding ligands as well as Plasmodium
falciparum reticulocyte binding - like protein homologues (PfRH) have been shown to be
necessary. These proteins have been shown to play a role in sensing the erythrocyte. Of the
PfRH family, it is becoming clearer of their ability to affect the secretion of microneme
proteins which are necessary to establish the tight junction. In this presentation, the role of
PfRH2b during merozoite invasion has studied. Like PfRH1, PfRH2b has been shown to
regulate the increase in merozoites Ca2+. This, we have shown to affect the release of
EBA175 to the erythrocyte surface. Our data also points to the fact that the secretion of
EBA175 to the surface is more prominent when the merozoites are engaged with the RBCs.
Furthermore we have provided the detailed processing events that occur in the PfRH2b
protein before and during merozoites invasion.
Functional insight on RH5-Basigin interaction has been provided. In this, we have shown
RH5 to be involved in invasion independent of EBA175 surface expression but functions
before tight junction formation. We have provided evidence of RH5-Basigin interaction
driving Ca2+ in the RBC leading to the remodelling of the RBC cytoskeletal proteins
arrangement. We have confirmed that recombinant RH5 has the ability to induce changes in
the RBC cytoskeleton upon binding. This mechanism we propose facilitates the insertion of
AMA1-RON complex into the RBC membrane leading to tight junction formation. This
knowledge we believe will help in advancing our understanding as well as provide avenue to
explore the mechanisms of merozoites invasion |
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