Research Interests
Antibodies can bind proteins via the Fab and Fc regions. The Fc interacts with receptors on the cells of the immune system causing effector responses such as phagocytosis and complement mediating lysis, however, pathogens have also developed a way to interact with human antibodies through regions on the Fc. We are currently trying to understand the mechanism underlying the binding of Plasmodium falciparum infected erythrocytes to IgM. The Cμ4 domain of multimeric IgM has been shown to bind to the C-terminal Duffy Binding Like (DBL) domains of Plasmodium falciparum Erythrocyte Membrane Protein 1 (PfEMP1) expressed by CSA-binding and rosetting strains of Plasmodium falciparum. CSA-binding has been linked to pregnancy associated malaria and rosetting (the binding of infected to uninfected erythrocytes) has been shown to correlate with many clinical manifestations of severe malaria in children living in sub-Saharan Africa. The binding of IgM has been termed as “non-immune” because its interaction with PfEMP1 occurs outside the antigen binding site. Furthermore, we have shown that laboratory adapted strains and field isolates of Plasmodium falciparum that bind non-immune IgM have the tendency to be recognised by specific antibodies raised against heterologous parasite strains suggesting cross-reactivity between shared adhesion phenotypes. The current aim of the research is to:
- Further understand the nature of cross-reactive and variant specific antibodies to PfEMP1.
- Understand why some strains of P. falciparum bind to IgM and how this is related to severe malaria.
- Optimise DBL protein expression for vaccine development.
CV
2008-present
- Postdoc at the University of Edinburgh
2004-2008
- PhD in Genetics at the University of Nottingham
2000-2004
- BSc in Medical Biochemistry (1st Class Hons) at the University of Leicester
