CANCELLED: Identifying host-parasite interactions and subunit vaccine candidates with libraries of recombinant cell-surface and secreted parasite proteins

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This event has been cancelled.

Parasite cell-surface and secreted proteins interact with host receptors to influence the pathology of infections and are constantly exposed to their host’s immune system, making then ideal vaccine targets. However, because these proteins occupy the oxidising extracellular space, they often contain post-translational modifications such as disulphide bonds making them difficult to express recombinantly in their functional conformation. Using mammalian cells as a heterologous expression system, we have developed a generalised approach to produce large libraries of recombinant cell surface and secreted parasite proteins.

Here, I will show how I have compiled two protein libraries for the Plasmodium falciparum merozoite and the schistosomula and adult stages of Schistosoma mansoni, and used them in a variety of contexts. In a first instance, I will describe how host-pathogen protein interaction screens identified the essential interaction between Basigin, expressed on the human red blood cell, and Plasmodium falciparum Rh5, which is now an exciting blood-stage vaccine candidate. Secondly, I will present how a library of cell surface and secreted proteins from Schistosoma mansoni was developed to identify early serological markers of infection in experimentally-controlled challenges of human volunteers and as vaccine candidates in a murine model of schistosomiasis.

Using these libraries of parasite proteins, we are planning on screening a recently-developed library of human immune receptors to identify new host-pathogen interactions involved in immunoregulation.