Feier Chen

Identification of novel malaria antigens expressed on the surface of red blood cells (RBCs) is essential as potential targets for neutralizing antibodies against cerebral malaria. Little is known about the role of many malaria ligands and their cognate host receptors in cell adhesion pathways. Hundreds of malaria proteins are targeted to specific sites within host RBCs. Plasmodium falciparum glutamate-rich protein (PfGARP) is a recently characterized cell-surface protein in malaria infected RBCs. PfGARP plays a functional role in the adhesion pathway but its molecular mechanism is not known. While investigating the function of PfGARP in cell adhesion, our group recently discovered that the polyclonal antibodies (Abs) raised against PfGARP exerted potent inhibition of parasite growth in vitro. Importantly, the inhibitory activity of Abs was independent of the expression of PfGARP in the malaria parasite. This exciting finding suggests that the neutralizing Abs against PfGARP likely target an unknown protein(s) with potent inhibitory activity against the growth of malaria-infected RBCs. I am currently working to identify the targets of these Abs using phage display cDNA screening technology.