Novel insights into the biological function of the high molecular weight PY235 rhoptry protein of plasmodium Yoelii

289 p.Malaria is one of the most economically important parasitic diseases in the world and is caused by Plasmodium species. The disease symptoms are due to the parasite's nature of invading and developing within the host erythrocyte. Invasion of malaria parasite in a suitable host cell involves a cascade of receptor-ligand interactions. Rodent malaria Py235 and their homologues in human Plasmodium falciparum play an important role in invasion. However, little is known about the biological function of these proteins except that they bind to erythrocytes.DOCTOR OF PHILOSOPHY (SBS

Superoxide anion inhibits drug-induced tumor cell death

10.1016/S0014-5793(99)01258-2FEBS Letters4593343-348FEBL

Structural Characterization of the Erythrocyte Binding Domain of the Reticulocyte Binding Protein Homologue Family of Plasmodium yoelii ▿ †

Invasion of the host cell by the malaria parasite is a key step for parasite survival and the only stage of its life cycle where the parasite is extracellular, and it is therefore a target for an antimalaria intervention strategy. Multiple members of the reticulocyte binding protein homologues (RH) family are found in all plasmodia and have been shown to bind to host red blood cells directly. In the study described here, we delineated the erythrocyte binding domain (EBD) of one member of the RH family, termed Py235, from Plasmodium yoelii. Moreover, we have obtained the low-resolution structure of the EBD using small-angle X-ray scattering. Comparison of the EDB structure to other characterized Plasmodium receptor binding domains suggests that there may be an overall structural conservation. These findings may help in developing new approaches to target receptor ligand interactions mediated by parasite proteins