Publications by authors named "Jeya Kumar Ramalingam"
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.
View Article and Find Full Text PDFInvasion of the erythrocyte by the invasive form of the malaria parasite, the merozoite, is a complex process involving numerous parasite proteins. The reticulocyte-binding protein homologues (RH) family of merozoite proteins has been previously shown to play an important role in the invasion process. Previously, it has been shown that the RH proteins of Plasmodium yoelii, Py235, play a role as an ATP/ADP sensor.
View Article and Find Full Text PDFArticle Synopsis
- The recognition of host cells by malaria parasites involves a series of receptor-ligand interactions, with ATP from red blood cells playing a crucial role in determining cell suitability for invasion.
- New research has identified a specific region in the reticulocyte-binding protein homologue (RBL) family that binds ATP, known as the nucleotide binding domain 94 (NBD94).
- Binding studies show that ATP has a higher affinity for NBD94 than ADP, and structural changes in the protein upon nucleotide binding suggest a potential role in the invasion process of malaria merozoites.