Basigin interacts with majority of the erythrocyte binding Pvfam ‘a’ family proteins of Plasmodium vivax to assist parasite entry into host cell

Abstract

Abstract Molecular mechanisms of red cell invasion by the Plasmodium vivax parasite remain obscure since information on receptor-ligand interaction is scarce. Our lab had identified Basigin as receptor molecule for one of the important members of Pvfam “a’ family protein i.e., PvTRAg38. Here, we demonstrate by using solid phase binding assay, and Surface Plasmon Resonance that seven out of ten-erythrocyte binding Pvfam ‘a’ family proteins of P. vivax interact with erythrocyte receptor Basigin. This receptor-ligand interaction seems to be important for parasite’s survival since each of these proteins interfered with the parasite growth in a heterologous culture system. Furthermore, a higher parasite growth inhibition rate was achieved with combination of proteins suggesting the significance of multiple parasite ligands interaction with the same erythrocyte receptor during invasion process. These results will be helpful in understanding P. vivax biology and developing the therapeutics for vivax malaria.