Receptor specific binding regions of Plasmodium vivax tryptophan rich antigens and parasite growth inhibition activity of PvTRAg35.2

Abstract

Plasmodium tryptophan rich proteins play important role in host-parasite interaction. Earlier, we have described that one of the merozoite expressed Plasmodium vivax tryptophan-rich antigen PvTRAg35.2 binds to the host erythrocytes, have conserved sequences in parasite population, and generates humoral as well as cellular immune responses in humans during this parasitic infection. Here, we show that PvTRAg35.2 interferes with the parasite growth in a heterologous Plasmodium falciparum culture system. This probably suggests the recognition of the common erythrocyte receptor(s) by certain merozoite ligands of these two parasite species. We have mapped the erythrocyte binding activity of PvTRAg35.2 to its two different regions positioned at amino acid residues 155-190 and 263-283. Binding of these peptide domains to the erythrocytes was inhibited by anti-PvTRAg35.2 antibodies either raised in rabbit or produced by the P. vivax patients. The cross-competition between peptides of PvTRAg35.2 and PvTRAg33.5 or PvTRAg38 during erythrocyte binding assay suggested sharing of host cell receptors by these PvTRAgs. Further studies on these receptor-ligand interactions may lead to the development of therapeutic agents for P. vivax malaria.

Keywords: Erythrocyte receptors; Peptide mapping; Protein-protein interactions; Red cell invasion; Vivax malaria.