Author: Alam, Mohd S.; Rathore, Sumit; Tyagi, Rupesh K.; Sharma, Yagya D.
Title: Host–parasite interaction: multiple sites in the Plasmodium vivax tryptophanâ€rich antigen PvTRAg38 interact with the erythrocyte receptor band 3 Cord-id: qf99b2j5 Document date: 2016_1_23
ID: qf99b2j5
Snippet: Tryptophanâ€rich antigens of malarial parasites interact with host molecules and play an important role in parasite survival. Merozoite expressed Plasmodium vivax tryptophanâ€rich antigen PvTRAg38 binds to human erythrocytes and facilitates parasite growth in a heterlologous Plasmodium falciparum culture system. Recently, we identified band 3 in human erythrocytes as one of its receptors, although the receptorâ€ligand binding mechanisms remain unknown. In the present study, using synthetic mu
Document: Tryptophanâ€rich antigens of malarial parasites interact with host molecules and play an important role in parasite survival. Merozoite expressed Plasmodium vivax tryptophanâ€rich antigen PvTRAg38 binds to human erythrocytes and facilitates parasite growth in a heterlologous Plasmodium falciparum culture system. Recently, we identified band 3 in human erythrocytes as one of its receptors, although the receptorâ€ligand binding mechanisms remain unknown. In the present study, using synthetic mutated peptides of PvTRAg38, we show that multiple amino acid residues of its 12 amino acid domain (KWVQWKNDKIRS) at position 197–208 interact with three different ectodomains of band 3 receptor on human erythrocytes. Our findings may help in the design of new therapeutic approaches for malaria.
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