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Host–parasite interaction: multiple sites in the Plasmodium vivax tryptophan‐rich antigen Pv TRA g38 interact with the erythrocyte receptor band 3
Author(s) -
Alam Mohd S.,
Rathore Sumit,
Tyagi Rupesh K.,
Sharma Yagya D.
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12053
Subject(s) - plasmodium vivax , parasite hosting , plasmodium falciparum , tryptophan , antigen , biology , receptor , plasmodium (life cycle) , malaria , amino acid , microbiology and biotechnology , virology , biochemistry , immunology , world wide web , computer science
Tryptophan‐rich antigens of malarial parasites interact with host molecules and play an important role in parasite survival. Merozoite expressed Plasmodium vivax tryptophan‐rich antigen Pv TRA g38 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 receptor‐ligand binding mechanisms remain unknown. In the present study, using synthetic mutated peptides of Pv TRA g38, 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.