Host-parasite interaction: multiple sites in the Plasmodium vivax tryptophan-rich antigen PvTRAg38 interact with the erythrocyte receptor band 3.

Autor: Alam MS; Department of Biotechnology, All India Institute of Medical Sciences, Ansari Nagar, New Delhi, India., Rathore S; Department of Biotechnology, All India Institute of Medical Sciences, Ansari Nagar, New Delhi, India., Tyagi RK; Department of Biotechnology, All India Institute of Medical Sciences, Ansari Nagar, New Delhi, India., Sharma YD; Department of Biotechnology, All India Institute of Medical Sciences, Ansari Nagar, New Delhi, India.
Jazyk: angličtina
Zdroj: FEBS letters [FEBS Lett] 2016 Jan; Vol. 590 (2), pp. 232-41. Date of Electronic Publication: 2016 Jan 23.
DOI: 10.1002/1873-3468.12053
Abstrakt: 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 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 receptor-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.
(© 2016 Federation of European Biochemical Societies.)
Databáze: MEDLINE
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