Host–parasite interaction: multiple sites in the Plasmodium vivax tryptophan‐rich antigen PvTRAg38 interact with the erythrocyte receptor band 3
Autor: | Rupesh K. Tyagi, Mohd. Shoeb Alam, Yagya D. Sharma, Sumit Rathore |
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Jazyk: | angličtina |
Rok vydání: | 2016 |
Předmět: |
0301 basic medicine
Erythrocytes Plasmodium vivax peptide mapping Molecular Sequence Data Biophysics Antigens Protozoan Biochemistry band 3 ectodomains Host-Parasite Interactions 03 medical and health sciences Antigen Structural Biology Anion Exchange Protein 1 Erythrocyte parasitic diseases Genetics Research Letter Cell Adhesion Parasite hosting Animals Amino Acid Sequence receptor‐ligand interactions Receptor Molecular Biology Peptide sequence Band 3 chemistry.chemical_classification Molecular Basis of Disease biology malaria parasite Cell Biology Alanine scanning biology.organism_classification erythrocyte binding Research Letters Amino acid alanine scanning 030104 developmental biology chemistry biology.protein |
Zdroj: | Febs Letters |
ISSN: | 1873-3468 0014-5793 |
Popis: | 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. |
Databáze: | OpenAIRE |
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