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Identification of Plasmodium falciparum MSP‐1 peptides able to bind to human red blood cells
Author(s) -
URQUIZA MAURICIO,
RODRIGUEZ LUIS E.,
SUAREZ JORGE E.,
GUZMÁN FANNY,
OCAMPO MARISOL,
CURTIDOR HERNANDO,
SEGURA CESAR,
TRUJILLO ESPERANZA,
PATARROYO MANUEL E.
Publication year - 1996
Publication title -
parasite immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.795
H-Index - 75
eISSN - 1365-3024
pISSN - 0141-9838
DOI - 10.1046/j.1365-3024.1996.d01-15.x
Subject(s) - plasmodium falciparum , biology , peptide , red blood cell , biochemistry , peptide sequence , sialic acid , amino acid , receptor , microbiology and biotechnology , malaria , immunology , gene
To determine amino acid sequences of the Plasmodium falciparum MSP‐1 protein that interact with red blood cell membranes in a specific receptor‐ligand interaction, 78 sequential peptides, 20 amino acids long and spanning the entire length of the molecule, were synthesized and analysed with a specific binding assay developed for this purpose. Results show that peptides based on conserved and dimorphic regions of MSP‐1, interact with human red blood cells (RBCs). This interaction occurs predominantly with peptides contained within the MSP‐1 proteolytic fragments of 83 kDa, 38 kDa, 33 kDa and 19 kDa. Affinity constants of these peptides were between 140 and 250 nM. Peptide‐RBC binding post enzyme treatment showed that the RBC receptors are not sialic acid dependent and appear to be proteic in nature. Some of these peptides inhibited merozoite invasion of RBCs yet did not inhibit intra‐erthrocytic development. These peptides, in conjunction with those from other merozoite surface proteins, may be used to rationally design a second generation of synthetic peptide‐based malaria vaccines.