Identification and polymorphism analysis of P. vivax RBP-1 peptides which bind specifically to reticulocytes.

Manuel Alfonso Patarroyo, Mauricio Urquiza, Marisol Ocampo Cifuentes, Viviana Marin-Esteban

Research output: Contribution to journalArticlepeer-review

26 Scopus citations

Abstract

Plasmodium vivax merozoite preferentially invades reticulocytes probably using PvRBP-1 as ligand. One hundred and ninety-five, 15-mer peptides has been synthesised from PvRBP-1 sequence; tested in reticulocyte- or erythrocyte-binding assays. Twenty-five peptides (K(d)=76-380 nM) specifically defined four reticulocyte-binding regions. It has been reported that a highly conserved Region-I recombinant fragment binds specifically to reticulocytes. HABP-critical residues for reticulocyte-binding were highly conserved in 20 Colombian P. vivax clinical isolates, suggesting an important biological function. There were six overlapping reticulocyte-binding sites for these peptides according to enzyme sensitivity and mutual competition-binding assays; located on 26- and 41-kDa reticulocyte membrane surface proteins.
Original languageEnglish (US)
Pages (from-to)2265 - 2277
Number of pages12
JournalPeptides
Volume23
Issue number12
StatePublished - Jan 2003

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