Identification and polymorphism of Plasmodium vivax RBP-1 peptides which bind specifically to reticulocytes

Peptides. 2002 Dec;23(12):2265-77. doi: 10.1016/s0196-9781(02)00267-x.

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.

MeSH terms

  • Animals
  • Binding Sites / genetics
  • Binding Sites / physiology
  • Erythrocytes / metabolism
  • Kinetics
  • Membrane Proteins / genetics
  • Membrane Proteins / isolation & purification*
  • Membrane Proteins / metabolism
  • Peptides / genetics
  • Peptides / isolation & purification
  • Peptides / metabolism
  • Plasmodium vivax / genetics*
  • Plasmodium vivax / metabolism
  • Polymorphism, Genetic*
  • Protozoan Proteins / genetics
  • Protozoan Proteins / isolation & purification*
  • Protozoan Proteins / metabolism
  • Receptors, Cell Surface / metabolism
  • Reticulocytes / metabolism*

Substances

  • Membrane Proteins
  • Peptides
  • Protozoan Proteins
  • Receptors, Cell Surface
  • reticulocyte-binding protein, Plasmodium vivax