A GBP 130 derived peptide from Plasmodium falciparum binds to human erythrocytes and inhibits merozoite invasion in vitro

Mem Inst Oswaldo Cruz. 2000 Jul-Aug;95(4):495-501. doi: 10.1590/s0074-02762000000400009.

Abstract

The malarial GBP 130 protein binds weakly to intact human erythrocytes; the binding sites seem to be located in the repeat region and this region's antibodies block the merozoite invasion. A peptide from this region (residues from 701 to 720) which binds to human erythrocytes was identified. This peptide named 2220 did not bind to sialic acid; the binding site on human erythrocyte was affected by treatment with trypsin but not by chymotrypsin. The peptide was able to inhibit Plasmodium falciparum merozoite invasion of erythrocytes. The residues F701, K703, L705, T706, E713 (FYKILTNTDPNDEVERDNAD) were found to be critical for peptide binding to erythrocytes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Chymotrypsin / pharmacology
  • Erythrocytes / drug effects
  • Erythrocytes / metabolism*
  • Erythrocytes / parasitology
  • Glycophorins / biosynthesis
  • Glycophorins / metabolism*
  • Humans
  • Molecular Sequence Data
  • N-Acetylneuraminic Acid / metabolism
  • Plasmodium falciparum / drug effects
  • Plasmodium falciparum / metabolism*
  • Protozoan Proteins / metabolism*
  • Sequence Analysis, Protein
  • Trypsin / pharmacology

Substances

  • Glycophorins
  • Protozoan Proteins
  • glycophorin-binding protein homologue, Plasmodium
  • Chymotrypsin
  • Trypsin
  • N-Acetylneuraminic Acid