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Plasmodium falciparum merozoite surface protein 6 (MSP-6) derived peptides bind erythrocytes and partially inhibit parasite invasion

  • Ramsés López
  • , John Valbuena
  • , Luis E. Rodríguez
  • , Marisol Ocampo
  • , Ricardo Vera
  • , Hernando Curtidor
  • , Alvaro Puentes
  • , Javier García
  • , Luis E. Ramirez
  • , Manuel E. Patarroyo

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

This work shows that Plasmodium falciparum merozoite surface protein-6 (MSP-6) peptides specifically bind to membrane surface receptor on human erythrocytes. Three high activity binding peptides (HABPs) were found: peptides 31175 (41MYNNDKILSKNEVDTNIESN60) and 31178 (101YDIQATYQFPSTSGGNNVIP120) in the amino terminal region and 31191 (361EIDSTINNLVQEMIHLFSNNY380) at the carboxy terminal. Their binding to erythrocytes was saturable. HABPs 31191 and 31178 recognized 56 and 26 kDa receptors on erythrocyte membrane and inhibited in vitro Plasmodium falciparum merozoite invasion of erythrocytes by between 27% and 46% at 200 μg ml-1 concentration, suggesting that these MSP-6 protein peptides play a possible role in the invasion process.

Original languageEnglish
Pages (from-to)1685-1692
Number of pages8
JournalPeptides
Volume27
Issue number7
DOIs
StatePublished - Jul 2006
Externally publishedYes

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

  1. SDG 3 - Good Health and Well-being
    SDG 3 Good Health and Well-being

Keywords

  • Binding
  • Invasion
  • Ligand
  • MSP-6
  • Plasmodium falciparum
  • Receptor
  • Vaccine

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