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Functional and immunological mapping of domains of the reticulocyte binding protein, Plasmodium vivax PvRBP2a.

Matthew Zirui TayWeiyi TangWenn-Chyau LeeAlice Soh Meoy OngWisna NoveraBenoît MalleretGuillaume CarissimoAnn-Marie ChackoAbbas El-SahiliJulien LescarYiping FanRose M McGreadyCindy S ChuJerry Kok Yen ChanLisa F P NgBruce M RussellFrançois NostenShanshan W Howland
Published in: The Journal of infectious diseases (2024)
We previously described a novel Plasmodium vivax invasion mechanism into human reticulocytes via the PvRBP2a-CD98 receptor-ligand pair. We assessed the PvRBP2a epitopes involved in CD98 binding and recognised by antibodies from infected patients using linear epitope mapping. We identified two epitope clusters mediating PvRBP2a-CD98 interaction. One cluster named cluster B (PvRBP2a431-448, TAALKEKGKLLANLYNKL) was the target of antibody responses in P. vivax-infected humans. Peptides from each cluster were able to prevent live parasite invasion of human reticulocytes. These results provide new insights for development of a malaria blood stage vaccine against P. vivax.
Keyphrases
  • plasmodium falciparum
  • binding protein
  • endothelial cells
  • high resolution
  • cell migration
  • pluripotent stem cells
  • nk cells
  • mass spectrometry
  • dna binding
  • toxoplasma gondii