Sequences of the Plasmodium falciparum cytoadherence-linked asexual protein 9 implicated in malaria parasite invasion to erythrocytes Academic Article

abstract

  • In this study, we synthesized the complete sequence of the CLAG-9 protein as 67 20-mer-long non-overlapped peptides and assessed their ability to bind to erythrocytes in receptor-ligand assays. Twenty CLAG-9 peptides were found to have specific high-affinity binding ability to erythrocytes (thereby named as HABPs), with nanomolar dissociation constants. CLAG-9 HABPs interacted with different erythrocyte surface receptors having apparent molecular weights of 85, 63 and 34 kDa. CLAG-9 HABPs binding was also affected by pre-treatment of RBCs with enzymes and inhibited erythrocyte invasion in vitro by up to 72% at 200 μM. These results suggest that some protein fragments of CLAG-9 may be part of the molecular machinery used by malaria parasites to invade erythrocytes, hence supporting their study as possible vaccine candidates. © 2010 Elsevier Ltd. All rights reserved.

publication date

  • 2010/3/19

keywords

  • Enzymes
  • Erythrocytes
  • In Vitro Techniques
  • Ligands
  • Malaria
  • Molecular Weight
  • Parasites
  • Peptides
  • Plasmodium falciparum
  • Proteins
  • Vaccines
  • assays
  • binding capacity
  • cell adhesion
  • enzymes
  • erythrocytes
  • ligands
  • malaria
  • molecular weight
  • parasites
  • peptides
  • pretreatment
  • proteins
  • receptors
  • vaccines

International Standard Serial Number (ISSN)

  • 0264-410X

number of pages

  • 11

start page

  • 2653

end page

  • 2663