Fine mapping of Plasmodium falciparum ribosomal phosphoprotein PfP0 revealed sequences with highly specific binding activity to human red blood cells

Gabriela Arevalo-Pinzon, Hernando Curtidor, Claudia Reyes, Martha Pinto, Carolina Vizcaíno, Manuel A. Patarroyo, Manuel E. Patarroyo

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

The Plasmodium falciparum P0 ribosomal phosphoprotein (PfP0) was identified for the first time by screening a cDNA expression library of P. falciparum parasites with sera from malaria-immune individuals. Due to its localization on the surface of different parasite life-cycle stages (merozoites and gametocytes) and its recognition by invasion-blocking antibodies, PfP0 has been considered a potential malaria-vaccine component. In this study, 16 20-mer-long synthetic peptides spanning the entire PfP0 sequence were evaluated by means of receptor-ligand assays with human red blood cells (RBCs) in order to determine the role played by these peptides in the invasion process. Four RBC high-activity binding peptides (HABPs), located mostly toward the N-terminal region, were identified: HABP 33898 (1MAKLSKQQKKQMYIEKLSSL 20), HABP 33900 (41ASVRKSLRGKATILMGKNTRY60), HABP 33901 (61IRTALKKNLQAVPQIEKLLPY 80), and HABP 33906 (161LIKQGEKVTASSATLLRKFNY180). The binding pattern of HABPs 33898 and 33906 to enzyme-treated RBCs suggests receptors of protein nature for these two HABPs, one of which could correspond to a common 58-kDa RBC membrane protein, as indicated by results of cross-linking assays. Both HABPs exhibited high content of α-helical features and prevented P. falciparum merozoite invasion to RBCs in vitro by up to 91%. The invasion-blocking ability reported here for these PfP0 HABPs supports their inclusion in immunological studies with the aim of assessing their potential as candidates for a vaccine against P. falciparum malaria.

Original languageEnglish (US)
Pages (from-to)61-74
Number of pages14
JournalJournal of Molecular Medicine
Volume88
Issue number1
DOIs
StatePublished - Jan 2010

All Science Journal Classification (ASJC) codes

  • Molecular Medicine
  • Drug Discovery
  • Genetics(clinical)

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