Synthetic peptides from two Pf sporozoite invasion-associated proteins specifically interact with HeLa and HepG2 cells

Two recently described molecules have been associated with sporozoite traversal ability and hepatocyte entry: sporozoite invasion-associated proteins (SIAP)-1 and -2. The HeLa and HepG2 cell binding ability of synthetic peptides spanning the whole SIAP-1 and -2 sequences has been studied in the search for identifying these proteins' functionally active specific regions. Twelve HepG-2 and seventeen HeLa cell high-activity binding peptides (HABPs) have been identified in SIAP-1, 8 of them having high specific binding affinity for both cell lines. Four HepG2 HABPs and two HeLa HABPs have been identified in SIAP-2, one of them interacting with both HeLa and HepG2 cells. SIAP-1 and SIAP-2 HABPs bound specifically and saturably to heparin sulfate and chondroitin sulfate-type membrane receptors on host cells. Circular dichroism assays have shown high ?-helix content in SIAP-1 and SIAP-2 HABP secondary structure. Immunofluorescence analysis has revealed that specific peptides against SIAP proteins are highly immunogenic in mice and that anti-SIAP-1 and -2 antibodies recognize the native protein in Plasmodium falciparum sporozoites. Polymorphism studies have shown that a most SIAP-1 and -2 HABPs are conserved among P. falciparum strains. Our results have suggested that SIAP-1 and -2 participate in host-pathogen interactions during cell-traversal and hepatocyte invasion and highlighted the relevance of the ongoing identification and study of potentially new molecules when designing a fully protective antimalarial vaccine. © 2011 Elsevier Inc.

• Fecha de publicación: 2011
• Institución: Universidad del Rosario
• Repositorio: Repositorio EdocUR - U. Rosario
• Idioma: eng
• OAI Identifier: oai:repository.urosario.edu.co:10336/22791
• Acceso en línea: https://doi.org/10.1016/j.peptides.2011.08.008; https://repository.urosario.edu.co/handle/10336/22791
• Palabra clave: Chondroitin sulfate; Circumsporozoite protein; Heparin; Protein siap 1; Protein siap 2; Unclassified drug; Article; Binding affinity; Circular dichroism; Controlled study; Genetic polymorphism; Human; Human cell; Immunofluorescence test; Immunogenicity; Liver cell; Plasmodium falciparum; Priority journal; Protein analysis; Protein interaction; Protein synthesis; Sporozoite; Amino acid sequence; Animals; Binding sites; Chondroitin sulfates; Circular dichroism; Hela cells; Hep g2 cells; Hepatocytes; Host-pathogen interactions; Humans; Mice; Molecular sequence data; Peptides; Plasmodium falciparum; Protein binding; Protozoan proteins; Sporozoites; Mus; Plasmodium falciparum; Antimalarial vaccine; Cell-traversal; High-activity binding peptide; Plasmodium falciparum; Sporozoite invasion; genetic; synthetic; indirect; inbred balb c; Chemistry techniques; Fluorescent antibody technique; Mice; Polymorphism
• License: Abierto (Texto Completo)