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

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Arévalo-Pinzón G.
Curtidor H.
Muñoz M.
Patarroyo M.A.
Patarroyo M.E.




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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.
Palabras clave
Chondroitin sulfate , genetic , 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 , Chemistry techniques , Chondroitin sulfates , Circular dichroism , Fluorescent antibody technique , Hela cells , Hep g2 cells , Hepatocytes , Host-pathogen interactions , Humans , Mice , Mice , Molecular sequence data , Peptides , Plasmodium falciparum , Polymorphism , Protein binding , Protozoan proteins , Sporozoites , Mus , Plasmodium falciparum , Antimalarial vaccine , Cell-traversal , High-activity binding peptide , Plasmodium falciparum , Sporozoite invasion