Plasmodium vivax antigen discovery based on alpha-helical coiled coil protein motif.

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Etat: Public
Version: de l'auteur
ID Serval
serval:BIB_4C88603DA7E0
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Plasmodium vivax antigen discovery based on alpha-helical coiled coil protein motif.
Périodique
PLoS One
Auteur(s)
Céspedes N., Habel C., Lopez-Perez M., Castellanos A., Kajava A.V., Servis C., Felger I., Moret R., Arévalo-Herrera M., Corradin G., Herrera S.
ISSN
1932-6203 (Electronic)
ISSN-L
1932-6203
Statut éditorial
Publié
Date de publication
2014
Volume
9
Numéro
6
Pages
e100440
Langue
anglais
Résumé
Protein α-helical coiled coil structures that elicit antibody responses, which block critical functions of medically important microorganisms, represent a means for vaccine development. By using bioinformatics algorithms, a total of 50 antigens with α-helical coiled coil motifs orthologous to Plasmodium falciparum were identified in the P. vivax genome. The peptides identified in silico were chemically synthesized; circular dichroism studies indicated partial or high α-helical content. Antigenicity was evaluated using human sera samples from malaria-endemic areas of Colombia and Papua New Guinea. Eight of these fragments were selected and used to assess immunogenicity in BALB/c mice. ELISA assays indicated strong reactivity of serum samples from individuals residing in malaria-endemic regions and sera of immunized mice, with the α-helical coiled coil structures. In addition, ex vivo production of IFN-γ by murine mononuclear cells confirmed the immunogenicity of these structures and the presence of T-cell epitopes in the peptide sequences. Moreover, sera of mice immunized with four of the eight antigens recognized native proteins on blood-stage P. vivax parasites, and antigenic cross-reactivity with three of the peptides was observed when reacted with both the P. falciparum orthologous fragments and whole parasites. Results here point to the α-helical coiled coil peptides as possible P. vivax malaria vaccine candidates as were observed for P. falciparum. Fragments selected here warrant further study in humans and non-human primate models to assess their protective efficacy as single components or assembled as hybrid linear epitopes.
Pubmed
Web of science
Open Access
Oui
Création de la notice
08/08/2014 18:28
Dernière modification de la notice
20/08/2019 14:01
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