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The synthetic, oxidized C-terminal fragment of the <i>Plasmodium berghei</i> circumsporozoite protein elicits a high protective response
Auteur(s)
Roggero, Mario A.
Meraldi, Valentin
López, José A.
Eberl, Gérard
Romero, Jackie C.
Matile, Hughe
Corradin, Giampietro
Renggli, John
Date de parution
2000
In
European Journal of Immunology, Wiley, 2000/30/9/2679-2685
Résumé
A polypeptide of 69 amino acids (PbCS 242-310) encompassing the C-terminal region of the circumsporozoite protein of <i>Plasmodium berghei</i> (PbCS) was generated using solid-phase peptide synthesis. The immunological and protective properties of peptide PbCS 242-310 were studied in BALB/c mice (H-2<sup>d</sup>). Two subcutaneous injections, in the presence of IFA at the base of the tail, generated (i) high titers of anti-peptide antibodies which also recognized the native <i>P. berghei</i> CS protein, (ii) cytolytic T cells specific for the K<sup>d</sup>-restricted peptide PbCS 245-253 and (iii) partial CD8<sup>+</sup>-dependent protection against sporozoite-induced malaria. The same frequencies of peptide PbCS 245-253 specific CD8<sup>+</sup> T cells were found by IFN-γ ELISPOT in the draining lymph nodes of animals immunized with the short optimal CTL peptide 245-253 or with the polypeptide 242-310, indicating that the longer polypeptide can be processed and presented <i>in vivo</i> in the context of MHC class I as efficiently as the short CTL peptide. Interestingly, higher levels of IFN-γ producing CD8<sup>+</sup> T cells and protection were observed when the four cysteine residues present in the C-terminal peptide were fully oxidized. These findings underline the potential importance of the chemical nature of the C-terminal fragment on the activation of the immune system and concomitant protection.
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Resource Types::text::journal::journal article
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