Immunogenicity of a dendrimer B 2 T peptide harboring a T-cell epitope from FMDV non-structural protein 3D

Cañas Arranz, Rodrigo; de León, Patricia; Forner, Mar, 1980-; Defaus, Sira; Bustos, María J.; Torres, Elisa; Andreu Martínez, David; Blanco, Esther; Sobrino, Francisco

doi:http://dx.doi.org/10.3389/fvets.2020.00498

Immunogenicity of a dendrimer B 2 T peptide harboring a T-cell epitope from FMDV non-structural protein 3D

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Cañas-Arranz R, de León P, Forner M, Defaus S, Bustos MJ, Torres E, Andreu D, Blanco E, Sobrino F. Immunogenicity of a dendrimer B 2 T peptide harboring a T-cell epitope from FMDV non-structural protein 3D. Front Vet Sci. 2020; 7:498. DOI: 10.3389/fvets.2020.00498

Abstract

Synthetic dendrimer peptides are a promising strategy to develop new FMD vaccines. A dendrimer peptide, termed B2T-3A, which harbors two copies of the major FMDV antigenic B-cell site [VP1 (140-158)], covalently linked to a heterotypic T-cell from the non-structural protein 3A [3A (21-35)], has been shown to protect pigs against viral challenge. Interestingly, the modular design of this dendrimer peptide allows modifications aimed at improving its immunogenicity, such as the replacement of the T-cell epitope moiety. Here, we report that a dendrimer peptide, B2T-3D, harboring a T-cell epitope from FMDV 3D protein [3D (56-70)], when inoculated in pigs, elicited consistent levels of neutralizing antibodies and high frequencies of IFN-γ-producing cells upon in vitro recall with the homologous dendrimers, both responses being similar to those evoked by B2T-3A. Lymphocytes from B2T-3A-immunized pigs were in vitro-stimulated by T-3A peptide and to a lesser extent by B-peptide, while those from B2T-3D- immunized animals preferentially recognized the T-3D peptide, suggesting that this epitope is a potent inducer of IFN-γ producing-cells. These results extend the repertoire of T-cell epitopes efficiently recognized by swine lymphocytes and open the possibility of using T-3D to enhance the immunogenicity and the protection conferred by B2T-dendrimers.