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A bivalent dendrimeric peptide bearing a T-cell epitope from foot-and-mouth disease virus protein 3A improves humoral response against classical swine fever virus

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dc.contributor.author Bohórquez, José Alejandro
dc.contributor.author Defaus, Sira
dc.contributor.author Muñoz-González, Sara
dc.contributor.author Perez-Simó, Marta
dc.contributor.author Rosell, Rosa
dc.contributor.author Fraile, Lorenzo
dc.contributor.author Sobrino, Francisco
dc.contributor.author Andreu Martínez, David
dc.contributor.author Ganges, Lliliane
dc.date.accessioned 2018-11-13T09:56:59Z
dc.date.available 2018-11-13T09:56:59Z
dc.date.issued 2017
dc.identifier.citation Bohórquez JA, Defaus S, Muñoz-González S, Perez-Simó M, Rosell R, Fraile L et al. A bivalent dendrimeric peptide bearing a T-cell epitope from foot-and-mouth disease virus protein 3A improves humoral response against classical swine fever virus. Virus Res. 2017 Jun 15;238:8-12. DOI: 10.1016/j.virusres.2017.05.020
dc.identifier.issn 0168-1702
dc.identifier.uri http://hdl.handle.net/10230/35738
dc.description.abstract Three dendrimeric peptides were synthesized in order to evaluate their immunogenicity and their potential protection against classical swine fever virus (CSFV) in domestic pigs. Construct 1, an optimized version of a previously used dendrimer, had four copies of a B-cell epitope derived from CSFV E2 glycoprotein connected to an also CSFV-derived T-cell epitope through maleimide instead of thioether linkages. Construct 2 was similarly built but included only two copies of the B-cell epitope, and in also bivalent construct 3 the CSFV T-cell epitope was replaced by a previously described one from the 3A protein of foot-and-mouth disease virus (FMDV). Animals were inoculated twice with a 21-day interval and challenged 15days after the second immunization. Clinical signs were recorded daily and ELISA tests were performed to detect antibodies against specific peptide and E2. The neutralising antibody response was assessed 13days after challenge. Despite the change to maleimide connectivity, only partial protection against CSFV was again observed. The best clinical protection was observed in group 3. Animals inoculated with constructs 2 and 3 showed higher anti-peptide humoral response, suggesting that two copies of the B-cell epitope are sufficient or even better than four copies for swine immune recognition. In addition, for construct 3 higher neutralizing antibody titres against CSFV were detected. Our results support the immunogenicity of the CSFV B-cell epitope and the cooperative role of the FMDV 3A T-cell epitope in inducing a neutralising response against CSFV in domestic pigs. This is also the first time that the FMDV T-cell epitope shows effectivity in improving swine immune response against a different virus. Our findings highlight the relevance of dendrimeric peptides as a powerful tool for epitope characterization and antiviral strategies development.
dc.description.sponsorship The research in CReSA was supported by grant AGL2015-66907 from the Spanish government. J.A. B. had a pre-doctoral fellowship FPI-MINECO 2016 from Spanish government. S. M. had a pre-doctoral fellowship FI-DGR 2014 from AGAUR, Generalitat de Catalunya. Work at CBMSO was supported by grants AGL2014-52395-C2-01 (MINECO, Spain) and S2013/ABI-2906-PLATESA (Comunidad Autónoma de Madrid). Work at UPF was funded by AGL2014-52395-C2-02 (MINECO, Spain)
dc.format.mimetype application/pdf
dc.language.iso eng
dc.publisher Elsevier
dc.relation.ispartof Virus Research. 2017 Jun 15;238:8-12
dc.rights © Elsevier http://dx.doi.org/10.1016/j.virusres.2017.05.020
dc.subject.other Pesta porcina clàssica
dc.subject.other Dendrímers
dc.subject.other Determinant antigènic
dc.subject.other Glossopeda
dc.subject.other Vacunes antivíriques
dc.title A bivalent dendrimeric peptide bearing a T-cell epitope from foot-and-mouth disease virus protein 3A improves humoral response against classical swine fever virus
dc.type info:eu-repo/semantics/article
dc.identifier.doi http://dx.doi.org/10.1016/j.virusres.2017.05.020
dc.relation.projectID info:eu-repo/grantAgreement/ES/1PE/AGL2015-66907
dc.relation.projectID info:eu-repo/grantAgreement/ES/1PE/AGL2014-52395-C2-01
dc.rights.accessRights info:eu-repo/semantics/openAccess
dc.type.version info:eu-repo/semantics/acceptedVersion

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