A Heterologous Viral Protein Scaffold for Chimeric Antigen Design: An Example PCV2 Virus Vaccine Candidate
Emilio Lamazares,
Fernando Gutiérrez,
Angela Hidalgo,
Nicolas A. Gutiérrez,
Felipe I. Espinoza,
Oliberto Sánchez,
Marcelo Cortez-San Martín,
Carolina Mascayano,
Javier González,
José Saavedra,
Claudia Altamirano,
Manuel Mansur,
Álvaro Ruiz,
Jorge R. Toledo
Affiliations
Emilio Lamazares
Biotechnology and Biopharmaceutical Laboratory, Departamento de Fisiopatología; Facultad de Ciencias Biológicas, Universidad de Concepción, Víctor Lamas 1290, P.O. Box 160-C, Concepción 4079386, Chile
Fernando Gutiérrez
Biotechnology and Biopharmaceutical Laboratory, Departamento de Fisiopatología; Facultad de Ciencias Biológicas, Universidad de Concepción, Víctor Lamas 1290, P.O. Box 160-C, Concepción 4079386, Chile
Angela Hidalgo
Biotechnology and Biopharmaceutical Laboratory, Departamento de Fisiopatología; Facultad de Ciencias Biológicas, Universidad de Concepción, Víctor Lamas 1290, P.O. Box 160-C, Concepción 4079386, Chile
Nicolas A. Gutiérrez
Biotechnology and Biopharmaceutical Laboratory, Departamento de Fisiopatología; Facultad de Ciencias Biológicas, Universidad de Concepción, Víctor Lamas 1290, P.O. Box 160-C, Concepción 4079386, Chile
Felipe I. Espinoza
Biotechnology and Biopharmaceutical Laboratory, Departamento de Fisiopatología; Facultad de Ciencias Biológicas, Universidad de Concepción, Víctor Lamas 1290, P.O. Box 160-C, Concepción 4079386, Chile
Oliberto Sánchez
Biotechnology and Biopharmaceutical Laboratory, Departamento de Fisiopatología; Facultad de Ciencias Biológicas, Universidad de Concepción, Víctor Lamas 1290, P.O. Box 160-C, Concepción 4079386, Chile
Marcelo Cortez-San Martín
Molecular Virology and Pathogen Control Laboratory, Departamento de Biología, Facultad de Química y Biología, Universidad de Santiago de Chile (USACH), Alameda 3363, Correo 40, Casilla 33, Santiago 9170022, Chile
Carolina Mascayano
Departamento de Ciencias del Ambiente, Facultad de Química y Biología, Universidad de Santiago de Chile (USACH), Alameda 3363, Correo 40, Casilla 33, Santiago 9170022, Chile
Javier González
Natural History Museum of Potsdam, 14467 Potsdam, Germany
José Saavedra
Molecular Virology and Pathogen Control Laboratory, Departamento de Biología, Facultad de Química y Biología, Universidad de Santiago de Chile (USACH), Alameda 3363, Correo 40, Casilla 33, Santiago 9170022, Chile
Claudia Altamirano
Laboratorio of Cultivos Celulares, Escuela de Ingeniería Bioquímica, Pontificia Universidad Católica de Valparaíso, Ave. Brasil 2085, Valparaíso 2362803, Chile
Manuel Mansur
Moderna Therapeutics 100 Upland Rd., Norwood, MA 02062, USA
Álvaro Ruiz
Pathology and Preventive Medicine Department, School of Veterinary Sciences, Universidad de Concepción, Ave. Vicente Méndez 595, Chillan 3812120, Chile
Jorge R. Toledo
Biotechnology and Biopharmaceutical Laboratory, Departamento de Fisiopatología; Facultad de Ciencias Biológicas, Universidad de Concepción, Víctor Lamas 1290, P.O. Box 160-C, Concepción 4079386, Chile
Recombinant vaccines have low-cost manufacturing, regulatory requirements, and reduced side effects compared to attenuated or inactivated vaccines. In the porcine industry, post-weaning multisystemic disease syndrome generates economic losses, characterized by progressive weight loss and weakness in piglets, and it is caused by porcine circovirus type 2 (PCV2). We designed a chimeric antigen (Qm1) to assemble the main exposed epitopes of the Cap-PCV2 protein on the capsid protein of the tobacco necrosis virus (TNV). This design was based on the Cap-N-terminal of an isolated PCV2 virus obtained in Chile. The virus was characterized, and the sequence was clustered within the PCV2 genotype b clade. This chimeric protein was expressed as inclusion bodies in both monomeric and multimeric forms, suggesting a high-molecular-weight aggregate formation. Pigs immunized with Qm1 elicited a strong and specific antibody response, which reduced the viral loads after the PCV2 challenge. In conclusion, the implemented design allowed for the generation of an effective vaccine candidate. Our proposal could be used to express the domains or fragments of antigenic proteins, whose structural complexity does not allow for low-cost production in Escherichia coli. Hence, other antigen domains could be integrated into the TNV backbone for suitable antigenicity and immunogenicity. This work represents new biotechnological strategies, with a reduction in the costs associated with vaccine development.