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Self-assembly of hexahistidine-tagged tobacco etch virus capsid protein into microfilaments that induce IgG2-specific response against a soluble porcine reproductive and respiratory syndrome virus chimeric protein.
Manuel-Cabrera, Carlos Alberto; Vallejo-Cardona, Alba Adriana; Padilla-Camberos, Eduardo; Hernández-Gutiérrez, Rodolfo; Herrera-Rodríguez, Sara Elisa; Gutiérrez-Ortega, Abel.
Afiliação
  • Manuel-Cabrera CA; Unidad de Biotecnología Médica y Farmacéutica, Centro de Investigación y Asistencia en Tecnología y Diseño del Estado de Jalisco A.C., Normalistas 800, Colinas de la Normal, 44270, Guadalajara, Jalisco, Mexico.
  • Vallejo-Cardona AA; Unidad de Biotecnología Médica y Farmacéutica, Centro de Investigación y Asistencia en Tecnología y Diseño del Estado de Jalisco A.C., Normalistas 800, Colinas de la Normal, 44270, Guadalajara, Jalisco, Mexico.
  • Padilla-Camberos E; Unidad de Biotecnología Médica y Farmacéutica, Centro de Investigación y Asistencia en Tecnología y Diseño del Estado de Jalisco A.C., Normalistas 800, Colinas de la Normal, 44270, Guadalajara, Jalisco, Mexico.
  • Hernández-Gutiérrez R; Unidad de Biotecnología Médica y Farmacéutica, Centro de Investigación y Asistencia en Tecnología y Diseño del Estado de Jalisco A.C., Normalistas 800, Colinas de la Normal, 44270, Guadalajara, Jalisco, Mexico.
  • Herrera-Rodríguez SE; Unidad de Biotecnología Médica y Farmacéutica, Centro de Investigación y Asistencia en Tecnología y Diseño del Estado de Jalisco A.C., Normalistas 800, Colinas de la Normal, 44270, Guadalajara, Jalisco, Mexico.
  • Gutiérrez-Ortega A; Unidad de Biotecnología Médica y Farmacéutica, Centro de Investigación y Asistencia en Tecnología y Diseño del Estado de Jalisco A.C., Normalistas 800, Colinas de la Normal, 44270, Guadalajara, Jalisco, Mexico. aortega@ciatej.mx.
Virol J ; 13(1): 196, 2016 11 29.
Article em En | MEDLINE | ID: mdl-27894314
BACKGROUND: Assembly of recombinant capsid proteins into virus-like particles (VLPs) still represents an interesting challenge in virus-based nanotechnologies. The structure of VLPs has gained importance for the development and design of new adjuvants and antigen carriers. The potential of Tobacco etch virus capsid protein (TEV CP) as adjuvant has not been evaluated to date. FINDINGS: Two constructs for TEV CP expression in Escherichia coli were generated: a wild-type version (TEV-CP) and a C-terminal hexahistidine (His)-tagged version (His-TEV-CP). Although both versions were expressed in the soluble fraction of E. coli lysates, only His-TEV-CP self-assembled into micrometric flexuous filamentous VLPs. In addition, the His-tag enabled high yields and facilitated purification of TEV VLPs. These TEV VLPs elicited broader IgG2-specific antibody response against a novel porcine reproductive and respiratory syndrome virus (PRRSV) protein when compared to the potent IgG1 response induced by the protein alone. CONCLUSIONS: His-TEV CP was purified by immobilized metal affinity chromatography and assembled into VLPs, some of them reaching 2-µm length. TEV VLPs administered along with PRRSV chimeric protein changed the IgG2/IgG1 ratio against the chimeric protein, suggesting that TEV CP can modulate the immune response against a soluble antigen.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Vacinas Virais / Adjuvantes Imunológicos / Potyvirus / Vírus da Síndrome Respiratória e Reprodutiva Suína / Virossomos / Proteínas do Capsídeo / Anticorpos Antivirais Idioma: En Revista: Virol J Assunto da revista: VIROLOGIA Ano de publicação: 2016 Tipo de documento: Article País de afiliação: México País de publicação: Reino Unido
Texto completo
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Vacinas Virais / Adjuvantes Imunológicos / Potyvirus / Vírus da Síndrome Respiratória e Reprodutiva Suína / Virossomos / Proteínas do Capsídeo / Anticorpos Antivirais Idioma: En Revista: Virol J Assunto da revista: VIROLOGIA Ano de publicação: 2016 Tipo de documento: Article País de afiliação: México País de publicação: Reino Unido