Título

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

Autor

CARLOS ALBERTO MANUEL CABRERA

ALBA ADRIANA VALLEJO CARDONA

EDUARDO PADILLA CAMBEROS

RODOLFO HERNANDEZ GUTIERREZ

SARA ELISA HERRERA RODRIGUEZ

ABEL GUTIERREZ ORTEGA

Nivel de Acceso

Acceso Abierto

Licencia

http://creativecommons.org/licenses/by-nc-nd/4.0

Referencia de publicación

doi: 10.1186/s12985-016-0651-y

Materias

virus del grabado del tabaco, proteína de la cápside, partículas pseudovíricas, etiqueta de hexahistidinas, adyuvante, proteína quimérica - (AUTOR) BIOLOGÍA Y QUÍMICA - (CTI) CIENCIAS DE LA VIDA - (CTI) BIOLOGÍA MOLECULAR - (CTI) BIOLOGÍA MOLECULAR - (CTI)

Resumen o descripción

"Abstract

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".

Editor

BioMed Central

Fecha de publicación

29 de noviembre de 2016

Tipo de publicación

Artículo

Versión de la publicación

Versión publicada

Recurso de información

http://ciatej.repositorioinstitucional.mx/jspui/handle/1023/397

Formato

application/pdf

Fuente

Virology Journal

Idioma

Inglés

Audiencia

Estudiantes

Investigadores

Repositorio Orígen

Repositorio Institucional de CIATEJ

Descargas

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