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Double-layered rotavirus-like particles are efficient carriers to elicit strong CTL responses to delivered heterologous antigens
Resumen
The first 92 amino acids of VP2 of rotavirus are dispensable for VLP assembly and can be replaced by heterologous reporter proteins without affecting either self-assembly of chimeric VP2 or the interaction with VP6 to render chimeric VP2/6 VLPs. In this study, we constructed recombinant baculoviruses expressing GFP or OVA fused to the amino terminus of a truncated VP2 sequence and produced chimeric VLPs by co-infection with a baculovirus expressing VP6.
[ver mas...]
The first 92 amino acids of VP2 of rotavirus are dispensable for VLP assembly and can be replaced by heterologous reporter proteins without affecting either self-assembly of chimeric VP2 or the interaction with VP6 to render chimeric VP2/6 VLPs. In this study, we constructed recombinant baculoviruses expressing GFP or OVA fused to the amino terminus of a truncated VP2 sequence and produced chimeric VLPs by co-infection with a baculovirus expressing VP6. The results showed that these chimeric VLPs were efficiently uptaken by murine dendritic cells and that the heterologous sequences contained in the core of these VLPs seemed to be able to reach the MHC-I pathway as they elicited strong and specific CTL responses. Therefore, the data presented here suggest that chimeric VLPs could be used as excellent carriers to elicit CTL responses to antigens transported inside the VLPs.
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Autor
Molinari, Maria Paula;
Peralta, Andrea Veronica;
Maletto, Belkys Angélica;
Pistoresi Palencia, Maria Cristina;
Crespo, Maria Ines;
Moron, Victor Gabriel;
Taboga, Oscar Alberto;
Fuente
Process Biochemistry 49 (11) : 1929-1935 (November 2014)
Fecha
2014-11
Editorial
Elsevier
ISSN
1359-5113
Formato
pdf
Tipo de documento
artículo
Palabras Claves
Derechos de acceso
Restringido
Excepto donde se diga explicitamente, este item se publica bajo la siguiente descripción: Creative Commons Attribution-NonCommercial-ShareAlike 2.5 Unported (CC BY-NC-SA 2.5)