INVESTIGADORES
CLEMENTE marina
artículos
Título:
The fusion of Toxoplasma gondii SAG1 vaccine candidate to Leishmania infantum heat shock protein 83-kDa improves expression levels in tobacco chloroplasts.
Autor/es:
ALBARRACIN, R.; LAGUíA BECHER, M.; FARRAN, I.; SANDER, V.; CORIGLIANO, M.; YACONO, M. L.; PARIANI, S.; SANCHEZ LOPEZ, E.; VERAMENDI, J.; CLEMENTE, M.
Revista:
Biotechnology Journal
Editorial:
Wiley Online Library
Referencias:
Año: 2015 vol. 10 p. 748 - 759
ISSN:
1860-7314
Resumen:
Chloroplast transformation technology has emerged as an alternative platform offering many
advantages over nuclear transformation. SAG1 is the main surface antigen of the intracellular parasite
Toxoplasma gondii and a promising candidate to produce an anti-T. gondii vaccine. The aim
of this study was to investigate the expression of SAG1 using chloroplast transformation technology
in tobacco plants. In order to improve expression in transplastomic plants, we also expressed
the 90-kDa heat shock protein of Leishmania infantum (LiHsp83) as a carrier for the SAG1 antigen.
SAG1 protein accumulation in transplastomic plants was approximately 0.1?0.2 ìg per gram of
fresh weight (FW). Fusion of SAG1 to LiHsp83 significantly increased the level of SAG1 accumulation
in tobacco chloroplasts (by up to 500-fold). We also evaluated the functionality of the
chLiHsp83-SAG1. Three human seropositive samples reacted with SAG1 expressed in transplastomic
chLiHsp83-SAG1 plants. Oral immunization with chLiHsp83-SAG1 elicited a significant
reduction of the cyst burden that correlated with an increase of SAG1-specific antibodies. We propose
the fusion of foreign proteins to LiHsp83 as a novel strategy to increase the expression level
of the recombinant proteins using chloroplast transformation technology, thus addressing one of
the current challenges for this approach in antigen protein production.