The fusion of Toxoplasma gondii SAG1 vaccine candidate to Leishmania infantum heat shock protein 83‐kDa improves expression levels in tobacco chloroplasts

作者: Romina M. Albarracín , Melina Laguía Becher , Inmaculada Farran , Valeria A. Sander , Mariana G. Corigliano

DOI: 10.1002/BIOT.201400742

关键词: VirologyBiologyLeishmania infantumTransformation (genetics)Fusion proteinAntigenTransplastomic plantHeat shock proteinChloroplastToxoplasma gondii

摘要: Chloroplast transformation technology has emerged as an alternative platform offering many advantages over nuclear transformation. SAG1 is the main surface antigen of intracellular parasite Toxoplasma gondii and a promising candidate to produce anti-T. vaccine. The aim this study was investigate expression using chloroplast in tobacco plants. In order improve transplastomic plants, we also expressed 90-kDa heat shock protein Leishmania infantum (LiHsp83) carrier for antigen. accumulation plants approximately 0.1-0.2 μg per gram fresh weight (FW). Fusion LiHsp83 significantly increased level chloroplasts (by up 500-fold). We evaluated functionality chLiHsp83-SAG1. Three human seropositive samples reacted with chLiHsp83-SAG1 Oral immunization elicited significant reduction cyst burden that correlated increase SAG1-specific antibodies. propose fusion foreign proteins novel strategy recombinant technology, thus addressing one current challenges approach production.

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