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

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dc.contributor.authorAlbarracín, Romina M.
dc.contributor.authorLaguía Becher, M
dc.contributor.authorFarrán Blanch, Inmaculada
dc.contributor.authorSander, Valeria
dc.contributor.authorCorigliano, Mariana G.
dc.contributor.authorYácono, María del L.
dc.contributor.authorPariani, S
dc.contributor.authorSánchez López, Edwin F.
dc.contributor.authorVeramendi Charola, Jon
dc.contributor.authorClemente, Marina
dc.contributor.departmentIdAB. Instituto de Agrobiotecnología / Agrobioteknologiako Institutuaes_ES
dc.date.accessioned2018-04-10T12:22:14Z
dc.date.available2018-04-10T12:22:14Z
dc.date.issued2015
dc.description.abstractChloroplast 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 is to investigate the expression of SAG1 using chloroplast transformation technology in tobacco plants. In order to improve its expression in transplastomic plants, we also expressed the 90-kDa heat shock protein of Leishmania infantum (LiHsp83) as a carrier for SAG1 antigen. SAG1 protein accumulation in transplastomic plants was approximately 0.1-0.2 µg 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.en
dc.description.sponsorshipThis work was supported by PIP 0494CO of the National Research Council (CONICET, Argentina), University of General San Martín (UNSAM, Argentina) and Bunge & Born Foundation (Argentina).en
dc.format.mimetypeapplication/pdfen
dc.identifier.doi10.1002/biot.201400742
dc.identifier.issn1860-6768 (Print)
dc.identifier.issn1860-7314 (Electronic)
dc.identifier.urihttps://academica-e.unavarra.es/handle/2454/28207
dc.language.isoengen
dc.publisherWileyen
dc.relation.ispartofBiotechnology Journal. Special Issue: Vaccine Biotechnology, Vol. 10, Issue 5, may 2015, pgs. 748-759en
dc.relation.publisherversionhttps://doi.org/10.1002/biot.201400742
dc.rights© 2015 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheimen
dc.rights.accessRightsAcceso abierto / Sarbide irekiaes
dc.rights.accessRightsinfo:eu-repo/semantics/openAccessen
dc.subjectChloroplast transformationen
dc.subjectHsp83en
dc.subjectLeishmania infantumen
dc.subjectSAG1en
dc.subjectToxoplasma gondiien
dc.titleThe fusion of Toxoplasma gondii SAG1 vaccine candidate to Leishmania infantum heat shock protein 83-kDa improves expression levels in tobacco chloroplastsen
dc.typeArtículo / Artikuluaes
dc.typeinfo:eu-repo/semantics/articleen
dc.type.versionVersión aceptada / Onetsi den bertsioaes
dc.type.versioninfo:eu-repo/semantics/acceptedVersionen
dspace.entity.typePublication
relation.isAuthorOfPublication6442ab25-7b61-4611-a7b8-d237c8cf5d82
relation.isAuthorOfPublicationa901e048-1a47-49df-a6f4-c2012c88c29e
relation.isAuthorOfPublication.latestForDiscovery6442ab25-7b61-4611-a7b8-d237c8cf5d82

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