Heat treatment alleviates the growth and photosynthetic impairment of transplastomic plants expressing Leishmania infantum Hsp83-Toxoplasma gondii SAG1 fusion protein

Previously, we showed that transplastomic tobacco plants expressing the LiHsp83-SAG1 fusion protein displayed a chlorotic phenotype and growth retardation, while plants expressing the SAG1 and GRA4 antigens alone did not. We conducted a comprehensive examination of the metabolic and photosynthetic p...

Descripción completa

Detalles Bibliográficos
Autores: Corigliano, Mariana G., Albarracín, Romina M., Vilas, Juan M., Sánchez López, Edwin F., Bengoa Luoni, Sofía A., Deng, Bin, Farrán Blanch, Inmaculada, Veramendi Charola, Jon
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2019
País:España
Institución:Universidad Pública de Navarra
Repositorio:Academica-e. Repositorio Institucional de la Universidad Pública de Navarra
OAI Identifier:oai:academica-e.unavarra.es:2454/36195
Acceso en línea:https://hdl.handle.net/2454/36195
Access Level:acceso abierto
Palabra clave:Pleiotropic effects
Transplastomic plants
heat shock protein
Tobacco
Toxoplasma gondii
id ES_b2671cd96ffaddae047cf045e8576ff3
oai_identifier_str oai:academica-e.unavarra.es:2454/36195
network_acronym_str ES
network_name_str España
repository_id_str
spelling Heat treatment alleviates the growth and photosynthetic impairment of transplastomic plants expressing Leishmania infantum Hsp83-Toxoplasma gondii SAG1 fusion proteinCorigliano, Mariana G.Albarracín, Romina M.Vilas, Juan M.Sánchez López, Edwin F.Bengoa Luoni, Sofía A.Deng, BinFarrán Blanch, InmaculadaVeramendi Charola, JonPleiotropic effectsTransplastomic plantsheat shock proteinTobaccoToxoplasma gondiiPreviously, we showed that transplastomic tobacco plants expressing the LiHsp83-SAG1 fusion protein displayed a chlorotic phenotype and growth retardation, while plants expressing the SAG1 and GRA4 antigens alone did not. We conducted a comprehensive examination of the metabolic and photosynthetic parameters that could be affecting the normal growth of LiHsp83-SAG1 plants in order to understand the origin of these pleiotropic effects. These plants presented all photosynthetic pigments and parameters related to PSII efficiency significantly diminished. However, the expression ofCHLI, RSSU and LHCa/b genes did not show significant differences between LiHsp83-SAG1 and control plants. Total protein, starch, and soluble sugar contents were also greatly reduced in LiHsp83-SAG1 plants. Since Hsp90 s are constitutively expressed at much higher concentrations at high temperatures, we tested if the fitness of LiHsp83-SAG1 over-expressing LiHsp83 would improve after heat treatment. LiHsp83-SAG1 plants showed an important alleviation of their phenotype and an evident recovery of the PSII function. As far as we know, this is the first report where it is demonstrated that a transplastomic line performs much better at higher temperatures. Finally, we detected that LiHsp83-SAG1 protein could be binding to key photosynthesis-related proteins at 37 °C. Our results suggest that the excess of this molecular chaperone could benefit the plant in a possible heat shock and prevent the expected denaturation of proteins. However, the LiHsp83-SAG1 protein content was weakly decreased in heat-treated plants. Therefore, we cannot rule out that the alleviation observed at 37 °C may be partially due to a reduction of the levels of the recombinant protein.This work was supported by grants from the Agencia Nacional de Promoción Científica y Tecnológica of Argentina (PICT: 2014-3473, 2016-0113 and 2016-0621). This study also received institutional support from the Universidad Nacional General de SanMartín (UNSAM, Argentina). The Vermont Genetics Network Proteomics Facility is supported through NIH grant P20GM103449 from the INBRE Program of the National Institute of General Medical Sciences.ElsevierAgronomía, Biotecnología y AlimentaciónAgronomia, Bioteknologia eta Elikadura2019info:eu-repo/semantics/articleinfo:eu-repo/semantics/acceptedVersionapplication/pdfhttps://hdl.handle.net/2454/36195reponame:Academica-e. Repositorio Institucional de la Universidad Pública de Navarrainstname:Universidad Pública de NavarraInglés© 2019 Elsevier B.V. This manuscript version is made available under the CC-BY-NC-ND 4.0.https://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/openAccessoai:academica-e.unavarra.es:2454/361952026-06-17T12:41:47Z
dc.title.none.fl_str_mv Heat treatment alleviates the growth and photosynthetic impairment of transplastomic plants expressing Leishmania infantum Hsp83-Toxoplasma gondii SAG1 fusion protein
title Heat treatment alleviates the growth and photosynthetic impairment of transplastomic plants expressing Leishmania infantum Hsp83-Toxoplasma gondii SAG1 fusion protein
spellingShingle Heat treatment alleviates the growth and photosynthetic impairment of transplastomic plants expressing Leishmania infantum Hsp83-Toxoplasma gondii SAG1 fusion protein
Corigliano, Mariana G.
Pleiotropic effects
Transplastomic plants
heat shock protein
Tobacco
Toxoplasma gondii
title_short Heat treatment alleviates the growth and photosynthetic impairment of transplastomic plants expressing Leishmania infantum Hsp83-Toxoplasma gondii SAG1 fusion protein
title_full Heat treatment alleviates the growth and photosynthetic impairment of transplastomic plants expressing Leishmania infantum Hsp83-Toxoplasma gondii SAG1 fusion protein
title_fullStr Heat treatment alleviates the growth and photosynthetic impairment of transplastomic plants expressing Leishmania infantum Hsp83-Toxoplasma gondii SAG1 fusion protein
title_full_unstemmed Heat treatment alleviates the growth and photosynthetic impairment of transplastomic plants expressing Leishmania infantum Hsp83-Toxoplasma gondii SAG1 fusion protein
title_sort Heat treatment alleviates the growth and photosynthetic impairment of transplastomic plants expressing Leishmania infantum Hsp83-Toxoplasma gondii SAG1 fusion protein
dc.creator.none.fl_str_mv Corigliano, Mariana G.
Albarracín, Romina M.
Vilas, Juan M.
Sánchez López, Edwin F.
Bengoa Luoni, Sofía A.
Deng, Bin
Farrán Blanch, Inmaculada
Veramendi Charola, Jon
author Corigliano, Mariana G.
author_facet Corigliano, Mariana G.
Albarracín, Romina M.
Vilas, Juan M.
Sánchez López, Edwin F.
Bengoa Luoni, Sofía A.
Deng, Bin
Farrán Blanch, Inmaculada
Veramendi Charola, Jon
author_role author
author2 Albarracín, Romina M.
Vilas, Juan M.
Sánchez López, Edwin F.
Bengoa Luoni, Sofía A.
Deng, Bin
Farrán Blanch, Inmaculada
Veramendi Charola, Jon
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Agronomía, Biotecnología y Alimentación
Agronomia, Bioteknologia eta Elikadura
dc.subject.none.fl_str_mv Pleiotropic effects
Transplastomic plants
heat shock protein
Tobacco
Toxoplasma gondii
topic Pleiotropic effects
Transplastomic plants
heat shock protein
Tobacco
Toxoplasma gondii
description Previously, we showed that transplastomic tobacco plants expressing the LiHsp83-SAG1 fusion protein displayed a chlorotic phenotype and growth retardation, while plants expressing the SAG1 and GRA4 antigens alone did not. We conducted a comprehensive examination of the metabolic and photosynthetic parameters that could be affecting the normal growth of LiHsp83-SAG1 plants in order to understand the origin of these pleiotropic effects. These plants presented all photosynthetic pigments and parameters related to PSII efficiency significantly diminished. However, the expression ofCHLI, RSSU and LHCa/b genes did not show significant differences between LiHsp83-SAG1 and control plants. Total protein, starch, and soluble sugar contents were also greatly reduced in LiHsp83-SAG1 plants. Since Hsp90 s are constitutively expressed at much higher concentrations at high temperatures, we tested if the fitness of LiHsp83-SAG1 over-expressing LiHsp83 would improve after heat treatment. LiHsp83-SAG1 plants showed an important alleviation of their phenotype and an evident recovery of the PSII function. As far as we know, this is the first report where it is demonstrated that a transplastomic line performs much better at higher temperatures. Finally, we detected that LiHsp83-SAG1 protein could be binding to key photosynthesis-related proteins at 37 °C. Our results suggest that the excess of this molecular chaperone could benefit the plant in a possible heat shock and prevent the expected denaturation of proteins. However, the LiHsp83-SAG1 protein content was weakly decreased in heat-treated plants. Therefore, we cannot rule out that the alleviation observed at 37 °C may be partially due to a reduction of the levels of the recombinant protein.
publishDate 2019
dc.date.none.fl_str_mv 2019
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2454/36195
url https://hdl.handle.net/2454/36195
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.rights.none.fl_str_mv © 2019 Elsevier B.V. This manuscript version is made available under the CC-BY-NC-ND 4.0.
https://creativecommons.org/licenses/by-nc-nd/4.0/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv © 2019 Elsevier B.V. This manuscript version is made available under the CC-BY-NC-ND 4.0.
https://creativecommons.org/licenses/by-nc-nd/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:Academica-e. Repositorio Institucional de la Universidad Pública de Navarra
instname:Universidad Pública de Navarra
instname_str Universidad Pública de Navarra
reponame_str Academica-e. Repositorio Institucional de la Universidad Pública de Navarra
collection Academica-e. Repositorio Institucional de la Universidad Pública de Navarra
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869417051538325504
score 15,812429

Similares en LA Referencia