Transgenic nicotiana tabacum seeds expressing the Mycobacterium tuberculosis Alanine- and Proline-rich Antigen.
Autor(a) principal: | |
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Data de Publicação: | 2018 |
Outros Autores: | , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) |
Texto Completo: | http://www.alice.cnptia.embrapa.br/alice/handle/doc/1105869 |
Resumo: | The glycoprotein APA (Alanine- and Proline-rich Antigen, a 45/47 kDa antigen complex, Rv1860) is considered as a major immunodominant antigen secreted by M. tuberculosis. This antigen has proved to be highly immunogenic in experimental models and humans, presenting a significant potential for further development of a new vaccine for tuberculosis. Glycosylation plays a key role in the immunogenicity of the APA protein. Because plants are known to promote post-translational modification such as glycosylation and to be one of the most economic and safe hosts for recombinant protein expression, we have over expressed the APA protein in transgenic tobacco plants aiming to produce a glycosylated version of the protein. Seeds are known to be a well-suited organ to accumulate recombinant proteins, due to low protease activity and higher protein stability. We used a seed-specific promoter from sorghum, a signal peptide to target the protein to the endoplasmic reticulum and ultimately in the protein storage vacuoles. We show that the recombinant protein accumulated in the seeds had similar isoelectric point and molecular weight compared with the native protein. These findings demonstrate the ability of tobacco plants to produce glycosylated APA protein, opening the way for the development of secure, effective and versatile vaccines or therapeutic proteins against tuberculosis. |
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Transgenic nicotiana tabacum seeds expressing the Mycobacterium tuberculosis Alanine- and Proline-rich Antigen.GlicosilaçãoTabacoGlicoproteínaTuberculoseSementeAntígenoThe glycoprotein APA (Alanine- and Proline-rich Antigen, a 45/47 kDa antigen complex, Rv1860) is considered as a major immunodominant antigen secreted by M. tuberculosis. This antigen has proved to be highly immunogenic in experimental models and humans, presenting a significant potential for further development of a new vaccine for tuberculosis. Glycosylation plays a key role in the immunogenicity of the APA protein. Because plants are known to promote post-translational modification such as glycosylation and to be one of the most economic and safe hosts for recombinant protein expression, we have over expressed the APA protein in transgenic tobacco plants aiming to produce a glycosylated version of the protein. Seeds are known to be a well-suited organ to accumulate recombinant proteins, due to low protease activity and higher protein stability. We used a seed-specific promoter from sorghum, a signal peptide to target the protein to the endoplasmic reticulum and ultimately in the protein storage vacuoles. We show that the recombinant protein accumulated in the seeds had similar isoelectric point and molecular weight compared with the native protein. These findings demonstrate the ability of tobacco plants to produce glycosylated APA protein, opening the way for the development of secure, effective and versatile vaccines or therapeutic proteins against tuberculosis.Diego G. Módolo, Universidade Estadual de Campinas; Cynthia S. Horn, Fundação Oswaldo Cruz; José S. M. Soares, Universidade Estadual de Campinas; José A. Yunes, Centro Infantil de Investigações Hematológicas Dr Domingos A Boldrini; Leila M. Lima, Fundação Oswaldo Cruz; SYLVIA MORAIS DE SOUSA TINOCO, CNPMS; Marcelo Menossi, Universidade Estadual de Campinas.MÓDOLO, D. G.HORN, C. S.SOARES, J. S. M.YUNES, J. A.LIMA, L. M.SOUSA, S. M. deMENOSSI, M.2019-02-12T23:48:16Z2019-02-12T23:48:16Z2019-02-1220182019-02-12T23:48:16Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleAMB Express, v. 8, n. 178, p. 1-10, 2018.http://www.alice.cnptia.embrapa.br/alice/handle/doc/110586910.1186/s13568-018-0708-yenginfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)instname:Empresa Brasileira de Pesquisa Agropecuária (Embrapa)instacron:EMBRAPA2019-02-12T23:48:25Zoai:www.alice.cnptia.embrapa.br:doc/1105869Repositório InstitucionalPUBhttps://www.alice.cnptia.embrapa.br/oai/requestopendoar:21542019-02-12T23:48:25falseRepositório InstitucionalPUBhttps://www.alice.cnptia.embrapa.br/oai/requestcg-riaa@embrapa.bropendoar:21542019-02-12T23:48:25Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) - Empresa Brasileira de Pesquisa Agropecuária (Embrapa)false |
dc.title.none.fl_str_mv |
Transgenic nicotiana tabacum seeds expressing the Mycobacterium tuberculosis Alanine- and Proline-rich Antigen. |
title |
Transgenic nicotiana tabacum seeds expressing the Mycobacterium tuberculosis Alanine- and Proline-rich Antigen. |
spellingShingle |
Transgenic nicotiana tabacum seeds expressing the Mycobacterium tuberculosis Alanine- and Proline-rich Antigen. MÓDOLO, D. G. Glicosilação Tabaco Glicoproteína Tuberculose Semente Antígeno |
title_short |
Transgenic nicotiana tabacum seeds expressing the Mycobacterium tuberculosis Alanine- and Proline-rich Antigen. |
title_full |
Transgenic nicotiana tabacum seeds expressing the Mycobacterium tuberculosis Alanine- and Proline-rich Antigen. |
title_fullStr |
Transgenic nicotiana tabacum seeds expressing the Mycobacterium tuberculosis Alanine- and Proline-rich Antigen. |
title_full_unstemmed |
Transgenic nicotiana tabacum seeds expressing the Mycobacterium tuberculosis Alanine- and Proline-rich Antigen. |
title_sort |
Transgenic nicotiana tabacum seeds expressing the Mycobacterium tuberculosis Alanine- and Proline-rich Antigen. |
author |
MÓDOLO, D. G. |
author_facet |
MÓDOLO, D. G. HORN, C. S. SOARES, J. S. M. YUNES, J. A. LIMA, L. M. SOUSA, S. M. de MENOSSI, M. |
author_role |
author |
author2 |
HORN, C. S. SOARES, J. S. M. YUNES, J. A. LIMA, L. M. SOUSA, S. M. de MENOSSI, M. |
author2_role |
author author author author author author |
dc.contributor.none.fl_str_mv |
Diego G. Módolo, Universidade Estadual de Campinas; Cynthia S. Horn, Fundação Oswaldo Cruz; José S. M. Soares, Universidade Estadual de Campinas; José A. Yunes, Centro Infantil de Investigações Hematológicas Dr Domingos A Boldrini; Leila M. Lima, Fundação Oswaldo Cruz; SYLVIA MORAIS DE SOUSA TINOCO, CNPMS; Marcelo Menossi, Universidade Estadual de Campinas. |
dc.contributor.author.fl_str_mv |
MÓDOLO, D. G. HORN, C. S. SOARES, J. S. M. YUNES, J. A. LIMA, L. M. SOUSA, S. M. de MENOSSI, M. |
dc.subject.por.fl_str_mv |
Glicosilação Tabaco Glicoproteína Tuberculose Semente Antígeno |
topic |
Glicosilação Tabaco Glicoproteína Tuberculose Semente Antígeno |
description |
The glycoprotein APA (Alanine- and Proline-rich Antigen, a 45/47 kDa antigen complex, Rv1860) is considered as a major immunodominant antigen secreted by M. tuberculosis. This antigen has proved to be highly immunogenic in experimental models and humans, presenting a significant potential for further development of a new vaccine for tuberculosis. Glycosylation plays a key role in the immunogenicity of the APA protein. Because plants are known to promote post-translational modification such as glycosylation and to be one of the most economic and safe hosts for recombinant protein expression, we have over expressed the APA protein in transgenic tobacco plants aiming to produce a glycosylated version of the protein. Seeds are known to be a well-suited organ to accumulate recombinant proteins, due to low protease activity and higher protein stability. We used a seed-specific promoter from sorghum, a signal peptide to target the protein to the endoplasmic reticulum and ultimately in the protein storage vacuoles. We show that the recombinant protein accumulated in the seeds had similar isoelectric point and molecular weight compared with the native protein. These findings demonstrate the ability of tobacco plants to produce glycosylated APA protein, opening the way for the development of secure, effective and versatile vaccines or therapeutic proteins against tuberculosis. |
publishDate |
2018 |
dc.date.none.fl_str_mv |
2018 2019-02-12T23:48:16Z 2019-02-12T23:48:16Z 2019-02-12 2019-02-12T23:48:16Z |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/publishedVersion info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
AMB Express, v. 8, n. 178, p. 1-10, 2018. http://www.alice.cnptia.embrapa.br/alice/handle/doc/1105869 10.1186/s13568-018-0708-y |
identifier_str_mv |
AMB Express, v. 8, n. 178, p. 1-10, 2018. 10.1186/s13568-018-0708-y |
url |
http://www.alice.cnptia.embrapa.br/alice/handle/doc/1105869 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.source.none.fl_str_mv |
reponame:Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) instname:Empresa Brasileira de Pesquisa Agropecuária (Embrapa) instacron:EMBRAPA |
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Empresa Brasileira de Pesquisa Agropecuária (Embrapa) |
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EMBRAPA |
institution |
EMBRAPA |
reponame_str |
Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) |
collection |
Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) |
repository.name.fl_str_mv |
Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) - Empresa Brasileira de Pesquisa Agropecuária (Embrapa) |
repository.mail.fl_str_mv |
cg-riaa@embrapa.br |
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1794503471412543488 |