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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Transgenic Nicotiana tabacum seeds expressing the Mycobacterium tuberculosis Alanine- and Proline-rich antigen

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Author(s):
Modolo, Diego G. [1, 2] ; Horn, Cynthia S. [3] ; Soares, Jose S. M. [2] ; Yunes, Jose A. [4] ; Lima, Leila M. [5] ; de Sousa, Sylvia M. [6] ; Menossi, Marcelo [2]
Total Authors: 7
Affiliation:
[1] Inst Butantan, Lab Genet, BR-05503900 Sao Paulo, SP - Brazil
[2] Univ Estadual Campinas, Inst Biol, Dept Genet Evolucao Microbiol & Imunol, Lab Genoma Func, Rua Monteiro Lobato 255, POB 6109, BR-13083970 Campinas, SP - Brazil
[3] Fundacao Oswaldo Cruz, Inst Nacl Infectol Evandro Chagas, Lab Imunol & Imunogenet Doencas Infecciosas, BR-21040900 Rio De Janeiro, RJ - Brazil
[4] Ctr Infantil Invest Hematol Dr Domingos A Boldrin, Lab Biol Mol, BR-13083210 Campinas, SP - Brazil
[5] Fundacao Oswaldo Cruz, Inst Oswaldo Cruz, Dept Bioquim & Biol Mol, BR-21040900 Rio De Janeiro, RJ - Brazil
[6] Empresa Brasileira Pesquisa Agr, Ctr Nacl Pesquisa Milho & Sorgo, BR-35701970 Sete Lagoas, MG - Brazil
Total Affiliations: 6
Document type: Journal article
Source: AMB EXPRESS; v. 8, OCT 31 2018.
Web of Science Citations: 0
Abstract

The glycoprotein APA (Alanine- and Proline-rich Antigen, a 45/47kDa 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. (AU)

FAPESP's process: 13/15576-5 - Molecular approaches to study the relationship between ethylene and sugarcane ripening
Grantee:Marcelo Menossi Teixeira
Support Opportunities: Program for Research on Bioenergy (BIOEN) - Thematic Grants