Rhodococcus erythropolis as a host for expression, secretion and glycosylation of Mycobacterium tuberculosis proteins


Por: Vallecillo, Antonio J., Parada, Cristina, Morales, Pedro, Espitia, Clara

Publicada: 19 ene 2017
Resumen:
Background: Glycosylation is one of the most abundant posttranslational polypeptide chain modification in nature. Although carbohydrate modification of protein antigens from many microbial pathogens constitutes important components of B cell epitopes, the role in T cell immunity is not completely understood. There is growing evidence about the importance of these modifications in host bacteria interactions in tuberculosis. It is known, that the sugars present in some Mycobacterium tuberculosis glycoproteins play an important role in both humoral and cellular immune response against the pathogen. Since this modification is lost in the recombinant proteins expressed in Escherichia coli, it is fundamental to search for host bacteria with the capacity to modify the foreign proteins. Amongst the bacteria that are likely to have this possibility are some members of Rhodococcus genus which are Gram-positive bacteria, with high GC-content and genetically very close related to M. tuberculosis. Results: In this work, apa, pstS1 and lprG genes that coding for M. tuberculosis glycoproteins were cloned and expressed in Rhodococcus erythropolis. All recombinant proteins were mannosylated as demonstrated by their interaction with mannose binding lectin Concanavalin A. In addition, as native proteins recombinants Apa and PstS1 were secreted to the culture medium in contrast with LprG that was retained in the cell wall. Conclusions: Together these results, point out R. erythropolis, as a new host for expression of M. tuberculosis glycoproteins. © 2017 The Author(s).

Filiaciones:
Vallecillo, Antonio J.:
 Univ Nacl Autonoma Mexico, Inst Invest Biomed, Dept Inmunol, Mexico City 04510, DF, Mexico

 Univ Cuenca, Escuela Med Vet & Zootecnia, Fac Ciencias Agr, Cuenca 010220, Azu, Ecuador

Parada, Cristina:
 Univ Nacl Autonoma Mexico, Inst Invest Biomed, Dept Inmunol, Mexico City 04510, DF, Mexico

Morales, Pedro:
 Univ Nacl Autonoma Mexico, Inst Invest Biomed, Dept Inmunol, Mexico City 04510, DF, Mexico

Espitia, Clara:
 Univ Nacl Autonoma Mexico, Inst Invest Biomed, Dept Inmunol, Mexico City 04510, DF, Mexico
ISSN: 14752859
Editorial
BIOMED CENTRAL LTD, 236 GRAYS INN RD, FLOOR 6, LONDON WC1X 8HL, ENGLAND, Reino Unido
Tipo de documento: Article
Volumen: 16 Número: 1
Páginas:
WOS Id: 000397717300001
ID de PubMed: 28103877