Construction of vectors to produce recombinant M. bovis-BCG to enhance the vaccine protection against tuberculosis. (144.27)
| Autor: | Lorena Santos, Don Estes, Andre Kipnis, Ana Paula Kipnis |
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| Rok vydání: | 2010 |
| Předmět: | |
| Zdroj: | The Journal of Immunology. 184:144.27-144.27 |
| ISSN: | 1550-6606 0022-1767 |
| Popis: | A third of the world’s population is exposed to the risk of tuberculosis (TB). The only currently available vaccine against TB is the Bacillus Calmette-Guerin (BCG). Development of a more effective vaccine has been considered as a major international public health priority. Some proteins from M. tuberculosis have been shown to be recognized by the immune system and can be correlated with protection against tuberculosis. The aim of this work was to design a recombinant fusion protein to use as subunit vaccine candidates against M. tuberculosis. We used epitopes of three different proteins as Ag85A, MPT-51 and Hsp-X based on their reported antigenicity. The corresponding gene segment of each epitope were cloned into pGEM-T Easy in fusion, and subcloned into the mycobacterial expression vectors, (pLA71, pLA73 and pMIP12). These vectors contain the E. coli and mycobacterial origins of replication and a multicloning site which places the heterologous gene in fusion with the signal sequence or the whole β-lactamase-encoding gene in pLA71 and pLA73, respectively. pMIP12 has a conserved mycobacterial Shine-Dalgarno sequence that may elevate antigen expression, and the native gene is expressed intracellularly. The recombinant plasmids for the development of recombinant BCG vaccine were produced and are now being tested for the fusion protein expression. |
| Databáze: | OpenAIRE |
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