Publication Date:
2016-03-13
Description:
We previously reported that the β-1,4-Mannanase ( manB ) gene from Bacillus pumilus functions as a good reporter gene in Lactobacillus casei . Two vectors were constructed. One carries the signal peptide of secretion protein Usp45 (SP Usp45 ) from Lactococcus lactis (pELSH), and the other carries the full-length S-layer protein, SlpA, from L. acidophilus (pELWH). In this work, another vector, pELSPH, was constructed to include the signal peptide of protein SlpA (SP SlpA ), and the capacity of all three vectors to drive expression of the manB gene in L. casei was evaluated. The results showed that SP Usp45 is functionally recognized and processed by the L. casei secretion machinery. The SP Usp45 -mediated secretion efficiency was ~87%, and SP SlpA drove the export of secreted ManB with ~80% efficiency. SP SlpA secretion was highly efficient, and expressed SlpA was anchored to the cell wall by an unknown secretion mechanism. Full-length SlpA drove the cell wall-anchored expression of an SlpA-ManB fusion protein but at a much lower level than that of protein SlpA.
Keywords:
Biotechnology & Synthetic Biology
Print ISSN:
0378-1097
Electronic ISSN:
1574-6968
Topics:
Biology
