Part:BBa_K4817004:Design
OmpA-Bac
- 10COMPATIBLE WITH RFC[10]
- 12INCOMPATIBLE WITH RFC[12]Illegal NheI site found at 64
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Design Notes
This part is composed of the signal peptide OmpA from Escherichia coli and the antibacterial peptide Bactenecin from bovine neutrophils. The antibacterial peptide Bactenecin has an inhibitory effect on Gram negative bacteria such as sulfate reducing bacteria[1],[2]. The signal peptide OmpA can transport the antibacterial peptide to the extracellular space[3], and the two parts are connected by amino acids A-S-A, which is the cleavage site of the signal peptidase, allowing the antibacterial peptide to be cut off from the fusion protein without affecting its original function. We have our engineered Escherichia coli express the OmpA-Bac fusion protein to inhibit the growth of sulfate reducing bacteria in the sewer.
Source
Bovine neutrophils Escherichia coli
References
1. Stillger, L., Viau, L., Kamm, L., Holtmann, D. & Müller, D. Optimization of antimicrobial peptides for the application against biocorrosive bacteria. Appl Microbiol Biotechnol 107, 4041–4049 (2023).
2. Jayaraman, A., Mansfeld, F. B. & Wood, T. K. Inhibiting sulfate-reducing bacteria in biofilms by expressing the antimicrobial peptides indolicidin and bactenecin. Journal of Industrial Microbiology and Biotechnology 22, 167–175 (1999).
3. Pechsrichuang, P. et al. OmpA signal peptide leads to heterogenous secretion of B. subtilis chitosanase enzyme from E. coli expression system. SpringerPlus 5, 1200 (2016).