Part:BBa_K5403003

N-terminal signal sequence of OmpA

The outer membrane protein A (OmpA) is found in E. coli and has been used as an anchor to attach other proteins to the membrane exterior by recombinant expression (Beck et al., 2017). A protein of interest can be attached to the C-terminus of OmpA, (see composite part BBa_5403013). Part BBa_K5403002 is used as a flexible linker in between the two proteins that make up the fusion protein. However, it is known that the 21 N-terminal amino acids of OmpA make up the signal sequence that is responsible for the trafficking to the cell membrane and anchoring (Movva et al., 1980). In hypothesis, this signal sequence would be sufficient for the anchoring of a protein of interest in the membrane. Therefore, this basic part was constructed, containing only the signal sequence of OmpA, as a basis for fusion proteins with proteins that one wishes to anchor into the outer membrane of e. coli. Composite part BBa_K5403012 was constructed using this basic part and GFP as the protein of interest.

References

Beck, B. R., Lee, S. H., Kim, D., Park, J. H., Lee, H. K., Kwon, S., Lee, K. H., Lee, J. I., & Song, S. K. (2017). A Lactococcus lactis BFE920 feed vaccine expressing a fusion protein composed of the OmpA and FlgD antigens from Edwardsiella tarda was significantly better at protecting olive flounder (Paralichthys olivaceus) from edwardsiellosis than single antigen vaccines. Fish & Shellfish Immunology, 68, 19–28. https://doi.org/10.1016/j.fsi.2017.07.004

Movva, N.R. et al. (1980) Amino acid sequence of the signal peptide of ompA protein, a major outer membrane protein of Escherichia coli. (1980, 10 januari). PubMed. https://pubmed.ncbi.nlm.nih.gov/6985608/