Investigation of Listeria Phage Endolysin Cell-wall Binding Domain (CBD) Surface Display in Escherichia coli
- Shan-Na Liu, Timo M. Takala, Justus Reunanen, Ossian Saris, Per E. J. Saris
- Corresponding Author
- Shan-Na Liu
Available Online January 2016.
- https://doi.org/10.2991/bst-16.2016.6How to use a DOI?
- Listeria phage, Endolysin, Cell-wall binding domain (CBD), Surface display.
- Cell surface display of target proteins has been widely used in biotechnology and industry. In this study, cell-wall binding domain (CBD) from Listeria phage endolysin A500 was fused with anchoring domains of YadA and OmpA, respectively, in Escherichia coli, aiming at binding of E. coli cells to Listeria cells. The fusion proteins were expressed after induction and their surface localizations were verified by Western blot. CBD-YadA fusion was displayed on the cell surface, however, was toxic to E. coli. OmpA-CBD fusion was translocated to the outer layer of the cell membrane but with compromised availability on the cell surface. Therefore, functional surface display of CBD in E. coli requires another anchor for fusion strategy.
- Open Access
- This is an open access article distributed under the CC BY-NC license.
Cite this article
TY - CONF AU - Shan-Na Liu AU - Timo M. Takala AU - Justus Reunanen AU - Ossian Saris AU - Per E. J. Saris PY - 2016/01 DA - 2016/01 TI - Investigation of Listeria Phage Endolysin Cell-wall Binding Domain (CBD) Surface Display in Escherichia coli BT - The International Conference on Biological Sciences and Technology PB - Atlantis Press SN - 2468-5747 UR - https://doi.org/10.2991/bst-16.2016.6 DO - https://doi.org/10.2991/bst-16.2016.6 ID - Liu2016/01 ER -