Proceedings of the 2016 International Conference on Biological Sciences and Technology

Investigation of Listeria Phage Endolysin Cell-wall Binding Domain (CBD) Surface Display in Escherichia coli

Authors
Shan-Na Liu, Timo M. Takala, Justus Reunanen, Ossian Saris, Per E. J. Saris
Corresponding Author
Shan-Na Liu
Available Online January 2016.
DOI
https://doi.org/10.2991/bst-16.2016.6How to use a DOI?
Keywords
Listeria phage, Endolysin, Cell-wall binding domain (CBD), Surface display.
Abstract
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.

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Proceedings
The International Conference on Biological Sciences and Technology
Part of series
Advances in Biological Sciences Research
Publication Date
January 2016
ISBN
978-94-6252-161-2
ISSN
2468-5747
DOI
https://doi.org/10.2991/bst-16.2016.6How to use a DOI?
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  -