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

DOI

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.

Copyright

© 2016, the Authors. Published by Atlantis Press.

Open Access

This is an open access article distributed under the CC BY-NC license (http://creativecommons.org/licenses/by-nc/4.0/).

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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  - Proceedings of the 2016 International Conference on Biological Sciences and Technology
PB  - Atlantis Press
SP  - 23
EP  - 28
SN  - 2468-5747
UR  - https://doi.org/10.2991/bst-16.2016.6
DO  - 10.2991/bst-16.2016.6
ID  - Liu2016/01
ER  -