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Development of a Novel Cell Surface Attachment System to Display Multi-Protein Complex Using the Cohesin-Dockerin Binding Pair

Authors
Ko, Hyeok-JinSong, HeesangChoi, In-Geol
Issue Date
8월-2021
Publisher
KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY
Keywords
Escherichia coli cell surface attachment; alpha-neoagarobiose hydrolase; cohesin-dockerin; non-covalent interaction module
Citation
JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.31, no.8, pp.1183 - 1189
Indexed
SCIE
SCOPUS
KCI
Journal Title
JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
Volume
31
Number
8
Start Page
1183
End Page
1189
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/136999
DOI
10.4014/jmb.2105.05022
ISSN
1017-7825
Abstract
Autodisplay of a multimeric protein complex on a cell surface is limited by intrinsic factors such as the types and orientations of anchor modules. Moreover, improper folding of proteins to be displayed often hinders functional cell surface display. While overcoming these drawbacks, we ultimately extended the applicability of the autodisplay platform to the display of a protein complex. We designed and constructed a cell surface attachment (CSA) system that uses a non-covalent protein-protein interaction. We employed the high-affinity interaction mediated by an orthogonal cohesin-dockerin (Coh-Doc) pair from Archaeoglobus fulgidus to build the CSA system. Then, we validated the orthogonal Coh-Doc binding by attaching a monomeric red fluorescent protein to the cell surface. In addition, we evaluated the functional anchoring of proteins fused with the Doc module to the autodisplayed Coh module on the surface of Escherichia coli. The designed CSA system was applied to create a functional attachment of dimeric alpha-neoagarobiose hydrolase to the surface of E. coli cells.
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