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Autotransporter-Mediated Display of a Naive Affibody Library on the Outer Membrane of Escherichia coli
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Protein Science.
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Protein Science.
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Protein Science.ORCID iD: 0000-0002-9282-0174
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Protein Science.ORCID iD: 0000-0001-9423-0541
2019 (English)In: Biotechnology Journal, ISSN 1860-6768, E-ISSN 1860-7314, Vol. 14, no 4, article id 1800359Article in journal (Refereed) Published
Abstract [en]

Development of new affinity proteins using combinatorial protein engineering is today established for generation of monoclonal antibodies and also essential for discovery of binders that are based on non-immunoglobulin proteins. Phage display is most frequently used, but yeast display is becoming increasingly popular, partly due to the option of utilizing fluorescence-activated cell sorting (FACS) for isolation of new candidates. Escherichia coli has several valuable properties for library applications and in particular the high transformation efficiency. The use of various autotransporters and intimins for secretion and anchoring on the outer membrane have shown promising results and particularly for directed evolution of different enzymes. Here, the authors report on display of a large naive affibody library on the outer membrane of E. coli using the autotransporter Adhesin Involved in Diffuse Adherence (AIDA-I). The expression cassette is first engineered by removing non-essential sequences, followed by introduction of an affibody library, comprising more than 10(9) variants, into the new display vector. The quality of the library and general performance of the method is assessed by FACS against five different targets, which resulted in a panel of binders with down to nanomolar affinities, suggesting that the method has potential as a complement to phage display for generation of affibody molecules.

Place, publisher, year, edition, pages
WILEY-V C H VERLAG GMBH , 2019. Vol. 14, no 4, article id 1800359
Keywords [en]
affibody library, AIDA-I, autodisplay, bacterial display, directed evolution
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:kth:diva-249806DOI: 10.1002/biot.201800359ISI: 000462917100020PubMedID: 30179307Scopus ID: 2-s2.0-85053871994OAI: oai:DiVA.org:kth-249806DiVA, id: diva2:1306279
Note

QC 20190423

Available from: 2019-04-23 Created: 2019-04-23 Last updated: 2019-04-23Bibliographically approved

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Andersson, Ken G.Ståhl, StefanLöfblom, John

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