Literature DB >> 21786423

Bacterial display in combinatorial protein engineering.

John Löfblom1.   

Abstract

Technologies for display of recombinant protein libraries are today essential tools in many research-intensive fields, such as in the drug discovery processes of biopharmaceutical development. Phage display is still the most widely used method, but alternative systems are available and are becoming increasingly popular. The most rapidly expanding of the alternative systems are the cell display-based technologies, offering innovative strategies for selection and characterization of affinity proteins. Most investigations have focused on eukaryotic yeast for display of protein libraries, but similar systems are also being developed using prokaryotic hosts. This review summarizes the field of bacterial surface display with a strong emphasis on library applications for generation of new affinity proteins. The main focus will be on the most recent progress of the work on primarily Escherichia coli, but also on studies using a recently developed system for display on Gram-positive Staphylococcus carnosus. In addition, general strategies for combinatorial protein engineering using cell display are discussed along with the latest developments of new methodologies with comparisons to mainly phage display technology.
Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

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Year:  2011        PMID: 21786423     DOI: 10.1002/biot.201100129

Source DB:  PubMed          Journal:  Biotechnol J        ISSN: 1860-6768            Impact factor:   4.677


  29 in total

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Authors:  Frédéric Ducancel; Bruno H Muller
Journal:  MAbs       Date:  2012-07-01       Impact factor: 5.857

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Review 3.  Synthetic biology of antimicrobial discovery.

Authors:  Bijan Zakeri; Timothy K Lu
Journal:  ACS Synth Biol       Date:  2012-12-04       Impact factor: 5.110

4.  Evaluation of Nanobody Conjugates and Protein Fusions as Bioanalytical Reagents.

Authors:  Virginia J Bruce; Brian R McNaughton
Journal:  Anal Chem       Date:  2017-03-20       Impact factor: 6.986

5.  Surface display of a single-domain antibody library on Gram-positive bacteria.

Authors:  Filippa Fleetwood; Nick Devoogdt; Mireille Pellis; Ulrich Wernery; Serge Muyldermans; Stefan Ståhl; John Löfblom
Journal:  Cell Mol Life Sci       Date:  2012-10-13       Impact factor: 9.261

6.  Cell surface display of cold-active esterase EstPc with the use of a new autotransporter from Psychrobacter cryohalolentis K5(T).

Authors:  L E Petrovskaya; K A Novototskaya-Vlasova; E A Kryukova; E M Rivkina; D A Dolgikh; M P Kirpichnikov
Journal:  Extremophiles       Date:  2014-09-25       Impact factor: 2.395

7.  Identification of novel proteins binding the AU-rich element of α-prothymosin mRNA through the selection of open reading frames (RIDome).

Authors:  Laura Patrucco; Clelia Peano; Andrea Chiesa; Filomena Guida; Imma Luisi; Ilenia Boria; Flavio Mignone; Gianluca De Bellis; Silvia Zucchelli; Stefano Gustincich; Claudio Santoro; Daniele Sblattero; Diego Cotella
Journal:  RNA Biol       Date:  2015       Impact factor: 4.652

8.  Fusion with the cold-active esterase facilitates autotransporter-based surface display of the 10th human fibronectin domain in Escherichia coli.

Authors:  L E Petrovskaya; A V Zlobinov; L N Shingarova; E F Boldyreva; S Sh Gapizov; K A Novototskaya-Vlasova; E M Rivkina; D A Dolgikh; M P Kirpichnikov
Journal:  Extremophiles       Date:  2017-12-18       Impact factor: 2.395

9.  Antibody VH and VL recombination using phage and ribosome display technologies reveals distinct structural routes to affinity improvements with VH-VL interface residues providing important structural diversity.

Authors:  Maria A T Groves; Lily Amanuel; Jamie I Campbell; D Gareth Rees; Sudharsan Sridharan; Donna K Finch; David C Lowe; Tristan J Vaughan
Journal:  MAbs       Date:  2014 Jan-Feb       Impact factor: 5.857

Review 10.  Engineered Autonomous Human Variable Domains.

Authors:  Johan Nilvebrant; Peter M Tessier; Sachdev S Sidhu
Journal:  Curr Pharm Des       Date:  2016       Impact factor: 3.116

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