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Journal articles on the topic 'Protein display'

Author: Grafiati

Published: 28 May 2022

Last updated: 30 July 2025

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1

Wen, Fei, Dhruv K. Sethi, Kai W. Wucherpfennig, and Huimin Zhao. "Cell surface display of functional human MHC class II proteins: yeast display versus insect cell display." Protein Engineering, Design and Selection 24, no. 9 (2011): 701–9. http://dx.doi.org/10.1093/protein/gzr035.

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2

Rice, Jeffrey J., and Patrick S. Daugherty. "Directed evolution of a biterminal bacterial display scaffold enhances the display of diverse peptides." Protein Engineering, Design and Selection 21, no. 7 (2008): 435–42. http://dx.doi.org/10.1093/protein/gzn020.

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3

He, M. "Ribosome display: Cell-free protein display technology." Briefings in Functional Genomics and Proteomics 1, no. 2 (2002): 204–12. http://dx.doi.org/10.1093/bfgp/1.2.204.

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4

Kościelska, K., L. Kiczak, M. Kasztura, O. Wesołowska, and J. Otlewski. "Phage display of proteins." Acta Biochimica Polonica 45, no. 3 (1998): 705–20. http://dx.doi.org/10.18388/abp.1998_4210.

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In recent years the phage display approach has become an increasingly popular method in protein research. This method enables the presentation of large peptide and protein libraries on the surface of phage particles from which molecules of desired functional property(ies) can be rapidly selected. The great advantage of this method is a direct linkage between an observed phenotype and encapsulated genotype, which allows fast determination of selected sequences. The phage display approach is a powerful tool in generating highly potent biomolecules, including: search for specific antibodies, dete

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5

Schimmele, Bernhard, Nico Gräfe, and Andreas Plückthun. "Ribosome display of mammalian receptor domains." Protein Engineering, Design and Selection 18, no. 6 (2005): 285–94. http://dx.doi.org/10.1093/protein/gzi030.

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6

Van Deventer, James A., Ryan L. Kelly, Saravanan Rajan, K. Dane Wittrup, and Sachdev S. Sidhu. "A switchable yeast display/secretion system." Protein Engineering Design and Selection 28, no. 10 (2015): 317–25. http://dx.doi.org/10.1093/protein/gzv043.

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7

Petrenko, V. A., G. P. Smith, M. M. Mazooji та T. Quinn. "α-Helically constrained phage display library". Protein Engineering, Design and Selection 15, № 11 (2002): 943–50. http://dx.doi.org/10.1093/protein/15.11.943.

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8

Daugherty, P. S., G. Chen, M. J. Olsen, B. L. Iverson, and G. Georgiou. "Antibody affinity maturation using bacterial surface display." Protein Engineering Design and Selection 11, no. 9 (1998): 825–32. http://dx.doi.org/10.1093/protein/11.9.825.

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9

Grage, Katrin, Verena Peters, and Bernd H. A. Rehm. "Recombinant Protein Production byIn VivoPolymer Inclusion Display." Applied and Environmental Microbiology 77, no. 18 (2011): 6706–9. http://dx.doi.org/10.1128/aem.05953-11.

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ABSTRACTA novel approach to produce purified recombinant proteins was established. The target protein is produced as polyhydroxyalkanoate (PHA) synthase fusion protein, which mediates intracellular formation of PHA inclusions displaying the target protein. After isolation of the PHA inclusions, the pure target protein was released by simple enterokinase digestion.

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10

Zahn, G., A. Skerra, and W. Höhne. "Investigation of a tetracycline-regulated phage display system." Protein Engineering, Design and Selection 12, no. 12 (1999): 1031–34. http://dx.doi.org/10.1093/protein/12.12.1031.

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11

Sidhu, Sachdev S., Wayne J. Fairbrother, and Kurt Deshayes. "Exploring Protein-Protein Interactions with Phage Display." ChemBioChem 4, no. 1 (2003): 14–25. http://dx.doi.org/10.1002/cbic.200390008.

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12

Santiago Vispo, Nelson. "Covalent Peptide Evolution: Redefining Protein–Protein Interaction Inhibition Through Phage Display." Bionatura Journal 2, no. 2 (2025): 1–5. https://doi.org/10.70099/bj/2025.02.02.16.

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Covalent cyclic peptides represent a transformative approach for targeting challenging protein-protein interactions (PPIs) characterized by flat, extensive binding surfaces. Recent advances in electrophilic phage display now enable the evolution of these peptides through integrating sulfur(VI) fluoride exchange (SuFEx) chemistry with functional selection strategies. This innovative platform combines genetic encoding with site-specific cyclization and warhead incorporation to generate high-affinity, irreversible binders. When targeting the SARS-CoV-2 Spike-ACE2 interface, the approach produced

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13

Hossain, SK Amir, SM Rifat Rahman, Toufiq Ahmed, and Chanchal Mandal. "An overview of yeast cell wall proteins and their contribution in yeast display system." Asian Journal of Medical and Biological Research 5, no. 4 (2020): 246–57. http://dx.doi.org/10.3329/ajmbr.v5i4.45261.

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Yeast surface display has become an increasingly popular tool for protein engineering and library screening applications. Although, recent advances have greatly expanded the capability of yeast surface display, the protein display system is still far away from industrial application. One of the major components of a stable, efficient and successful yeast surface display system is cell wall anchor protein with which our desired foreign protein will be attached. We studied 80 different yeast cell wall anchored proteins originated mostly from Saccharomyces cerevisiae and Candida albicans. We stud

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14

Chikaev, A. N., A. P. Rudometov, Yu A. Merkulyeva, and L. I. Karpenko. "Phage display as a tool for identifying HIV-1 broadly neutralizing antibodies." Vavilov Journal of Genetics and Breeding 25, no. 5 (2021): 562–72. http://dx.doi.org/10.18699/vj21.063.

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Combinatorial biology methods offer a good solution for targeting interactions of specific molecules by a high-throughput screening and are widely used for drug development, diagnostics, identification of novel monoclonal antibodies, search for linear peptide mimetics of discontinuous epitopes for the development of immunogens or vaccine components. Among all currently available techniques, phage display remains one of the most popular approaches. Despite being a fairly old method, phage display is still widely used for studying protein-protein, peptide-protein and DNA-protein interactions due

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15

Dai, M., J. Temirov, E. Pesavento, et al. "Using T7 phage display to select GFP-based binders." Protein Engineering Design and Selection 21, no. 7 (2008): 413–24. http://dx.doi.org/10.1093/protein/gzn016.

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16

Kenrick, S. A., and P. S. Daugherty. "Bacterial display enables efficient and quantitative peptide affinity maturation." Protein Engineering Design and Selection 23, no. 1 (2009): 9–17. http://dx.doi.org/10.1093/protein/gzp065.

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17

Sarhan, Mohammed. "Ice nucleation protein as a bacterial surface display protein." Archives of Biological Sciences 63, no. 4 (2011): 943–48. http://dx.doi.org/10.2298/abs1104943s.

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Surface display technology can be defined as that phenotype (protein or peptide) which is linked to a genotype (DNA or RNA) through an appropriate anchoring motif. A bacterial surface display system is based on expressing recombinant proteins fused to sorting signals (anchoring motifs) that direct their incorporation on the cell surface.

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18

Grabherr, Reingard, and Wolfgang Ernst. "Baculovirus for Eukaryotic Protein Display." Current Gene Therapy 10, no. 3 (2010): 195–200. http://dx.doi.org/10.2174/156652310791321297.

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19

Daugherty, Patrick S. "Protein engineering with bacterial display." Current Opinion in Structural Biology 17, no. 4 (2007): 474–80. http://dx.doi.org/10.1016/j.sbi.2007.07.004.

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20

Chakravarty, Suvobrata, Nivedita Mitra, Iris Queitsch, Avadhesha Surolia, Raghavan Varadarajan, and Stefan Dübel. "Protein stabilization through phage display." FEBS Letters 476, no. 3 (2000): 296–300. http://dx.doi.org/10.1016/s0014-5793(00)01725-7.

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21

Hoess, Ronald H. "Protein Design and Phage Display." Chemical Reviews 101, no. 10 (2001): 3205–18. http://dx.doi.org/10.1021/cr000056b.

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22

Mullaney, Brian P., and Maria G. Pallavicini. "Protein-protein interactions in hematology and phage display." Experimental Hematology 29, no. 10 (2001): 1136–46. http://dx.doi.org/10.1016/s0301-472x(01)00693-2.

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23

Wentz, Alane E., and Eric V. Shusta. "A Novel High-Throughput Screen Reveals Yeast Genes That Increase Secretion of Heterologous Proteins." Applied and Environmental Microbiology 73, no. 4 (2006): 1189–98. http://dx.doi.org/10.1128/aem.02427-06.

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ABSTRACT The yeast Saccharomyces cerevisiae is an attractive host for the production of heterologous proteins. However, low-yield production of many proteins (from micrograms to milligrams/liter) leaves considerable room for optimization. By engineering the yeast cell via traceable genome-wide libraries, genes that can enhance protein expression level because of their roles in protein transcription, translation, folding, and trafficking processes can be readily identified. This report details a novel approach that combines yeast cDNA overexpression libraries with yeast surface display to allow

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24

Berntzen, G., O. H. Brekke, S. A. Mousavi та ін. "Characterization of an FcγRI-binding peptide selected by phage display". Protein Engineering, Design and Selection 19, № 3 (2006): 121–28. http://dx.doi.org/10.1093/protein/gzj011.

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25

Bertschinger, Julian, Dragan Grabulovski, and Dario Neri. "Selection of single domain binding proteins by covalent DNA display." Protein Engineering, Design and Selection 20, no. 2 (2007): 57–68. http://dx.doi.org/10.1093/protein/gzl055.

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26

Dudgeon, K., R. Rouet, and D. Christ. "Rapid prediction of expression and refolding yields using phage display." Protein Engineering Design and Selection 26, no. 10 (2013): 671–74. http://dx.doi.org/10.1093/protein/gzt019.

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27

Hirose, M., T. Hayano, H. Shirai, H. Nakamura, and M. Kikuchi. "Isolation of anti-glutathione antibodies from a phage display library." Protein Engineering Design and Selection 11, no. 3 (1998): 243–48. http://dx.doi.org/10.1093/protein/11.3.243.

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28

Lipovsek, Dasa, and Andreas Plückthun. "In-vitro protein evolution by ribosome display and mRNA display." Journal of Immunological Methods 290, no. 1-2 (2004): 51–67. http://dx.doi.org/10.1016/j.jim.2004.04.008.

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29

Wendel, Sofie, Emil C. Fischer, Virginia Martínez, Susanna Seppälä, and Morten H. H. Nørholm. "A nanobody:GFP bacterial platform that enables functional enzyme display and easy quantification of display capacity." Microbial Cell Factories 15, no. 1 (2016): 71. https://doi.org/10.1186/s12934-016-0474-y.

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<strong>Background: </strong>Bacterial surface display is an attractive technique for the production of cell-anchored, functional proteins and engineering of whole-cell catalysts. Although various outer membrane proteins have been used for surface display, an easy and versatile high-throughput-compatible assay for evaluating and developing surface display systems is missing.<strong>Results: </strong>Using a single domain antibody (also called nanobody) with high affinity for green fluorescent protein (GFP), we constructed a system that allows for fast, fluorescence-based detection of displayed

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30

Ko, Hyeok-Jin, Eunhye Park, Joseph Song, et al. "Functional Cell Surface Display and Controlled Secretion of Diverse Agarolytic Enzymes by Escherichia coli with a Novel Ligation-Independent Cloning Vector Based on the Autotransporter YfaL." Applied and Environmental Microbiology 78, no. 9 (2012): 3051–58. http://dx.doi.org/10.1128/aem.07004-11.

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ABSTRACTAutotransporters have been employed as the anchoring scaffold for cell surface display by replacing their passenger domains with heterologous proteins to be displayed. We adopted an autotransporter (YfaL) ofEscherichia colifor the cell surface display system. The critical regions in YfaL for surface display were identified for the construction of a ligation-independent cloning (LIC)-based display system. The designed system showed no detrimental effect on either the growth of the host cell or overexpressing heterologous proteins on the cell surface. We functionally displayed monomeric

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31

Lajoie, Jason M., Yong Ku Cho, Dustin Frost, Samantha Bremner, Lingjun Li, and Eric V. Shusta. "A yeast display immunoprecipitation screen for targeted discovery of antibodies against membrane protein complexes." Protein Engineering, Design and Selection 32, no. 5 (2019): 219–30. http://dx.doi.org/10.1093/protein/gzz035.

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Abstract Yeast display immunoprecipitation is a combinatorial library screening platform for the discovery and engineering of antibodies against membrane proteins using detergent-solubilized membrane fractions or cell lysates as antigen sources. Here, we present the extension of this method for the screening of antibodies that bind to membrane protein complexes, enabling discovery of antibodies that target antigens involved in a functional protein-protein interaction of interest. For this proof-of-concept study, we focused on the receptor-mediated endocytosis machinery at the blood-brain barri

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32

Koh, Darius Wen-Shuo, Jian-Hua Tay, and Samuel Ken-En Gan. "Engineering Ag43 Signal Peptides with Bacterial Display and Selection." Methods and Protocols 6, no. 1 (2022): 1. http://dx.doi.org/10.3390/mps6010001.

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Protein display, secretion, and export in prokaryotes are essential for utilizing microbial systems as engineered living materials, medicines, biocatalysts, and protein factories. To select for improved signal peptides for Escherichia coli protein display, we utilized error-prone polymerase chain reaction (epPCR) coupled with single-cell sorting and microplate titer to generate, select, and detect improved Ag43 signal peptides. Through just three rounds of mutagenesis and selection using green fluorescence from the 56 kDa sfGFP-beta-lactamase, we isolated clones that modestly increased surface

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33

Bessette, Paul H., Jeffrey J. Rice, and Patrick S. Daugherty. "Rapid isolation of high-affinity protein binding peptides using bacterial display." Protein Engineering, Design and Selection 17, no. 10 (2004): 731–39. http://dx.doi.org/10.1093/protein/gzh084.

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34

Ja, William W., Brett N. Olsen, and Richard W. Roberts. "Epitope mapping using mRNA display and a unidirectional nested deletion library." Protein Engineering, Design and Selection 18, no. 7 (2005): 309–19. http://dx.doi.org/10.1093/protein/gzi038.

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35

Park, Sheldon, Yao Xu, Xiaoran Fu Stowell, Feng Gai, Jeffery G. Saven, and Eric T. Boder. "Limitations of yeast surface display in engineering proteins of high thermostability." Protein Engineering, Design and Selection 19, no. 5 (2006): 211–17. http://dx.doi.org/10.1093/protein/gzl003.

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36

Koide, A., J. Wojcik, R. N. Gilbreth, A. Reichel, J. Piehler, and S. Koide. "Accelerating phage-display library selection by reversible and site-specific biotinylation." Protein Engineering Design and Selection 22, no. 11 (2009): 685–90. http://dx.doi.org/10.1093/protein/gzp053.

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37

Pavoor, T. V., J. A. Wheasler, V. Kamat, and E. V. Shusta. "An enhanced approach for engineering thermally stable proteins using yeast display." Protein Engineering Design and Selection 25, no. 10 (2012): 625–30. http://dx.doi.org/10.1093/protein/gzs041.

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38

Stafford, R. L., M. L. Matsumoto, G. Yin, et al. "In vitro Fab display: a cell-free system for IgG discovery." Protein Engineering Design and Selection 27, no. 4 (2014): 97–109. http://dx.doi.org/10.1093/protein/gzu002.

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39

Rossmann, Maxim, Sandra J. Greive, Tommaso Moschetti, Michael Dinan, and Marko Hyvönen. "Development of a multipurpose scaffold for the display of peptide loops." Protein Engineering, Design and Selection 30, no. 6 (2017): 419–30. http://dx.doi.org/10.1093/protein/gzx017.

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40

Dall'Acqua, William, Cornelia Halin, Maria L. Rodrigues, and Paul Carter. "Elastase substrate specificity tailored through substrate-assisted catalysis and phage display." Protein Engineering, Design and Selection 12, no. 11 (1999): 981–87. http://dx.doi.org/10.1093/protein/12.11.981.

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41

Davidson, Thomas A., Samantha J. McGoldrick, and David H. Kohn. "Phage Display to Augment Biomaterial Function." International Journal of Molecular Sciences 21, no. 17 (2020): 5994. http://dx.doi.org/10.3390/ijms21175994.

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Biomaterial design relies on controlling interactions between materials and their biological environments to modulate the functions of proteins, cells, and tissues. Phage display is a powerful tool that can be used to discover peptide sequences with high affinity for a desired target. When incorporated into biomaterial design, peptides identified via phage display can functionalize material surfaces to control the interaction between a biomaterial and its local microenvironment. A targeting peptide has high specificity for a given target, allowing for homing a specific protein, cell, tissue, o

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42

Rosander, Anna, Lars Frykberg, Nora Ausmees, and Peter Müller. "Identification of Extracytoplasmic Proteins in Bradyrhizobium japonicum Using Phage Display." Molecular Plant-Microbe Interactions® 16, no. 8 (2003): 727–37. http://dx.doi.org/10.1094/mpmi.2003.16.8.727.

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A novel gene bank of Bradyrhizobium japonicum USDA110spc4 was constructed using pG3DSS, a phagemid vector designed for detecting genes encoding secreted proteins. In this phagemid, the phage protein III lacks its indigenous signal peptide required for protein secretion, thus recombinant fusion proteins are displayed on the phage surface only if a functional signal peptide is provided by an inserted DNA fragment. In addition, the N-terminal half of protein III has been replaced by a short linker region (the E-tag) that is recognized by a monoclonal antibody, which enables isolation of phages di

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43

Fryszczyn, Bartlomiej G., Nicholas G. Brown, Wanzhi Huang, Miriam A. Balderas, and Timothy Palzkill. "Use of periplasmic target protein capture for phage display engineering of tight-binding protein–protein interactions." Protein Engineering, Design and Selection 24, no. 11 (2011): 819–28. http://dx.doi.org/10.1093/protein/gzr043.

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44

Wittrup, K. Dane. "Protein engineering by cell-surface display." Current Opinion in Biotechnology 12, no. 4 (2001): 395–99. http://dx.doi.org/10.1016/s0958-1669(00)00233-0.

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45

Gera, Nimish, Mahmud Hussain, and Balaji M. Rao. "Protein selection using yeast surface display." Methods 60, no. 1 (2013): 15–26. http://dx.doi.org/10.1016/j.ymeth.2012.03.014.

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46

DeWitt, Natalie. "Mapping protein interactions by phage display." Nature Biotechnology 17, no. 12 (1999): 1150. http://dx.doi.org/10.1038/70682.

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47

Löfblom, John. "Bacterial display in combinatorial protein engineering." Biotechnology Journal 6, no. 9 (2011): 1115–29. http://dx.doi.org/10.1002/biot.201100129.

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48

Speck, J., K. M. Arndt, and K. M. Muller. "Efficient phage display of intracellularly folded proteins mediated by the TAT pathway." Protein Engineering Design and Selection 24, no. 6 (2011): 473–84. http://dx.doi.org/10.1093/protein/gzr001.

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49

Rakestraw, J. A., D. Aird, P. M. Aha, B. M. Baynes, and D. Lipovsek. "Secretion-and-capture cell-surface display for selection of target-binding proteins." Protein Engineering Design and Selection 24, no. 6 (2011): 525–30. http://dx.doi.org/10.1093/protein/gzr008.

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50

Ganesan, R., Y. Zhang, K. E. Landgraf, S. J. Lin, P. Moran, and D. Kirchhofer. "An allosteric anti-hepsin antibody derived from a constrained phage display library." Protein Engineering Design and Selection 25, no. 3 (2012): 127–33. http://dx.doi.org/10.1093/protein/gzr067.

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