scholarly journals Phage Display Technology as a Powerful Platform for Antibody Drug Discovery

Viruses ◽  
2021 ◽  
Vol 13 (2) ◽  
pp. 178
Author(s):  
Kazuya Nagano ◽  
Yasuo Tsutsumi

Antibody drugs with a high affinity and specificity are effective and safe for intractable diseases, such as cancers and autoimmune diseases. Furthermore, they have played a central role in drug discovery, currently accounting for eight of the top 20 pharmaceutical products worldwide by sales. Forty years ago, clinical trials on antibody drugs that were thought to be a magic bullet failed, partly due to the immunogenicity of monoclonal antibodies produced in mice. The recent breakthrough in antibody drugs is largely because of the contribution of phage display technology. Here, we reviewed the importance of phage display technology as a powerful platform for antibody drug discovery from various perspectives, such as the development of human monoclonal antibodies, affinity enhancement of monoclonal antibodies, and the identification of therapeutic targets for antibody drugs.

Author(s):  
Cecilia Deantonio ◽  
Diego Cotella ◽  
Paolo Macor ◽  
Claudio Santoro ◽  
Daniele Sblattero

2020 ◽  
Vol 27 ◽  
Author(s):  
Yuyang Li ◽  
Min Liu ◽  
Songbo Xie

: Phage display is a powerful high-throughput screening technology that presents a large and diverse selection of functional peptides, proteins, or antibody fragments on phage capsid surfaces for affinity determination towards a target of interest. Due to its advantages of a large screening capacity, mass production through fermentation, and straightforward execution, phage display has been widely used in bioengineering and biomedicine, especially for diagnostics and therapeutics. With the advent of next-generation sequencing and microfluidics technologies, phage display has become an even more powerful and popular tool for drug discovery and development. Here, we briefly review phage display technology and its application to drug discovery, including the discovery and development of peptide-based drugs and monoclonal antibodies. Combined with the emerging proteolysis targeting chimeras (PROTAC), we also discuss the advantages and future directions, aiming to facilitate the drug discovery and development.


Author(s):  
Marco Dal Ferro ◽  
Serena Rizzo ◽  
Emanuela Rizzo ◽  
Francesca Marano ◽  
Immacolata Luisi ◽  
...  

2017 ◽  
Vol 38 (6) ◽  
pp. 3915
Author(s):  
Greice Japolla ◽  
Ana Flávia Batista Penido ◽  
Greyciele Rodrigues Almeida ◽  
Luiz Artur Mendes Bataus ◽  
Jair Pereira Cunha Junior ◽  
...  

The specificity of monoclonal antibodies (mAbs) to desired targets makes these molecules suitable for therapeutic and diagnostic uses against a wide range of pathogens. Phage display antibody libraries offer one method by which mAbs can be selected for, without the use of conventional hybridoma technology. In this work, phage display technology was used to construct, select and characterize a combinatorial single chain fragment variable (scFv) antibody library against bovine herpesvirus type 1 (BoHV-1) from the immune repertoire of chickens immunized with the virus. In silico analysis of the hypervariable domains of the antibody heavy chains revealed a high frequency of scFv fragments with low variability, suggesting that selection had probably been carried out and favored by a few im-munogenic viral antigens. The reactivity of the scFv fragments selected against BoHV-1 was demon-strated by Phage-ELISA. A significant increase in antibody reactivity to the target was observed after six rounds of library selection, showing its potential use as a molecule for BoHV-1 diagnosis. The strategy described here opens up a field for the use of phage display as a tool for selection of mono-clonal antibodies that could be used for theranostic applications against infectious and parasitic dis-eases of veterinary interest.


Gene ◽  
1994 ◽  
Vol 148 (1) ◽  
pp. 7-13 ◽  
Author(s):  
Luciana Dente ◽  
Gianni Cesareni ◽  
Gioacchino Micheli ◽  
Franco Felici ◽  
Antonella Folgori ◽  
...  

1996 ◽  
Vol 243 (2) ◽  
pp. 264-269 ◽  
Author(s):  
Moshe Balass ◽  
Ely Morag ◽  
Edward A. Bayer ◽  
Sara Fuchs ◽  
Meir Wilchek ◽  
...  

2012 ◽  
Vol 59 (3) ◽  
Author(s):  
Anna Cyranka-Czaja ◽  
Jacek Otlewski

Specific, high affinity binding macromolecules are of great importance for biomedical and biotechnological applications. The most popular classical antibody-based molecules have recently been challenged by alternative scaffolds with desirable biophysical properties. Phage display technology applied to such scaffolds allows generation of potent affinity reagents by in vitro selection. Here, we report identification and characterization of a novel helical polypeptide with advantageous biophysical properties as a template for construction of phage display libraries. A three-helix bundle structure, based on Measles virus phosphoprotein P shows a very favourable stability and solubility profile. We designed, constructed and characterized six different types of phage display libraries based on the proposed template. Their functional size of over 10(9) independent clones, balanced codon bias and decent display level are key parameters attesting to the quality and utility of the libraries. The new libraries are a promising tool for isolation of high affinity binders based on a small helical scaffold which could become a convenient alternative to antibodies.


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