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Phage display is also a widely used method for in vitro protein evolution (also called protein engineering). As such, phage display is a useful tool in drug discovery. It is used for finding new ligands (enzyme inhibitors, receptor agonists and antagonists) to target proteins.
For example, the library size for phage and bacterial display is limited to 1-10 × 10^9 different members. The library size for yeast display is even smaller. Moreover, these cell-based display system only allow the screening and enrichment of peptides/proteins containing natural amino acids.
Ribosome display is a technique used to perform in vitro protein evolution to create proteins that can bind to a desired ligand. The process results in translated proteins that are associated with their mRNA progenitor which is used, as a complex, to bind to an immobilized ligand in a selection step.
John McCafferty is a British scientist, one of the founders of Cambridge Antibody Technology alongside Sir Gregory Winter and David Chiswell. He is well known as one of the inventors of scFv antibody fragment phage display, [1] a technology that revolutionised the monoclonal antibody drug discovery.
The 'helper' phage infects the bacterial host by first attaching to the host cell's pilus and then, after attachment, transporting the phage genome into the cytoplasm of the host cell. Inside the cell, the phage genome triggers production of single stranded phagemid DNA in the cytoplasm. This phagemid DNA is then packaged into phage particles.
In 2018, the Nobel Prize organisation awarded one quarter of the Nobel Prize in Chemistry to a founding member of CAT, Sir Greg Winter FRS "for the phage display of peptides and antibodies.". [2] Founded in 1989, CAT was acquired by AstraZeneca for £702m in 2006. [3] [4] AstraZeneca subsequently acquired MedImmune LLC, [5] which it combined ...
The article does seem to focus on filamentous phage display and accentuates the need for helper phage. This ignores methods based not on phagemids but on engineered M13 phage - the approach taken at the outset by Smith. Phil Scrutinator 17:44, 14 March 2008 (UTC) T7 phage display should be mentioned also.
Infection begins when the gp9 tailspike of the P22 phage binds to the O-antigen lipopolysaccharide on the surface of Salmonella typhimurium host. [1] The virion's tail fiber protein has endorhamnosidase activity, which cleaves the O-antigen chain. [3] Upon infection, P22 can enter either a lytic or lysogenic growth pathway. [1]