Source: http://www.asmscience.org/content/book/10.1128/9781555816506.chap21
Timestamp: 2019-04-26 14:15:57+00:00

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The display of peptides and proteins on the surfaces of bacteriophages is a powerful technique for the identification of specific ligands. Today, phage display technology is a well established method that has revolutionized our capability of selecting specific molecules. Phage display technology has enjoyed enormous success in recent years and has been used in countless studies. Alternative phage display systems utilizing bacteriophages such as λ, T4, and T7, which assemble in the host cytosol and are released via cell lysis, have now been developed. Recently, microbial cell surface displays for peptide library screening, bioadsorption, and live vaccine development have been reported. The filamentous bacteriophage M13 is the most popular and widely used display vehicle. The use of M13 vectors for the display of cDNA-encoded libraries is also not well established because of the lack of efficient C-terminal display in M13. Alternative systems based on large-genome phages, mainly T7, T4, and λ, have been used recently. The commercial availability of the T7 phage display system, optimized protocols, and ready-made libraries for selections has led to an increasing use of this system for a variety of studies. Apparently, HOC and SOC provide additional stability to T4 phage under adverse conditions such as extreme pH or osmotic shock. Lambda display has been used for epitope mapping of monoclonal antibodies against a large number of human and microbial proteins.
Schematic representation of the filamentous bacteriophage M13. The single-stranded circular DNA core is coated with five viral coat proteins. The schematic locations of the different proteins are shown. The gpVIII protein is present at about 2,700 copies, while gpIII, gpVI, gpVII, and gpIX are present at about 5 copies each. All of the coat proteins can be used as platforms for protein display. With the exception of gpIII, the capsid proteins are small, with 33 to 112 amino acids.
Arrangement of the bacteriophage lambda head proteins D and E. Both the D and E proteins are present at over 400 copies. The D protein serves as an efficient platform for display. Arrangements of the trimeric D protein surrounding the hexameric E protein are shown. The figure shows one face of the icosahedral head, with the vertices of the E pentamers. The three corners of the face are shown as triangles.
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