Phage display is a laboratory technique for the study of protein–protein, protein–peptide, and protein–DNA interactions that uses bacteriophages to connect proteins with the genetic information that encodes them. Phage display was first described by George P. Smith in 1985, when he demonstrated the display of peptides on filamentous phage by fusing the peptide of interest on to gene III of filamentous phage. A patent by George Pieczenik claiming priority from 1985 also describes the generation of phage display libraries. This technology was further developed and improved by groups at the MRC Laboratory of Molecular Biology with Winter and McCafferty and The Scripps Research Institute with Lerner and Barbas for display of proteins such as antibodies for therapeutic protein engineering. The connection between genotype and phenotype enables large libraries of proteins to be screened and amplified in a process called in vitro selection, which is analogous to natural selection. The most common bacteriophages used in phage display are M13 and fd filamentous phage, though T4, T7, and λ phage have also been used.
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