
2 This genotype-phenotype linkage ensures that identical phage particles will be obtained from the same Escherichia coli clone. Indeed, the gene encoding the displayed molecule is packed within the same virion as a single-strained DNA (ssDNA) and the displayed peptides or proteins are expressed in fusion with phage coat protein. This technology is based on the fact that phage phenotype and genotype are physically linked. Since then, this method has become one of the most effective ways for producing large amounts of peptides, proteins and antibodies. Smith in 1985 1 as a method for presenting polypeptides on the surface of lysogenic filamentous bacteriophages. This review describes the phage display technology and presents the recent advancements in therapeutic applications of phage display.

Phages have been applicable to immunization therapies, which may lead to development of new tools used for treating autoimmune and cancer diseases. Techniques originating from phage display have been applied to transfusion medicine, neurological disorders, mapping vascular addresses and tissue homing of peptides.

Generating monoclonal antibodies and improving their affinity, cloning antibodies from unstable hybridoma cells and identifying epitopes, mimotopes and functional or accessible sites from antigens are also important advantages of this technology.

Phage display is utilized in studying protein-ligand interactions, receptor binding sites and in improving or modifying the affinity of proteins for their binding partners. This technology is based on a direct linkage between phage phenotype and its encapsulated genotype, which leads to presentation of molecule libraries on the phage surface. One of the most effective molecular diversity techniques is phage display.
