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Phage display antibody repertoire9/16/2023 Thus, phage display has been widely used in immunotherapy, regenerative medicine, development of biosensors and synthetic biology. The technique has many applications, such as selection of monoclonal antibody and bioactive peptides, epitope mapping, selection of disease specific antigen mimics, cell-specific or organ-specific peptides, peptidomimetics and development of drug delivery systems. The detailed information about filamentous phage genomes has been the key to success for widespread applications of phage display technology. Phage display technique can be used for targeting different biological entities, such as proteins, viruses, bacteria, cancer cells and non-organic substances, like metals, alloys, semiconductors, toxins and plastic surfaces. affinity selection of specific peptide from a large repertoire of clones. Peptide phage libraries containing billions of variants are used to interact with target molecules and the most specifically binding peptide is enriched after 3–5 rounds of biopanning, i.e. Phage display technique is an in vitro method used to select a specific fusion peptide displayed on the surface of bacteriophages. Hopefully, this technique can complement studies on host–pathogen interactions and assist novel strategies of drug discovery for coronaviruses. As phage display is an important technique for antibody selection, this review presents a concise summary of the very recent applications of phage display technique with a special reference to progress in diagnostics and therapeutics for coronavirus diseases. In the current situation of pandemic of Coronavirus disease (COVID-19), a search for neutralizing antibodies is motivating the researchers to find therapeutic candidates against novel SARS-CoV-2. The translation of new diagnostic tools thus developed has been used in situations arising due to pathogenic microbes, including bacteria and deadly viruses, such as Zika, Ebola, Hendra, Nipah, Hanta, MERS and SARS. This versatile technique has been modified tremendously over last three decades, leading to generation of different platforms for combinatorial peptide display. The ligand–receptor interactions forming the basis of phage display have been well utilized in epitope mapping and antigen presentation on the surface of bacteriophages for screening novel vaccine candidates by using affinity selection-based strategy called biopanning. As a large number of nucleotide fragments may be cloned into the phage genome, a phage library may harbour millions or sometimes billions of unique and distinctive displayed peptide ligands. Phage display is one of the important and effective molecular biology techniques and has remained indispensable for research community since its discovery in the year 1985.
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