Production of recombinant antibodies using bacteriophages

Abstract

Recombinant antibody fragments such as Fab, scFv, diabodies, triabodies, single domain antibodies and minibodies have recently emerged as potential alternatives to monoclonal antibodies, which can be engineered using phage display technology. These antibodies match the strengths of conventionally produced monoclonal antibodies and offer advantages for the development of immunodiagnostic kits and assays. These fragments not only retain the specificity of the whole monoclonal antibodies but also easy to express and produce in prokaryotic expression system. Further, these antibody fragments are genetically stable, less expensive, easy to modify in response to viral mutations and safer than monoclonal antibodies for use in diagnostic and therapeutic applications. This review describes the potential of antibody fragments generated using phage display and their use as diagnostic reagents.

Back to the future: bacteriophages as promising therapeutic tools

“…Phage display libraries can be constructed for different parts of the antibodies, including single chains of the heavy or light fragments, or only for some interesting domains. Antibody libraries can include naive antibody libraries, immunized antibody libraries, synthetic antibody libraries and in vivo recombined antibody libraries . Recombinant antibodies are of interest for different reasons.…”

i-bodies, Human Single Domain Antibodies That Antagonize Chemokine Receptor CXCR4

“…Single domain antibodies and alternative scaffolds have been promoted as attractive next-generation antibodies with the potential to address some of the limitations of monoclonal antibodies (1)(2)(3)(4). Indeed several have been reported in recent years that target antigens that are refractory to traditional antibody therapies, such as G protein-coupled receptors (GPCRs) 9 (5,6).…”

High Affinity Maturated Human Antibodies from Naïve and Synthetic Antibody Repertoires

“…The antibody fragments can be expressed as a fusion protein on the surface of phages, without affecting the infectivity of phages [50]. Moreover, the displayed antibody molecules retains its antigen-antibody binding capabilities [51]. However, the challenge in generating high affinity antibodies is closely related to the quality of the library generated.…”