Conclusions

Phage display technology permits the selection of antibody fragments from large libraries constructed from the B lymphocytes of individuals or assembled in vitro from the genetic elements encoding antibodies. The procedure is rapid and independent of the immunogenicity of the target antigen, a drawback associated with conventional hybridoma technology. An array of selection procedures on whole eukaryotic cells and intact tissues facilitates the isolation of antibodies against membrane molecules and epitopes, even when the target cells are extremely rare or lose phenotypic characteristics upon preparation. These characteristics render this technology a valuable research tool in searches for novel cell surface molecules, including tumor-specific antigens. Engineering steps allow the tailoring of antibody fragments to meet specific needs in terms of avidity, pharmacokinetic properties and biological effector functions. Monoclonal antibodies from phage display libraries constructed from human V regions represent a class of molecules particularly suitable for immunotherapy in humans.

See also: Affinity; Affinity maturation; B lymphocyte repertoire; Domains, immunoglobulin-type; Immunoglobulin class switching; Immunoglobulin genes; Somatic mutation.

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