Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1993655 | Methods | 2013 | 8 Pages |
Abstract
Traditional immunization and display antibody discovery methods rely on competitive selection amongst a pool of antibodies to identify a lead. While this approach has led to many successful therapeutic antibodies, targets have been limited to proteins which are easily purified. In addition, selection driven discovery has produced a narrow range of antibody functionalities focused on high affinity antagonism. We review the current progress in developing arrayed protein libraries for screening-based, rather than selection-based, discovery. These single molecule per microtiter well libraries have been screened in multiplex formats against both purified antigens and directly against targets expressed on the cell surface. This facilitates the discovery of antibodies against therapeutically interesting targets (GPCRs, ion channels, and other multispanning membrane proteins) and epitopes that have been considered poorly accessible to conventional discovery methods.
Keywords
SARCVBLIMSGPCRIMACCDRFACSmAbG-protein coupled receptorMonoclonal antibodyBLAST, basic local alignment search toolBlastDiversityStructure activity relationshipLaboratory Information Management SystemFabfluorescence activated cell sortingfragment antigen-bindingVariablemajor histocompatibility complexMHCcomplementary determining regionProtein engineeringAntibodyJoining
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Authors
Cornelia A. Bentley, Omar A. Bazirgan, James J. Graziano, Evan M. Holmes, Vaughn V. Smider,