“From Therapeutic Monoclonal Antibodies: From Bench to Clinic” – Zhiqiang An 2011
Yeast display is a technology that has become significantly more popular in the past few years, much of this owed to the success showed by Dane Wittrup and his colleagues (reviewed in Boder and Wittrup 2000; Gai and Wittrup 2007), who have demonstrated the incredible power of yeast display in isolate of optimized antibodies with Kd values in the subpicomolar range (Boder, Midelfort, and Wittrup 20C).
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The strengths of phage display include ease of use, robustness, and stability of the phage particles. Because of these properties, phage display lends itself not only to panning on proteins, but also to various cell-based panning strategies which are now allowing for isolation of antibodies against active conformers of cell surface proteins (Schwartz et al. 2004). One potential negative attribute of phage display is that selection of antibody fragments on the surface of phages may not provide the best pressures for selecting the best-behaving (ie. Folding, solubility) antibody fragments.
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