Journal
PROTEIN ENGINEERING DESIGN & SELECTION
Volume 24, Issue 9, Pages 711-719Publisher
OXFORD UNIV PRESS
DOI: 10.1093/protein/gzr034
Keywords
cross-species display; phage display; yeast display; antibody library; antibody engineering; library selection
Funding
- Merck Research Laboratories
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We created a cross-species display system that allows the display of the same antibody libraries on both prokaryotic phage and eukaryotic yeast without the need for molecular cloning. Using this cross-display system, a large, diverse library can be constructed once and subsequently used for display and selection in both phage and yeast systems. In this article, we performed the parallel phage and yeast selection of an antibody maturation library using this cross-display platform. This parallel selection allowed us to isolate more unique hits than single-species selection, with 162 unique clones from phage and 107 unique clones from yeast. In addition, we were able to shuttle yeast hits back to Escherichia coli cells for affinity characterization at a higher throughput.
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