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Isolating and engineering human antibodies using yeast surface display.

Ginger Chao1, Wai L Lau, Benjamin J Hackel

  • 1Department of Chemical Engineering and Biological Engineering Division, Massachusetts Institute of Technology, 77 Massachusetts Avenue E19-563, Cambridge, Massachusetts 02139, USA.

Nature Protocols
|April 5, 2007
PubMed
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This study details a method for improving antibody fragments using yeast display technology. The process enhances antibody affinity and stability for better antigen binding.

Area of Science:

  • Biotechnology
  • Molecular Biology
  • Immunology

Background:

  • Yeast surface display is a powerful technique for protein engineering.
  • Improving antibody affinity and stability is crucial for therapeutic applications.

Purpose of the Study:

  • To describe a protocol for isolating and engineering single-chain antibody fragments (scFvs) with enhanced affinity and stability.
  • To detail methods for directed evolution of scFvs using yeast surface display.

Main Methods:

  • Isolation of scFvs from a yeast-displayed human library using magnetic-activated cell sorting and flow cytometry.
  • Directed evolution of scFvs through random mutagenesis and iterative flow cytometry selection.
  • Characterization and titration of engineered scFv clones displayed on yeast.

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Main Results:

  • Successful isolation and engineering of scFvs with increased affinity and stability.
  • Demonstration of directed evolution for optimizing scFv properties.
  • Established methods for characterizing and quantifying scFv clones.

Conclusions:

  • The described protocol provides a robust framework for developing high-affinity and stable antibodies.
  • Yeast surface display is an effective platform for antibody engineering and directed evolution.
  • This method facilitates the generation of tailored antibody fragments for specific antigen targets.