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Related Concept Videos

Hybridoma Technology01:31

Hybridoma Technology

Hybridoma technology is used for the large-scale production of monoclonal antibodies. Monoclonal antibodies bind to only a single antigenic determinant or epitope. Such antibodies are used in research, diagnostics, and disease therapy. The hybridoma technology established in 1975 by Georges Köhler and Cesar Milstein was awarded the Nobel Prize in Medicine in 1984 for revolutionizing research and therapy.
Hybridoma Selection
Commonly used fusion techniques — electroporation, polyethylene glycol...

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Related Experiment Video

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Scalable High Throughput Selection From Phage-displayed Synthetic Antibody Libraries
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Published on: January 17, 2015

A mammalian expression system for high throughput antibody screening.

Linda Xu1, Xiaofang Jin, G Jonah Rainey

  • 1Department of Antibody Discovery and Protein Engineering, MedImmune, LLC, One MedImmune Way, Gaithersburg, MD 20878, United States.

Journal of Immunological Methods
|July 9, 2013
PubMed
Summary

This study presents a high-throughput mammalian cell expression system for screening soluble protein libraries, like antibody fragments (scFvs) and Fc-fusion proteins, enabling efficient antibody discovery and characterization.

Keywords:
Adenovirus expression systemCMVEBNA-1Epstein–Barr virus nuclear antigen 1FabHTPHigh throughput screeningIRESMammalian expressionPhage displayVHcytomegalovirus.fragment antigen-bindingheavy chain variable regionshigh throughputinternal ribosome entry sitescFvsingle chain Fv

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Area of Science:

  • Biotechnology
  • Protein Engineering
  • Mammalian Cell Culture

Background:

  • High-throughput screening (HTS) is crucial for identifying novel therapeutic proteins.
  • Existing methods for expressing soluble proteins in mammalian cells can be low-throughput.
  • Efficient generation of diverse protein libraries is essential for antibody discovery.

Purpose of the Study:

  • To develop and optimize a high-throughput mammalian expression system for soluble protein libraries.
  • To enable efficient screening of antibody variants like single-chain variable fragments fused to Fc (scFv-Fc) and immunoglobulin G (IgG).
  • To facilitate downstream antibody characterization and development.

Main Methods:

  • Utilized adenovirus transduction for expressing protein libraries in mammalian cells.
  • Employed Gateway technology to recombine antibody gene fragments into an adenovirus vector.
  • Optimized protocols for batch reformatting of antibody single chains (scFvs) and fragment antigen-binding (Fabs) into scFv-Fc or IgG formats.
  • Established clonality in 96-well plates using a low ratio of viral particles per cell.

Main Results:

  • Achieved high expression levels of scFv-Fc and IgGs, up to 100μg/mL in 96-well plates.
  • Successfully established clonality in 78% of protein-expressing wells, ensuring single-sequence representation.
  • Demonstrated a robust mammalian expression system capable of producing soluble protein variants in a high-throughput manner.
  • Validated the system's efficiency for generating diverse antibody libraries.

Conclusions:

  • The developed mammalian expression system enables high-throughput screening of soluble protein libraries.
  • This method facilitates the efficient production and characterization of antibody variants.
  • The system provides a foundation for developing advanced downstream screening methodologies for antibody discovery.