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Two expression vectors for the phage-displayed chicken monoclonal antibody
Naoto Nakamura1, Mariko Shimokawa, Kazuyoshi Miyamoto
1Laboratory of Immunobiology, Department of Molecular and Applied Biosciences, Graduate School of Biosphere Sciences, Hiroshima University, 1-4-4 Kagamiyama, Higashi, Hiroshima 739-8528, Japan.
Journal of Immunological Methods
|September 16, 2003
Summary
Researchers developed new expression vectors for producing recombinant chicken monoclonal antibodies (mAbs). These vectors enable easier purification and use in assays, offering an alternative to traditional hybridoma methods for chicken mAb production.
Area of Science:
- Immunotechnology
- Recombinant Antibody Engineering
- Biotechnology
Background:
- Traditional chicken hybridomas yield low antibody amounts.
- Existing mouse monoclonal antibody (mAb) vectors have limitations for chicken mAb applications, particularly in dual-antibody assays due to mouse Ckappa detection tags.
Purpose of the Study:
- To develop novel expression vectors for producing functional recombinant chicken mAbs.
- To overcome limitations of existing methods for chicken mAb production and application.
Main Methods:
- Engineered two expression vectors accommodating single chain variable fragments (scFv) with chicken Clambda and FLAG/histidine tags.
- Expressed a prion protein (PrP)-specific chicken mAb (HUC2-13) as phage-displayed and soluble scFv forms.
Main Results:
- The recombinant scFv mAbs retained the antigen-binding specificity of the original HUC2-13 mAb.
- The expressed scFv mAbs were easily purified and suitable for use in combination with mouse mAbs.
- The new vectors facilitate production of chicken mAbs with improved utility.
Conclusions:
- The developed expression vectors provide an effective alternative for producing chicken mAbs.
- These methods enhance the utility of chicken mAbs in various research and diagnostic applications.
- The approach may broaden the use of chicken mAb reagents across multiple scientific fields.