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Human and murine immunoglobulin expression vector cassettes.

G R McLean1, A Nakouzi, A Casadevall

  • 1Department of Cell Biology, Albert Einstein College of Medicine, 1300 Morris Park Ave., 10461, Bronx, NY, USA.

Molecular Immunology
|March 21, 2001
PubMed
Summary
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Researchers developed new immunoglobulin (Ig) expression vectors for producing recombinant chimeric antibodies in mammalian cells. These vectors enable efficient antibody production and antigen-specific antibody generation, advancing antibody engineering.

Area of Science:

  • Immunology
  • Molecular Biology
  • Biotechnology

Background:

  • Recombinant antibody production is crucial for therapeutic and diagnostic applications.
  • Existing expression systems may have limitations in efficiency and versatility.

Purpose of the Study:

  • To develop novel immunoglobulin (Ig) expression vectors for efficient production of recombinant chimeric Ig molecules.
  • To enable the generation of functional antibodies with retained antigen specificity.

Main Methods:

  • Construction of versatile Ig expression vectors encoding human and murine Ig constant regions.
  • Utilized unique restriction sites for variable region replacement via PCR.
  • Employed the CMV promoter for expression in non-lymphoid cells.
  • Incorporated distinct drug selection markers for sequential or co-transfection.

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Main Results:

  • Achieved high secretion levels of recombinant Ig (1.2 microg/ml/million cells/day) in transfected B cells.
  • Demonstrated successful replacement of variable regions, yielding functional Ig.
  • Confirmed retention of antigen specificity in the produced recombinant antibodies.

Conclusions:

  • The developed Ig expression vectors are effective tools for producing recombinant chimeric antibodies.
  • These vectors facilitate the generation of functional, antigen-specific antibodies in mammalian cells.
  • The system offers flexibility for antibody engineering and production applications.