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Related Experiment Videos

Variable region differences affect antibody binding to immobilized but not soluble antigen.

C Horgan1, K Brown, S H Pincus

  • 1Laboratory of Microbial Structure and Function, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT.

Human Antibodies and Hybridomas
|July 1, 1992
PubMed
Summary

Two chimeric antibodies showed similar solution binding but differing affinities for immobilized antigens. Antibody B11

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Area of Science:

  • Immunology
  • Biochemistry
  • Molecular Biology

Background:

  • Chimeric IgG1 antibodies were engineered using distinct heavy chain variable regions.
  • These antibodies target the (Tyr,Glu)-Ala-Lys antigen.

Purpose of the Study:

  • To investigate the antigen binding characteristics of two chimeric IgG1 antibodies.
  • To determine how epitope density affects antibody affinity in solid-phase assays.

Main Methods:

  • Expression of chimeric IgG1 antibodies (10B and B11) with different VH genes.
  • Solution and solid-phase assays to measure antibody binding to (Tyr,Glu)-Ala-Lys and a peptide conjugate.
  • Analysis of Fab fragment binding to immobilized antigens.

Main Results:

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  • Antibodies 10B and B11 exhibited similar affinities in solution assays.
  • Antibody affinity for immobilized antigens was dependent on epitope density.
  • Antibody B11 showed reduced binding at lower antigen densities compared to antibody 10B.
  • Fab fragments of B11 displayed impaired binding to immobilized antigens.

Conclusions:

  • Epitope density significantly influences the binding characteristics of chimeric IgG1 antibodies.
  • The heavy chain variable region impacts antibody affinity in solid-phase assays.
  • These findings are crucial for understanding antibody-antigen interactions in immobilized systems.