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Related Experiment Videos

Serologic crossreactions among primate immunoglobulins

M H Shearer1, F J Stevens, F A Westholm

  • 1Department of Microbiology and Immunology, University of Oklahoma Health Sciences Center, Oklahoma City 73190, USA.

Developmental and Comparative Immunology
|November 1, 1995
PubMed
Summary

Researchers developed 50 monoclonal antibodies (mAb) targeting baboon IgG. One mAb shows broad reactivity with human immunoglobulin (Ig) subclasses and kappa light chains, identifying a specific epitope.

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Area of Science:

  • Immunology
  • Primate research

Background:

  • Monoclonal antibodies (mAbs) are crucial tools in immunological research.
  • Characterizing antibodies against non-human primate immunoglobulins aids comparative immunology and preclinical studies.

Purpose of the Study:

  • To generate and characterize monoclonal antibodies (mAbs) specific for baboon IgG.
  • To assess the cross-reactivity of these mAbs with immunoglobulins (Ig) from various primate species, including humans.
  • To identify a mAb with broad reactivity to human Ig subclasses and light chains for epitope analysis.

Main Methods:

  • Generation and characterization of 50 murine monoclonal antibodies (mAbs) against baboon IgG.
  • Cross-reactivity testing against baboon IgM and Ig from human, chimpanzee, rhesus monkey, cynomolgus monkey, and African green monkey.

Related Experiment Videos

  • Specificity analysis using human myeloma proteins and Bence Jones proteins to determine Ig subclass and light chain reactivity.

    • Main Results:

    • 50 murine mAbs specific for baboon IgG were successfully generated.
    • One mAb demonstrated cross-reactivity with all four human IgG subclasses and human IgM.
    • This mAb recognized a kappa (k) light chain specificity, excluding kappa II subgroups, indicating a discontinuous epitope defined by six amino acids.

    Conclusions:

    • A novel mAb with broad reactivity to human IgG subclasses and IgM has been developed.
    • This mAb provides a valuable tool for studying human immunoglobulin structure and function.
    • The identified epitope offers insights into kappa light chain variability and antibody recognition mechanisms.