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Related Experiment Videos

IgE structure-function relationships defined by sequence directed antibodies induced by synthetic peptides.

M W Robertson1, F T Liu

  • 1Division of Molecular Biology, Medical Biology Institute, La Jolla, CA 92037.

Molecular Immunology
|February 1, 1988
PubMed
Summary

Researchers synthesized six peptides from murine IgE domains to create antibodies. Four antibodies showed IgE reactivity, with two stimulating mediator release and identifying key IgE-receptor binding sites.

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Molecular cloning and tissue distribution profiles of the chicken R-spondin1 gene.

Genetics and molecular research : GMR·2015

Area of Science:

  • Immunology
  • Molecular Biology
  • Allergy Research

Background:

  • Immunoglobulin E (IgE) plays a critical role in allergic reactions.
  • Understanding IgE's interaction with its receptor is crucial for developing targeted therapies.
  • Specific IgE domains and their involvement in receptor binding require detailed investigation.

Purpose of the Study:

  • To synthesize peptides representing domains of murine IgE.
  • To generate antibodies against these peptides and assess their IgE reactivity.
  • To investigate the role of specific IgE sequences in receptor binding and mediator release.

Main Methods:

  • Synthesis of six peptides from murine IgE C epsilon 2, C epsilon 3, and C epsilon 4 domains.
  • Production of rabbit polyclonal antibodies against peptide-KLH conjugates.

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  • Testing antibody reactivity against various murine immunoglobulin classes and human IgE.
  • Assessing antibody-induced mediator release from IgE-sensitized rat basophilic leukemia (RBL) cells.
  • Evaluating antibody binding to receptor-bound IgE.

    • Main Results:

    • Four out of six antisera showed preferential reactivity with murine IgE.
    • One antiserum (anti-epsilon peptide 5) reacted with both human and murine IgE.
    • Two antisera (anti-epsilon peptides 4 and 5) strongly stimulated mediator release from RBL cells.
    • Epsilon-peptide 3 showed the least binding to receptor-bound IgE, suggesting proximity to the receptor recognition site.
    • Epsilon-peptide 6 showed the highest binding but no stimulatory activity, indicating accessibility without effective cross-linking.

    Conclusions:

    • Epsilon-peptides 4 and 5 are not significantly involved in IgE receptor binding.
    • Epsilon-peptide 3 is likely proximal to the IgE-receptor recognition site.
    • Epsilon-peptide 6 is accessible on cell-bound IgE but does not facilitate effective receptor cross-linking.