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Related Experiment Videos

IgE binding studies with large peptides expressed from Der p II cDNA constructs.

K Y Chua1, W K Greene, P Kehal

  • 1Western Australian Research Institute for Child Health, Princess Margaret Hospital for Children, Subiaco.

Clinical and Experimental Allergy : Journal of the British Society for Allergy and Clinical Immunology
|March 1, 1991
PubMed
Summary

The major mite allergen Der p II retains IgE binding activity but requires its complete structure. Large protein fragments do not bind IgE, indicating conformational determinants in this dust mite allergen.

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Area of Science:

  • Immunology
  • Allergen research
  • Molecular biology

Background:

  • Der p II is a major dust mite allergen known for its resistance to denaturation.
  • Recombinant Der p II expressed in bacteria retains significant IgE binding activity.
  • The structural requirements for Der p II's IgE binding are not fully understood.

Purpose of the Study:

  • To investigate the structural basis of IgE binding to the mite allergen Der p II.
  • To determine if linear or conformational epitopes are responsible for IgE recognition.
  • To assess the IgE binding potential of truncated Der p II fragments.

Main Methods:

  • Expression of full-length and truncated Der p II fragments using bacterial systems (pGEX vectors).
  • Construction and screening of random cDNA fragment libraries.

Related Experiment Videos

  • Testing IgE binding activity of recombinant proteins and peptides using patient sera (including children with atopic dermatitis).

    • Main Results:

    • Full-length recombinant Der p II exhibits strong IgE binding.
    • Large overlapping peptides (e.g., 1-69, 69-129, 42-117) showed weak or no IgE binding in most sera.
    • Sera from children with atopic dermatitis showed weak IgE binding to large peptides compared to intact Der p II.

    Conclusions:

    • The IgE binding activity of Der p II is critically dependent on its complete primary structure.
    • These findings suggest that the antigenic determinants of Der p II are predominantly conformational.
    • Linear epitopes within Der p II are unlikely to elicit significant IgE responses.