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Related Experiment Video

Updated: May 10, 2026

Application of Biochip Microfluidic Technology to Detect Serum Allergen-specific Immunoglobulin E (sIgE)
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Published on: April 21, 2019

Lectins and the radioallergosorbent test.

D Barnett1, M E Howden

  • 1Commonwealth Scientific and Industrial Research Organization, Division of Food Research, North Ryde, Australia.

The Journal of Allergy and Clinical Immunology
|October 1, 1987
PubMed
Summary

Lectin binding of immunoglobulin E (IgE) to common food allergens like legumes and wheat was investigated. Results show that while non-immune binding is minimal, specific IgE binding to certain lectins suggests their role in allergic responses.

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Area of Science:

  • Allergy and Immunology
  • Food Science
  • Biochemistry

Background:

  • Lectin binding to immunoglobulin E (IgE) may influence allergy testing.
  • Legume and wheat allergens are common causes of food allergies.

Purpose of the Study:

  • To investigate the role of lectin binding of IgE in RAST for legume and wheat extracts.
  • To determine if lectin-specific sugars can inhibit IgE binding to these allergens.

Main Methods:

  • Lectins from various legumes and wheat germ were coupled to RAST discs.
  • RAST inhibition assays were performed using sera from sensitive patients and lectin-specific sugars.
  • Total IgE levels and endogenous glucose were measured in patient sera.

Main Results:

  • Inhibition of RAST by sugars was minimal, suggesting limited non-immune IgE binding to lectins on paper discs.
  • Significant immune binding of specific IgE to certain lectins was observed.
  • Endogenous glucose in sera may cause some self-inhibition of lectin binding.

Conclusions:

  • Non-immune lectin binding of IgE is not significant in standard RAST for these allergens.
  • Specific IgE binding to certain lectins indicates their potential importance in IgE-mediated allergic responses.
  • Further research is needed to elucidate the precise mechanisms of lectin involvement in food allergies.