Low-affinity but high-avidity interactions may offer an explanation for IgE-mediated allergen cross-reactivity

Allergy. 2021 Aug;76(8):2565-2574. doi: 10.1111/all.14864. Epub 2021 May 28.

Abstract

Background: Allergy is a global disease with overall frequencies of >20%. Symptoms vary from irritating local itching to life-threatening systemic anaphylaxis. Even though allergies are allergen-specific, there is a wide range of cross-reactivities (eg apple and latex) that remain largely unexplained. Given the abilities of low-affinity IgG antibodies to inhibit mast cells activation, here we elucidate the minimal affinity of IgE antibodies to induce type I hypersensitivity.

Methods: Three mature (high-affinity) IgE antibodies recognizing three distinct epitopes on Fel d 1, the major cat allergen, were back-mutated to germline conformation, resulting in binding to Fel d 1 with low affinity. The ability of these IgE antibodies to activate mast cells in vitro and in vivo was tested.

Results: We demonstrate that affinities as low as 10-7 M are sufficient to activate mast cells in vitro and drive allergic reactions in vivo. Low-affinity IgE antibodies are able to do so, since they bind allergens bivalently on the surface of mast cells, leading to high-avidity interactions.

Conclusions: These results suggest that the underlying mechanism of allergen cross-reactivity may be low-affinity but high-avidity binding between IgE antibodies and cross-reactive allergen.

Keywords: IgE antibody; affinity; allergen cross-reactivity; allergy; avidity; specificity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allergens*
  • Animals
  • Cats
  • Cross Reactions
  • Humans
  • Hypersensitivity*
  • Immunoglobulin E
  • Immunoglobulin G

Substances

  • Allergens
  • Immunoglobulin G
  • Immunoglobulin E