Engineering of major house dust mite allergens Der p 1 and Der p 2 for allergen-specific immunotherapy

Clin Exp Allergy. 2009 Jul;39(7):1088-98. doi: 10.1111/j.1365-2222.2009.03264.x. Epub 2009 Apr 21.

Abstract

Background: Specifically designed recombinant allergens with reduced IgE reactivity are promising candidates for a more defined, effective, and safer specific immunotherapy (SIT).

Objective: We sought to obtain hypoallergenic hybrid molecules which could potentially be applied to house dust mite (HDM) allergy treatment.

Methods: Two hybrid molecules (QM1 and QM2) derived from the two major Dermatophagoides pteronyssinus allergens, Der p 1 and Der p 2, were engineered by PCR, produced in Escherichia coli, and purified. The overall IgE-binding capacity of the hybrids was compared with their single components by Western blot, specific IgE, skin prick test (SPT), and IgE-inhibition assays. T cell proliferation assay were performed to confirm their retention of T cell reactivity. Immune responses to the hybrid molecules were studied in BALB/c mice.

Results: The IgE reactivity of both hybrid proteins was strongly reduced as evaluated by in vitro methods. Furthermore, in vivo SPTs performed on 106 HDM-allergic patients showed that the hybrid proteins had a significantly lower potency to induce cutaneous reactions than the individual components. Hybrid molecules induced higher T cell proliferation responses than those produced by an equimolecular mixture of Der p 1 and Der p 2. Immunization of mice with the hybrid proteins induced Der p 1- and Der p 2-specific IgG, which inhibited the binding of allergic patients' IgE to these natural allergens.

Conclusion: QM1 and QM2 hybrids exhibited less IgE-binding activity but preserved immunogenicity and fulfilled the basic requirements for hypoallergenic molecules suitable for a future SIT of HDM allergy.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adolescent
  • Adult
  • Aged
  • Allergens / immunology*
  • Allergens / isolation & purification
  • Allergens / therapeutic use
  • Animals
  • Antigens, Dermatophagoides / immunology*
  • Antigens, Dermatophagoides / isolation & purification
  • Antigens, Dermatophagoides / therapeutic use
  • Arthropod Proteins
  • Cell Proliferation
  • Cloning, Molecular
  • Cysteine Endopeptidases
  • Female
  • Genetic Engineering*
  • Humans
  • Hypersensitivity / immunology
  • Hypersensitivity / therapy
  • Immunoglobulin E / immunology
  • Immunotherapy / methods*
  • Male
  • Mice
  • Mice, Inbred BALB C
  • Middle Aged
  • Polymerase Chain Reaction
  • Recombinant Fusion Proteins / immunology*
  • Recombinant Fusion Proteins / isolation & purification
  • Recombinant Fusion Proteins / therapeutic use
  • Skin Tests
  • T-Lymphocytes / immunology
  • Young Adult

Substances

  • Allergens
  • Antigens, Dermatophagoides
  • Arthropod Proteins
  • Dermatophagoides pteronyssinus antigen p 2
  • Recombinant Fusion Proteins
  • Immunoglobulin E
  • Cysteine Endopeptidases
  • Dermatophagoides pteronyssinus antigen p 1