Publications by authors named "Angelika Tscheppe"

Peanut allergy is a potentially life-threatening disease that is mediated by allergen-specific immunoglobulin E (IgE) antibodies. The major peanut allergen Ara h 2, a 2S albumin seed storage protein, is one of the most dangerous and potent plant allergens. Ara h 2 is posttranslationally modified to harbor four disulfide bridges and three hydroxyprolines.

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Background: To date, no safe allergen-specific immunotherapy for patients with peanut allergy is available. Previous trials were associated with severe side effects.

Objective: We sought to determine the relative importance of conformational and linear IgE-binding epitopes of the major peanut allergen Ara h 2 and to produce a hypoallergenic variant with abolished anaphylactogenic activity.

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The prevalence of fish allergy among fish-processing workers is higher than in the general population, possibly due to sensitization via inhalation and higher exposure. However, the response of the bronchial epithelium to fish allergens has never been explored. Parvalbumins (PVs) from bony fish are major sensitizers in fish allergy, while cartilaginous fish and their PVs are considered less allergenic.

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The years 1988-1995 witnessed the beginning of allergen cloning and the generation of recombinant allergens, which opened up new avenues for the diagnosis and research of human allergic diseases. Most crystal and solution structures of allergens have been obtained using recombinant allergens. Structural information on allergens allows insights into their evolutionary biology, illustrates clinically observed cross-reactivities, and makes the design of hypoallergenic derivatives for allergy vaccines possible.

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Article Synopsis
  • Peanut allergy is a serious IgE-mediated condition with no current treatment, leading to research on potential vaccines targeting the most potent allergen, Ara h 2.
  • A fusion protein combining the S-layer protein from Lactobacillus and a peptide derived from Ara h 2 was developed and tested for its ability to inhibit IgE binding in allergic patients.
  • Results showed that while the fusion protein recognized IgE in many cases, it did not trigger a significant allergic response, suggesting this peptide-based vaccine approach could be viable but may require multiple allergen peptides for broader protection.
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