Cross-protection of AIT-induced antibodies to related allergens requires a high degree of structural identity.

Background: In contrast to sublingual immunotherapy (SLIT) with recombinant Mal d 1 (rMal d 1-SLIT), SLIT with rBet v 1 (rBet v 1-SLIT) induced Mal d 1-cross-reactive antibodies without IgE-blocking activity. To elucidate whether the development of cross-protective IgG responses depends on the degree of molecular identity of allergens we compared the cross-reactivity, cross-blocking activity, and affinity of SLIT-induced antibodies with allergens of varying amino acid sequence identities to Bet v 1 and Mal d 1, namely Cor a 1.04 (hazelnut), Pru av 1 (cherry), and Dau c 1 (carrot).

EAACI Molecular Allergology User's Guide 2.0.

Since the discovery of immunoglobulin E (IgE) as a mediator of allergic diseases in 1967, our knowledge about the immunological mechanisms of IgE-mediated allergies has remarkably increased. In addition to understanding the immune response and clinical symptoms, allergy diagnosis and management depend strongly on the precise identification of the elicitors of the IgE-mediated allergic reaction. In the past four decades, innovations in bioscience and technology have facilitated the identification and production of well-defined, highly pure molecules for component-resolved diagnosis (CRD), allowing a personalized diagnosis and management of the allergic disease for individual patients.

Peanut lipids influence the response of bronchial epithelial cells to the peanut allergens Ara h 1 and Ara h 2 by decreasing barrier permeability.

Peanut-allergic individuals react upon their first known ingestion of peanuts, suggesting sensitization occurs through non-oral exposure. Increasing evidence suggests that the respiratory tract is a probable site for sensitization to environmental peanuts. However, the response of the bronchial epithelium to peanut allergens has never been explored.

Cosensitization to the 3 Nonhomologous Major Cashew Allergens Ana o 1, Ana o 2, and Ana o 3 Is Caused by IgE Cross-reactivity.

Background: Cashew nuts often cause strong allergic reactions, which are even more severe than those of peanuts. Ana o 1 (vicilin), Ana o 2 (legumin), and Ana o 3 (2S albumin) are major cashew allergens. Cosensitization to all 3 nonhomologous cashew nut allergens has been observed.

Pru du 1, the Bet 1-homologue from almond, is a major allergen in patients with birch pollen associated almond allergy.

Background: Almond allergy is common and can manifest in two different forms. Primary almond allergy has been reported to be associated with sensitization to almond legumin Pru du 6. In birchendemic regions, there is a link between birch-pollinosis which is likely based on a cross-reactive Bet v 1 homologue, a yet unidentified allergen in almond.

Corrigendum: Fish Allergy Around the World-Precise Diagnosis to Facilitate Patient Management.

[This corrects the article DOI: 10.3389/falgy.2021.

Fish Allergy Around the World-Precise Diagnosis to Facilitate Patient Management.

The accurate and precise diagnosis of IgE-mediated fish allergy is one of the biggest challenges in allergy diagnostics. A wide range of fish species that belong to evolutionary distant classes are consumed globally. Moreover, each fish species may contain multiple isoforms of a given allergen that often differ in their allergenicity.

Isotype-specific binding patterns of serum antibodies to multiple conformational epitopes of Bet v 1.

Background: Birch pollen is an important elicitor of respiratory allergy. The major allergen, Bet v 1, binds IgE exclusively via conformational epitopes.

Objective: We identified Bet v 1-specific epitope repertoires of IgE and IgG from birch pollen-allergic and nonallergic subjects.

The Major Peanut Allergen Ara h 2 Produced in Contains Hydroxyprolines and Is a Viable Alternative to the Product in Allergy Diagnosis.

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.

Identification of vicilin, legumin and antimicrobial peptide 2a as macadamia nut allergens.

Macadamia nut is an increasingly popular food item of a healthy diet. However, macadamia nut is also a potent allergenic food. To date, there is little information about the allergenic proteins involved.

IgE-cross-blocking antibodies to Fagales following sublingual immunotherapy with recombinant Bet v 1.

Background: Evidence has accumulated that birch pollen immunotherapy reduces rhinoconjunctivitis to pollen of birch homologous trees. Therapeutic efficacy has been associated with IgE-blocking IgG antibodies. We have recently shown that sera collected after 16 weeks of sublingual immunotherapy with recombinant Bet v 1 (rBet v 1-SLIT) display strong IgE-blocking bioactivity for Bet v 1.

Development of a novel Ara h 2 hypoallergen with no IgE binding or anaphylactogenic activity.

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.

Fish-derived low molecular weight components modify bronchial epithelial barrier properties and release of pro-inflammatory cytokines.

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.

Impact of lipid binding on the tertiary structure and allergenic potential of Jug r 3, the non-specific lipid transfer protein from walnut.

Plant non-specific lipid transfer proteins type 1 (nsLTP1) are small basic proteins with a hydrophobic cavity able to host a number of different ligands: i.e. fatty acids, fatty acyl-CoA, phospholipids, glycolipids, and hydroxylated fatty acids.

WHO/IUIS Allergen Nomenclature: Providing a common language.

A systematic nomenclature for allergens originated in the early 1980s, when few protein allergens had been described. A group of scientists led by Dr. David G.

Concomitant sensitization to legumin, Fag e 2 and Fag e 5 predicts buckwheat allergy.

Background: Buckwheat (Fagopyrum esculentum) has become increasingly popular as a healthy food in Europe. However, for sensitized individuals, consumption can cause anaphylactic reactions. The aim of this study was to identify individual well-characterized buckwheat allergens for component-resolved diagnosis.

Navigating through the Jungle of Allergens: Features and Applications of Allergen Databases.

The increasing number of available data on allergenic proteins demanded the establishment of structured, freely accessible allergen databases. In this review article, features and applications of 6 of the most widely used allergen databases are discussed. The WHO/IUIS Allergen Nomenclature Database is the official resource of allergen designations.

A Cross-Reactive Human Single-Chain Antibody for Detection of Major Fish Allergens, Parvalbumins, and Identification of a Major IgE-Binding Epitope.

Fish allergy is associated with moderate to severe IgE-mediated reactions to the calcium binding parvalbumins present in fish muscle. Allergy to multiple fish species is caused by parvalbumin-specific cross-reactive IgE recognizing conserved epitopes. In this study, we aimed to produce cross-reactive single chain variable fragment (scFv) antibodies for the detection of parvalbumins in fish extracts and the identification of IgE epitopes.

Qualitative analysis of xinyue capsules by high-performance liquid chromatography: Preliminary evaluation of drug quality in a Sino-Austrian joint study.

Objective: To develop a reliable method to assess the stability of xinyue capsules containing Panax quinquefolius saponins according to European quality standards.

Methods: An efficient high-performance liquid chromatography ultraviolet (HPLC-UV) method was established to analyse six main ginsenosides (Rb1, Rb2, Rc, Rd, Re and Rg1) in six different batches (120 capsules/batch) from the same lot of xinyue capsules and in one batch measured six times within one day. The six ginsenosides were separated on a Hypersil BDS-C18 column (3 μm, 100 mm×3 mm) at a flow rate of 0.

Cor a 14, the allergenic 2S albumin from hazelnut, is highly thermostable and resistant to gastrointestinal digestion.

Scope: Allergens from nuts frequently induce severe allergic reactions in sensitive individuals. The aim of this study was to elucidate the physicochemical characteristics of natural Cor a 14, the 2S albumin from hazelnut.

Methods And Results: Cor a 14 was purified from raw hazelnuts using a combination of precipitation and chromatographic techniques.