Wheat and maize thioredoxins: A novel cross-reactive cereal allergen family related to baker's asthma

Weichel, Michael; Glaser, Andreas; Ballmer‐Weber, Barbara; Schmid‐Grendelmeier, Peter; Crameri, Reto

doi:10.1016/j.jaci.2005.11.040

Cited by 94 publications

(80 citation statements)

References 36 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Cross-reactivity between allergens and closely related homologous human Ags is often observed in allergic individuals suffering from chronic atopic diseases (8 -11) and potentially contribute to exacerbation and/or perpetuation of chronic allergic reactions (6,10). These studies provide strong evidence for in vitro and in vivo humoral and cell-mediated IgE autoreactivity in patients suffering from long-lasting atopic diseases (8,11). Structural studies have shown that the availability of the crystal structure of a given allergen and its human homolog allows a detailed definition of the residues potentially involved in cross-reactivity (12).…”

mentioning

confidence: 99%

Cross-Reactivity and 1.4-Å Crystal Structure ofMalassezia sympodialisThioredoxin (Mala s 13), a Member of a New Pan-Allergen Family

Limacher¹,

Glaser²,

Meier³

et al. 2007

The Journal of Immunology

Self Cite

View full text Add to dashboard Cite

We have identified thioredoxins (Trx) of Malassezia sympodialis, a yeast involved in the pathogenesis of atopic eczema, and of Aspergillus fumigatus, a fungus involved in pulmonary complications, as novel IgE-binding proteins. We show that these Trx, including the human enzyme, represent cross-reactive structures recognized by serum IgE from individuals sensitized to M. sympodialis Trx. Moreover, all three proteins were able to elicit immediate-type allergic skin reactions in sensitized individuals, indicating a humoral immune response based on molecular mimicry. To analyze structural elements involved in these reactions, the three-dimensional structure of M. sympodialis Trx (Mala s 13) has been determined at 1.4-Å resolution by x-ray diffraction analysis. The structure was solved by molecular replacement and refined to a crystallographic R factor of 14.0% and a free R factor of 16.8% and shows the typical Trx fold. Mala s 13 shares 45% sequence identity with human Trx and superposition of the solved Mala s 13 structure with those of human Trx reveals a high similarity with a root mean square deviation of 1.11 Å for all Cα atoms. In a detailed analysis of the molecular surface in combination with sequence alignment, we identified conserved solvent-exposed amino acids scattered over the surface in both structures which cluster to patches, thus forming putative conformational B cell epitopes potentially involved in IgE-mediated cross- and autoreactivity.

show abstract

mentioning

confidence: 99%

Cross-Reactivity and 1.4-Å Crystal Structure ofMalassezia sympodialisThioredoxin (Mala s 13), a Member of a New Pan-Allergen Family

Limacher¹,

Glaser²,

Meier³

et al. 2007

The Journal of Immunology

Self Cite

View full text Add to dashboard Cite

show abstract

“…The presence of cross-reactive structures like enolase and MnSOD, which are also described as latex allergens [16,17], cyclophilin known as a birch pollen allergen [53], thioredoxin described as a prominent food allergen [54], and serine proteases which play an important role in house dust mite allergy [55] indicate that the whole repertoire of allergenic molecules is highly redundant and, thus, limited to a discrete number of structures [56]. In contrast to polysensitisation which is easy to demonstrate by simple determination of the RAST values against different allergen extracts [8], cross-reactivity between fungal extracts is a poorly investigated phenomenon which, however, could contribute to a better understanding of polysensitisation.…”

Section: Cross-and Autoreactivitymentioning

confidence: 99%

Overview of Aspergillus Allergens

Crameri¹,

Glaser²,

Vilhelmsson

et al. 2009

Aspergillosis: From Diagnosis to Prevention

View full text Add to dashboard Cite

Fungi in general and, Aspergillus fumigatus (A. fumigatus) in particular, are able to produce complex patterns of IgE-binding molecules. Robotics-based high throughput screening of A. fumigatus cDNA libraries displayed on phage surfaces revealed at last 81 different sequences encoding structures potentially able to bind to serum IgE of sensitised individuals suffering from A. fumigatus-related complications. Although not all of these allergens have been characterised in detail, A. fumigatus still represents the best investigated allergenic source. A total of 23 A. fumigatus allergens are recorded by the official allergen list of the International Union of Immunological Societies ( www.allergen.org ) and this is by far the longest allergen list reported for a single allergenic source. The IgE-binding molecules include species-specific as well as phylogenetically highly conserved cross-reactive structures and such with unknown function. A subset of cDNAs have been used to produce and characterise the corresponding recombinant allergens which have proven to be useful diagnostic reagents allowing specific detection of A. fumigatus sensitisation and differential diagnosis of allergic bronchopulmonary aspergillosis. Structures highly conserved through different species like manganese-dependent superoxide dismutase, P 2 acidic ribosomal protein, cyclophilins and thioredoxins induce, beyond sensitisation, IgE antibodies able to cross-react with the corresponding homologous self-antigens. The frequently observed cross-reactivity is traceable back to shared discontinuous B-cell epitopes as shown by detailed analyses of the crystal structures.

show abstract

“…[14][15][16][17] Later, several groups identified wheat allergens. [18][19][20][21] The proteins responsible for wheat-induced atopic dermatitis are described below in section 2.…”

Section: Igementioning

confidence: 99%

“…Recombinant low-molecular-weight glutenins with many Gln-Gln-Gln-Pro-Pro motifs have been expressed in Escherichia coli by a pET vector system, and were confirmed to possess IgE-binding ability. 29) As other allergens, thioredoxin, 19) lipid transfer protein, 20) acyl-CoA oxidase, 30) peroxidase, 31) and fructose-bisphosphate aldolase 32) were identified. 8,21) In addition, the epitope structures of gliadin in patients with FDEIA 24) and celiac disease 33) have been recently reported.…”

Section: Identification Of Wheat Allergens and Their Epitopesmentioning

confidence: 99%

Analysis of Food Allergen Structures and Development of Foods for Allergic Patients

Tanabe

2008

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

Wheat and maize thioredoxins: A novel cross-reactive cereal allergen family related to baker's asthma

Cited by 94 publications

References 36 publications

Cross-Reactivity and 1.4-Å Crystal Structure ofMalassezia sympodialisThioredoxin (Mala s 13), a Member of a New Pan-Allergen Family

Cross-Reactivity and 1.4-Å Crystal Structure ofMalassezia sympodialisThioredoxin (Mala s 13), a Member of a New Pan-Allergen Family

Overview of Aspergillus Allergens

Analysis of Food Allergen Structures and Development of Foods for Allergic Patients

Contact Info

Product

Resources

About