PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 9689337

Characterized allergens causing bakers' asthma.

X Baur·A Posch
View original source ↗Export metadata ↓

Abstract

Although airborne allergens in bakeries and confectioneries cause one of the most common forms of occupational asthma, namely, bakers' asthma, only a few of them are known in detail so far. Here we summarize current knowledge of bakery allergens and describe our own two-dimensional (2-D) immunoelectrophoresis studies of wheat-flour allergens as well as the allergenic baking enzyme Asp o 2. Out of approximately 700 soluble wheat polypeptides, 70 show IgE binding; the following wheat-flour allergens could be identified and characterized: members of the alpha-amylase inhibitor family (14-18 kDa), acyl-CoA oxidase (26 kDa), peroxidase (36 kDa), and fructose-bisphosphate aldolase (37 kDa). However, the great majority of the soluble wheat-flour allergens, mainly located in the 27-, 55-, and 70-kDa areas of the 2-D immunoblots with pI values of 5.8-6.8, 5.9-6.5, and 5.5-6.1, respectively, are not known at present. Asp o 2, to which approximately 25% of all bakers with respiratory symptoms are sensitized, is a well-characterized starch-cleaving enzyme. We conclude that great effort is still needed to describe all major wheat-flour allergens. As shown by Asp o 2, knowledge of the causative allergens and their characteristics enables us to initiate very effective preventive measures such as the introduction of granulated allergenic products.

Explore related subjects

AllergensAsthmaFlourHumansHypersensitivityOccupational DiseasesTriticumJournal ArticleReview

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

X Baur, A Posch. 1998. Characterized allergens causing bakers' asthma.. https://doi.org/10.1111/j.1398-9995.1998.tb03931.x

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed1999

Sequence-divergent units of the ABA-1 polyprotein array of the nematode Ascaris suum have similar fatty-acid- and retinol-binding properties but different binding-site environments.

Polyproteins comprise long polypeptides that are post-translationally cleaved into proteins of different function, or tandemly repetitive polypeptides which are processed into multiple versions of proteins which are presumed to have the same function. In the latter case the individual units of the polyprotein can differ substantially in sequence. Identity of function between the different units therefore cannot be assumed. Here we have examined the ABA-1 polyprotein allergen of the parasitic nematode Ascaris suum and found it to contain units which show a 50% difference in amino acid sequence. The parasite therefore produces at least two radically different forms of the allergen encoded within the polyprotein array. In fluorescence-based ligand-binding assays, recombinant polypeptides representing the two forms (designated ABA-1A1 and ABA-1B1) showed similar binding affinities for a range of fluorescent active-site probes [retinol, dansylundecanoic acid, dansyl-DL-alpha-amino-octanoic acid, cis-parinaric acid (cPnA)] and for the non-specific hydrophobic surface probe 8-anilinonaphthalene-1-sulphonic acid. However, the molecular environments in the active sites are markedly different, as indicated by disparate fluorescence emission peaks and intensities of bound probes. CD showed that the proteins have similar secondary structures but differ in susceptibility to chemical denaturation/unfolding by guanidinium chloride. Both retain a single conserved tryptophan residue in a characteristic non-polar environment, as revealed by extreme fluorescence blue shift. Thus the gross differences in sequence of the two proteins are not reflected in their ligand-binding specificities but in their binding-site environments.

Allergens↗
PubMed1999

Long term prevention of allergic lung inflammation in a mouse model of asthma by CpG oligodeoxynucleotides.

Asthma is an inflammatory disease of the airways that is induced by Th2 cytokines and inhibited by Th1 cytokines. Despite a steady increase in the incidence, morbidity, and mortality from asthma, no current treatment can reduce or prevent asthma for a prolonged period. We examined the ability of unmethylated CpG oligodeoxynucleotides (ODN), which are potent inducers of Th1 cytokines, to prevent the inflammatory and physiological manifestations of asthma in mice sensitized to ragweed allergen. Administration of CpG ODN 48 h before allergen challenge increased the ratio of IFN-gamma to IL-4 secreting cells, diminished allergen-induced eosinophil recruitment, and decreased the number of ragweed allergen-specific IgE-producing cells. These effects of CpG ODN were sustained for at least 6 wk after its administration. Furthermore, there was a vigorous Th1 memory response to the recall Ag, inhibition of peribronchial and perivascular lung inflammation, and inhibition of bronchial hyperresponsiveness 6 wk after administration of CpG ODN. Administration of CpG ODN in IFN-gamma -/- mice failed to inhibit eosinophil recruitment, indicating a critical role of IFN-gamma in mediating these effects. This is the first report of a treatment that inhibits allergic lung inflammation in presensitized animals for a prolonged period and thus has relevance to the development of an effective long term treatment for asthma.

Allergens↗
PubMed1999

Humoral and cell-mediated autoimmune reactions to human acidic ribosomal P2 protein in individuals sensitized to Aspergillus fumigatus P2 protein.

A panel of cDNAs encoding allergenic proteins was isolated from an Aspergillus fumigatus cDNA library displayed on the surface of filamentous phage. Solid phase-immobilized serum immunoglobulin E (IgE) from A. fumigatus-allergic individuals was used to enrich phage displaying IgE-binding molecules. One of the cDNAs encoded a 11.1-kD protein that was identified as acidic ribosomal phosphoprotein type 2 (P2 protein). The allergen, formally termed rAsp f 8, shares >62% sequence identity and >84% sequence homology to corresponding eukaryotic P2 proteins, including human P2 protein. The sequences encoding human and fungal P2 protein were subcloned, expressed in Escherichia coli as His6-tagged fusion proteins, and purified by Ni2+-chelate affinity chromatography. Both recombinant P2 proteins were recognized by IgE antibodies from allergic individuals sensitized to the A. fumigatus P2 protein and elicited strong type 1-specific skin reactions in these individuals. Moreover, human and fungal P2 proteins induced proliferative responses in peripheral blood mononuclear cells of A. fumigatus- allergic subjects sensitized to the fungal P2 protein. These data provide strong evidence for in vitro and in vivo humoral and cell-mediated autoreactivity to human P2 protein in patients suffering from chronic A. fumigatus allergy.

Allergens↗