Home About us Contact
|
Home About us Contact | ||
|
|
||
New Allergens (new + allergen)
Selected AbstractsAnalysis of allergens in metalworking fluidsCONTACT DERMATITIS, Issue 5 2008Maj-Len Henriks-Eckerman Background:, Metalworking fluids (MWFs) are well-known causes of occupational contact dermatitis in machinists. Objective:, To gain information about skin sensitizers in MWFs and to compare it with the information in safety data sheets (SDSs). Methods:, A total of 17 samples of MWF concentrates were analysed for skin sensitizers known or suspected to be used in MWF. Alkanolamines, formaldehyde, isothiazolinones, methyldibromo glutaronitrile (MDBGN), and iodopropynyl butylcarbamate (IPBC) were separated by liquid chromatography. Resin acids of colophonium (colophony) were separated by gas chromatography. The substances were identified with mass spectrometric detection and ultraviolet detection. Results:, Of the MWFs, 15 contained 6,39% of alkanolamines, mostly monoethanolamine and triethanolamine. Formaldehyde was detected in all MWFs: the concentrations of total formaldehyde ranged between 0.002% and 1.3%. Benzisothiazolinone and octylisothiazolinone were detected in one fluid each. IPBC was detected in nine MWFs, and the highest concentration was 0.09%. Methylisothiazolinone and MDBGN were not detected in any of the fluids. Resin acids of colophonium were detected in seven MWFs in concentrations ranging from 0.41% to 3.8%. On the whole, the allergens analysed were poorly declared in the SDSs. Conclusions:, The content of total formaldehyde was not declared in any SDS. IPBC, a relatively new allergen, seems to be common in MWFs. Isothiazolinones may be relevant allergens of machinists, and they should be analysed in MWFs in case other sources are not identified. The occupational relevance of positive patch test results to MWF ingredients in machinists is difficult to determine if information in the SDSs is relied upon. [source] P17 Allergic contact dermatitis from hydrolyzed wheat proteinCONTACT DERMATITIS, Issue 3 2004Olivia Bordalo Allergic Contact Dermatitis (ACD) from hydrolysed wheat protein (HWP) is rarely reported in the literature. We describe 2 cases of ACD to this new allergen. Case1- A 39-year-old non atopic woman presented with a dermatitis of the face, mainly eyelids and neck. She had been using a new cosmetic cream for 2 months. The lesions subsided with topical corticosteroids. Patch tests with the standard, cosmetic, fragrance series and with her own products gave positive reactions only to the new cosmetic cream. We also tested all the components of this cream and only HWP gave a doubtful reaction with occlusive tests and positive reaction with ROAT. Case 2 , A 48-year-old atopic woman presented with a dermatitis of the face and hands for 1 month. She had been using a new cosmetic cream for 11 months and kept using the product without any suspicion. The dermatitis subsided with cetirizine and topical corticosteroids. Patch tests with the standard, cosmetic, fragrance series and her own products revealed positive reactions to the cosmetic cream. Again, testing all the components of the cream, only HWP gave doubtful reactions with occlusive tests and positive reactions with ROAT. Discussion:, In recent years, a number of protein hydrolysates have been introduced into cosmetic manufacture. HWP is being used in cosmetic creams for its moisturizing properties. As far as we know, there is only one previously reported case of ACD induced by this allergen. More cases may be expected. [source] Molecular and immunological characterization of Asp f 34, a novel major cell wall allergen of Aspergillus fumigatusALLERGY, Issue 8 2009A. G. Glaser Background:, Although fungal spores have been recognized as triggers of respiratory allergy and asthma, only two allergenic fungal cell wall components have so far been described. Methods:, Eighty-one sequences derived from an Aspergillus fumigatus cDNA library encoding putative allergens were examined for the presence of cell wall components. A new allergen (Asp f 34) was evaluated by Western blots, enzyme-linked immunosorbent assay (ELISA), peripheral blood mononuclear cell (PBMC) proliferation assays, and skin prick test (SPT). Results:, The cDNA encoding Asp f 34 contained an open reading frame predicting a protein of 185 amino acids with a molecular weight of 19.38 kDa, showing sequence homology to phiA, an essential protein for the formation of conidia in the genus Aspergillus. The recombinant Asp f 34 was binding IgE from sensitized individuals in Western blots. An ELISA survey showed that 94% of the ABPA and 46% of the A. fumigatus -sensitized individuals tested had Asp f 34-specific serum IgE. Asp f 34 induced allergen-specific proliferation exclusively of PBMCs from patients sensitized to the allergen. Eight patients with anti-Asp f 34 serum IgE tested reacted positively in SPT, whereas four A. fumigatus -sensitized individuals without Asp f 34-specific IgE and eight healthy controls scored negatively. Conclusions:, A cell wall protein of the phialides of A. fumigatus was identified as a major allergen. Asp f 34 belongs to the Aspergillus -specific proteins of the phiA family and has relevant potential for a specific diagnosis of Aspergillus sensitization. [source] Miconidin and miconidin methyl ether from Primula obconica Hance: new allergens in an old sensitizerCONTACT DERMATITIS, Issue 4 2006Evy Paulsen Several chemical and clinical observations have suggested the presence of at least one more allergen in addition to primin in Primula obconica. The aim of this study was to investigate the allergenicity of the primin precursor miconidin and the related miconidin methyl ether, both isolated from P. obconica. 12 primin-positive persons were patch tested with miconidin 0.01% petrolatum (pet.), miconidin in 96% ethanol incorporated into 0.01% pet., and miconidin methyl ether 1.0% pet. All persons were positive to miconidin 0.01% pet., with the strength of reactions very similar to those of the individual primin reactions, and remained inexplicably negative while testing with miconidin in 96% ethanol and pet., while miconidin methyl ether elicited 7 positive reactions. Although both miconidin and miconidin methyl ether may be allergenic only due to their conversion to primin in the skin, the presence of these substances nevertheless has to be taken into account when assessing the allergenicity of new P. obconica cultivars. [source] Today's allergic rhinitis patients are different: new factors that may play a roleALLERGY, Issue 9 2007R. Mösges Most of today's patients suffering from allergic rhinitis (AR) are sensitized to more than one trigger and suffer from persistent and moderate/severe symptoms, which severely impair their quality of life (QOL). The objective of this article was to review the data on the effect of increased air pollution, changes in indoor environment/lifestyle/affluence, exposure to new allergens and psychologically stressful lifestyles, as also to explore their potential in the development of this more ,aggressive' form of disease. Increased fossil fuel-generated air pollution may increase the risk of allergic sensitization, airway responsiveness to allergens, and allergenicity and the bioavailability of airborne allergens. Changes in indoor environment/lifestyle/affluence appear to have led to more time being spent indoors and resulted in perennial exposure to indoor allergens, changes in sensitization patterns, and polysensitization to a variety of novel cross-reacting exotic food and pet allergens. Although evidence suggests an association between psychological stress and increased risk for atopy and allergic disease, further studies are required to demonstrate this unequivocally. The more persistent and moderate/severe nature of the disease suggests a need for modification of current treatment strategies and advocacy of the use from the outset of agents, which are both efficacious and safe in managing severe and persistent AR symptoms and in improving the QOL of affected individuals. [source] Screening the allergenic repertoires of wheat and maize with sera from double-blind, placebo-controlled food challenge positive patientsALLERGY, Issue 1 2006M. Weichel Background:, Food allergy to wheat and maize is an increasing factor of deterioration of life quality, especially childhood and can, in rare cases, even induce anaphylaxis. Although omega-5 gliadin from wheat and maize lipid transfer protein have been characterized as major cereal allergens on the molecular level, the list of food allergens is far to be complete. Methods:, To identify the IgE-binding repertoires of wheat and maize we screened respective cDNA libraries displayed on phage surface with sera from patients with a confirmed food allergy. The study included six patients with a positive double-blind, placebo-controlled food challenge (DBPCFC) to wheat, nine patients with a positive DBPCFC to maize, and six patients with anaphylactic reactions after ingestion of wheat. Results:, The enriched sequences encoding IgE-binding proteins showed heterogeneous repertoires for both, wheat and maize. The selected wheat repertoire yielded 12, the maize repertoire 11 open reading frames. Among these we identified allergens belonging to already characterized allergens families, such as gliadin, profilin and beta-expansin. Besides, we found novel proteins with high cross-reactive potential, such as thioredoxins, as well as sequences that had so far not been related to cereal allergy at all. The IgE-binding capacity of some selected proteins was evaluated in vitro and cross-reactivity was demonstrated by competition ELISA. Conclusion:, With regard to the heterogeneity of the characterized sequences as well as to the biochemical nature of the new allergens detected we conclude that wheat and maize-related food allergy is more complex than so far anticipated. [source] Identification of two pistachio allergens, Pis v 1 and Pis v 2, belonging to the 2S albumin and 11S globulin familyCLINICAL & EXPERIMENTAL ALLERGY, Issue 6 2009K. Ahn Summary Background IgE-mediated allergic reactions to pistachio appear to be occurring more frequently; however, little is known about its allergenic proteins. Objective We attempted to identify pistachio allergens and to clone the encoding genes. Methods Pistachio proteins were extracted and separated by SDS-PAGE. Immunolabelling was performed with sera from 28 pistachio-allergic individuals. Proteins of interest were further analysed by Edman sequencing and mass spectrometry/mass spectrometry (MS/MS). In parallel, a cDNA library was generated from immature pistachios and screened with primers designed on the basis of internal sequences and peptide spectra. Full-length cDNA clones were isolated from the library and sequenced. Recombinant proteins were expressed and tested with sera from pistachio-allergic patients. Results Nineteen out of 28 patients (68%) showed IgE binding to a 7 kDa protein fraction, while 14 (50%) showed specific IgE to a 32 kDa protein fraction. Analysis by Edman sequencing and MS/MS revealed that these proteins were homologue to the cashew nut allergens Ana o 3 and Ana o 2, respectively. Screening of the pistachio cDNA library resulted in isolation of novel protein cDNAs. Open-reading frame translation provided the complete amino acid sequences of two new allergenic pistachio proteins. Recombinant proteins were recognized by six out of six selected patients. Therefore, these new allergens were named Pis v 1 and Pis v 2 by the Allergen Nomenclature Subcommittee. Conclusion Novel allergens in pistachio, Pis v 1 and Pis v 2, which belong to 2S albumin and 11S globulin family, respectively, were isolated and the genes encoding these allergens were identified. [source] | ||||||||||