Autoallergy: a pathogenetic factor in atopic dermatitis?
Department of General and Experimental Pathology, Vienna General Hospital, University of Vienna, Austria.Current problems in dermatology 02/1999; 28:45-50. pp.45-50
Article: Relationship between skin bacterial colonization and the occurrence of allergen-specific and non-allergen-specific antibodies in sera of children with atopic eczema/dermatitis syndrome.[show abstract] [hide abstract]
ABSTRACT: In this study we investigated skin bacterial colonization, allergen-specific IgE and antiphospholipid/antinuclear antibodies in 72 children with atopic eczema/dermatitis syndrome (age 2-17 years). Bacteria were found on the skin in 41 cases and serological allergen-specific IgE positivity in 37. The different forms of antibodies appeared in the ratio 21/72 (33 antibodies in 21 children). The occurrence of antiphospholipid antibodies was significantly higher in the patients than in the controls. There were significantly more allergens in the group with bacterial colonization than in the group without colonization. The SCORAD index showed a significant positive association with the skin colonization. We conclude that there are significant relationships between the occurrence of Staphylococcus aureus colonization and the levels of inhalant allergen-specific IgE in children with atopic eczema/dermatitis syndrome, and between the occurrence of antiphospholipid IgM positivity and atopic eczema/dermatitis syndrome.Acta Dermato Venereologica 02/2004; 84(1):32-6. · 3.18 Impact Factor
[show abstract] [hide abstract]
ABSTRACT: Allergy is a widespread, often severe health problem. In vivo or in vitro identification of new allergenic proteins (natural or bioengineered) is time- and resource-consuming, and in vivo testing can be dangerous. Thus, allergenicity prediction through computation (in silico) was proposed to narrow down the number of potential allergens to be tested with traditional methods. In 2001, the Food and Agriculture Organization (FAO) and the World Health Organization (WHO) officially defined guidelines for in silico allergenicity prediction, based on amino acid sequence similarity to known allergens; these guidelines, however, have been criticized because of frequent false positives. In the present work, the BLAST (Basic Local Alignment Search Tool) software was used to compare known and potential allergens, and select only statistically significant homologies (i.e. homologies whose E value, calculated by BLAST, was < 1); FAO/WHO rules were then applied to these homologies. With this method, correct recognition of all known allergens, with only 10 false positives (1.26% of all predicted allergens) was achieved when using an upper limit of 0.1 for E values; complete suppression of wrong predictions, while maintaining 100% sensitivity, was obtained with little modifications of the minimum requirements contained in the FAO/WHO guidelines.Atti della Accademia Peloritana dei Pericolanti : Classe di Scienze Fisiche, Matematiche e Naturali. 01/2010;
Article: Comparison of the crystal structures of the human manganese superoxide dismutase and the homologous Aspergillus fumigatus allergen at 2-A resolution.[show abstract] [hide abstract]
ABSTRACT: Manganese superoxide dismutase (MnSOD) of Aspergillus fumigatus, a fungus involved in many pulmonary complications, has been identified as IgE-binding protein. It has been shown also that MnSODs from other organisms, including human, are recognized by IgE Abs from individuals sensitized to A. fumigatus MnSOD. Comparison of the fungal and the human crystal structure should allow the identification of structural similarities responsible for IgE-mediated cross-reactivity. The three-dimensional structure of A. fumigatus MnSOD has been determined at 2-A resolution by x-ray diffraction analysis. Crystals belonged to space group P2(1)2(1)2(1) with unit cell dimensions of a = 65.88 A, b = 98.7 A, and c = 139.28 A. The structure was solved by molecular replacement using the structure of the human MnSOD as a search model. The final refined model included four chains of 199-200 amino acids, four manganese ions, and 745 water molecules, with a crystallographic R-factor of 19.4% and a free R-factor of 23.3%. Like MnSODs of other eukaryotic organisms, A. fumigatus MnSOD forms a homotetramer with the manganese ions coordinated by three histidines, one aspartic acid, and one water molecule. The fungal and the human MnSOD share high similarity on the level of both primary and tertiary structure. We identified conserved amino acids that are solvent exposed in the fungal and the human crystal structure and are therefore potentially involved in IgE-mediated cross-reactivity.The Journal of Immunology 03/2002; 168(3):1267-72. · 5.79 Impact Factor
Data provided are for informational purposes only. Although carefully collected, accuracy cannot be guaranteed. The impact factor represents a rough estimation of the journal's impact factor and does not reflect the actual current impact factor. Publisher conditions are provided by RoMEO. Differing provisions from the publisher's actual policy or licence agreement may be applicable.