PubMed · 11234812
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M A Quilliam, AOAC International. Committee on Natural Toxins and Food Allergens. Phycotoxins.. https://pubmed.ncbi.nlm.nih.gov/11234812/
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BACKGROUND: Tropical countries experience wide variations in daytime temperature and relative humidity. This affects the quality of the source material used for allergen extracts. The present study was undertaken to standardize the processing and preservation conditions of Imperata cylindrica grass pollen. METHODS: I. cylindrica (Ic) inflorescence were freeze-dried, pollens sieved out and stored at -70 degrees C (IcA). Alternatively, the inflorescence were dried at room temperature and then at 37 degrees C, pollens sieved out and stored at 4 degrees C (IcB). The extracts prepared in PBS were analyzed in vivo by skin tests and in vitro by immunochemical methods. RESULTS: Reduced SDS-PAGE revealed 37 protein bands in IcA extract and 23 in IcB extract. IgE immunoblot with a pool of sera from Ic hypersensitive patients showed 30 allergenic bands in IcA and 14 in IcB. Immunoblot using anti-Ic rabbit sera revealed 33 antigenic bands in IcA and 22 in IcB. In both blots, the IcA extract exhibited sharp bands and the IcB extract exhibited diffuse bands. ELISA, ELISA inhibition and skin test procedures showed that IcA extracts had a higher potency than IcB extracts. CONCLUSIONS: Extracts prepared from -70 degrees C processed and preserved pollens (IcA) are allergenically more potent and contain a greater number of major and minor allergens than IcB extracts.
The concept of specific immune treatment against allergic diseases requires the development of antibodies capable of specifically neutralizing anti-allergen antibodies. The aim of the present study was to investigate whether a novel approach, consisting in raising anti-idiotypic blocking antibodies through peptide immunization, could be envisaged in the field of allergy. Using allergy to cow's milk as a model, we prepared polyclonal antibodies against a peptide that is complementary (i.e. hydropathically opposed) to a major epitope of bovine beta-lactoglobulin (BLG), one of the main allergens of bovine milk. Anti-complementary peptide antibodies were found to neutralize in vitro both well-characterized anti-BLG monoclonal antibodies from mice sensitized to BLG and anti-BLG IgE from two patients suffering from milk allergy. These results suggest a new strategy for the functional inhibition of specific disease-associated IgE that may be applicable to the specific treatment of various allergic disorders.
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.