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- Title
Allergens of <em>Pityrosporum ovale</em> and <em>Candida albicans</em>. II. Physicochemical characterization.
- Authors
Doekes, G.; Kaal, M. J. H.; van Ieperen-van Dijk, A. G.
- Abstract
<em>Pityrosporum ovale</em> has recently been recognized as a source of allergens to which many patients with atopic dermatitis (AD) show type I skin reactions and specific IgE antibodies. In this study the IgE-binding components and/or epitopes in <em>P. ovale</em> extract were shown to be partially sensitive to pronase or trypsin treatment, whereas periodate oxidation resulted in a complete loss of IgE-binding capacity, thus suggesting the involvement of carbohydrate structures. In Con A affinity chromatography most of the IgE-binding capacity of crude <em>P. ovale</em> extract bound to the column, and could be eluted with mannoside. Gel filtration on Sephacryl S-400 revealed a marked heterogeneity with respect to molecular mass, with most of the IgE-binding activity associated with high-mol.-mass fractions (from 5 × 104 up to 2 × 106 Da). A similar heterogeneity was found after chromatofocusing, with IgE-binding in the whole pI-range from 7.0 to 4.0. Essentially identical results were obtained with extracts of <em>Candida albicans</em>, in agreement with the previously shown cross-reactivity of IgE-binding components in the two yeast extracts. In inhibition ELISA, gel filtration and chromatofocusing fractions containing components with widely different mol. mass or pI showed complete reciprocal cross-inhibition, and were all capable of inhibiting the binding of IgE to unfractionated extracts. We therefore conclude that the cross-reacting anti-<em>P. ovale</em>/anti-<em>C. albicans</em> IgE antibodies in the sera of AD patients are mainly directed at a restricted number of carbohydrate epitopes that are expressed on a heterodisperse range of high-mol.-mass components, probably mannans or mannoproteins.
- Subjects
SKIN inflammation; MALASSEZIA ovale; ALLERGENS; IMMUNOGLOBULIN E; CARRIER proteins; EPITOPES; AFFINITY chromatography
- Publication
Allergy, 1993, Vol 48, Issue 6, p401
- ISSN
0105-4538
- Publication type
Article
- DOI
10.1111/j.1398-9995.1993.tb00737.x