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- Title
Antibodies from patients with psoriasis recognize N-acetylglucosamine terminals in glycoproteins from Pityrosporum ovale.
- Authors
Mathov, I.; Plotkinn, L.; Abatangelo, C.; Galimberti, R.; Squiquera, L.; Leoni, J.
- Abstract
We have previously reported the finding of circulating antibodies recognizing two proteins of 100 and 120kD (PO100 and PO120) from Pityrosporum ovale in patients with psoriasis. These antibodies were specific, since they were not detected in normal sere nor in other diseases linked to P. ovale such as seborrhoeic dermatitis or pityriasis versicolor. The present study aimed at further characterizing the specificity of these antibodies. Enzyme-labelled lectins were used to determine the carbohydrate composition of PO120 and PO100. BSII, a lectin that recognizes terminal ɴ-acetylglucosamine (GlcNAc), showed the same banding pattern as sera from patients. Reactivity against these proteins was inhibited after mild oxidation of the carbohydrate moieties of the extract. Treatment of the extracts with lyticase altered the immune reactivity against the PO 120 band as seen in Western blot assays. POI00 was not detected after lyticase disestion. Disestion with lysozyme did not alter the immune reactivity of the PO100 and PO120 bands, although the protein pattern in SDS-PAGE was modified. To examine the relevance of anti-GlcNAc antibodies in the immune response to P. ovole in psoriasis, we performed a binding inhibition ELISA. Psoriatic sera that were positive in the ELISA against a heat-denatured extract of P. ovale were rendered negative only by pre-incubation with GlcNAc in a concentration-dependent manner. Our results are indicative that the antibody response to PO100 and PO120 in patients with psoriasis is directed towards terminal GlcNAc residues.
- Subjects
IMMUNOGLOBULINS; PSORIASIS; MALASSEZIA ovale; SKIN diseases; GLYCOPROTEINS; LECTINS; LYSOZYMES
- Publication
Clinical & Experimental Immunology, 1996, Vol 105, Issue 1, p79
- ISSN
0009-9104
- Publication type
Article
- DOI
10.1046/j.1365-2249.1996.d01-719.x