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Pigeon fanciers' lung: identification of disease-associated carbohydrate epitopes on pigeon intestinal mucin.
Clin Exp Immunol. 1999 Aug; 117(2):230-6.CE

Abstract

Pigeon intestinal mucin, a complex high molecular weight glycoprotein, is a key antigen in the development of pigeon fanciers' lung (PFL). We have studied the specificity of antibodies to mucin in patients with PFL and asymptomatic antibody-positive individuals. Extensive papain digestion, which removes the non-glycosylated regions of the mucin leaving the heavily glycosylated 'bottle brush' regions, resulted in a 600-fold decrease in IgG3 antibody titres with little effect on IgG1 and IgG2 titres. This suggests that IgG1 and IgG2 are directed against the region rich in O-linked sugar chains whilst the majority of the IgG3 is directed against epitopes which are proteinase-sensitive. Lectin mapping of the carbohydrates present on pigeon intestinal mucin demonstrated high levels of exposed N-acetyl neuraminic acid, N-acetyl galactosamine and N-acetyl glucosamine, with lower levels of fucose and some galactose. Sera from pigeon fanciers inhibited binding of lectins specific for N-acetyl neuraminic acid, N-acetyl galactosamine, internal N-acetyl glucosamine and fucose. Sera from people with PFL, compared with sera from asymptomatic antibody-positive fanciers, had significantly higher titres of antibody that inhibited binding of four lectins specific for N-acetyl galactosamine and one fucose-specific lectin, suggesting that these sugars may play a dominant role in disease-associated epitopes. The results suggest that different IgG subclasses recognize different epitopes on mucin and that the epitopes recognized by the major subclasses are present on the O-linked oligosaccharides. Further, the carbohydrate-specific anti-mucin antibodies produced by PFL patients may differ in their specificity from those found in asymptomatic individuals.

Authors+Show Affiliations

Department of Physiological Sciences, The Medical School, University of Newcastle upon Tyne, UK. c.i.baldwin@newcastle.ac.ukNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

10444252

Citation

Baldwin, C I., et al. "Pigeon Fanciers' Lung: Identification of Disease-associated Carbohydrate Epitopes On Pigeon Intestinal Mucin." Clinical and Experimental Immunology, vol. 117, no. 2, 1999, pp. 230-6.
Baldwin CI, Todd A, Bourke SJ, et al. Pigeon fanciers' lung: identification of disease-associated carbohydrate epitopes on pigeon intestinal mucin. Clin Exp Immunol. 1999;117(2):230-6.
Baldwin, C. I., Todd, A., Bourke, S. J., Allen, A., & Calvert, J. E. (1999). Pigeon fanciers' lung: identification of disease-associated carbohydrate epitopes on pigeon intestinal mucin. Clinical and Experimental Immunology, 117(2), 230-6.
Baldwin CI, et al. Pigeon Fanciers' Lung: Identification of Disease-associated Carbohydrate Epitopes On Pigeon Intestinal Mucin. Clin Exp Immunol. 1999;117(2):230-6. PubMed PMID: 10444252.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Pigeon fanciers' lung: identification of disease-associated carbohydrate epitopes on pigeon intestinal mucin. AU - Baldwin,C I, AU - Todd,A, AU - Bourke,S J, AU - Allen,A, AU - Calvert,J E, PY - 1999/8/12/pubmed PY - 1999/8/12/medline PY - 1999/8/12/entrez SP - 230 EP - 6 JF - Clinical and experimental immunology JO - Clin Exp Immunol VL - 117 IS - 2 N2 - Pigeon intestinal mucin, a complex high molecular weight glycoprotein, is a key antigen in the development of pigeon fanciers' lung (PFL). We have studied the specificity of antibodies to mucin in patients with PFL and asymptomatic antibody-positive individuals. Extensive papain digestion, which removes the non-glycosylated regions of the mucin leaving the heavily glycosylated 'bottle brush' regions, resulted in a 600-fold decrease in IgG3 antibody titres with little effect on IgG1 and IgG2 titres. This suggests that IgG1 and IgG2 are directed against the region rich in O-linked sugar chains whilst the majority of the IgG3 is directed against epitopes which are proteinase-sensitive. Lectin mapping of the carbohydrates present on pigeon intestinal mucin demonstrated high levels of exposed N-acetyl neuraminic acid, N-acetyl galactosamine and N-acetyl glucosamine, with lower levels of fucose and some galactose. Sera from pigeon fanciers inhibited binding of lectins specific for N-acetyl neuraminic acid, N-acetyl galactosamine, internal N-acetyl glucosamine and fucose. Sera from people with PFL, compared with sera from asymptomatic antibody-positive fanciers, had significantly higher titres of antibody that inhibited binding of four lectins specific for N-acetyl galactosamine and one fucose-specific lectin, suggesting that these sugars may play a dominant role in disease-associated epitopes. The results suggest that different IgG subclasses recognize different epitopes on mucin and that the epitopes recognized by the major subclasses are present on the O-linked oligosaccharides. Further, the carbohydrate-specific anti-mucin antibodies produced by PFL patients may differ in their specificity from those found in asymptomatic individuals. SN - 0009-9104 UR - https://www.unboundmedicine.com/medline/citation/10444252/Pigeon_fanciers'_lung:_identification_of_disease_associated_carbohydrate_epitopes_on_pigeon_intestinal_mucin_ L2 - https://onlinelibrary.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=0009-9104&date=1999&volume=117&issue=2&spage=230 DB - PRIME DP - Unbound Medicine ER -