The glycosylation of human serum IgD and IgE and the accessibility of identified oligomannose structures for interaction with mannan-binding lectin.

Journal article

Analysis of the glycosylation of human serum IgD and IgE indicated that oligomannose structures are present on both Igs. The relative proportion of the oligomannose glycans is consistent with the occupation of one N-linked site on each heavy chain. We evaluated the accessibility of the oligomannose glycans on serum IgD and IgE to mannan-binding lectin (MBL). MBL is a member of the collectin family of proteins, which binds to oligomannose sugars. It has already been established that MBL binds ...

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Authors: Arnold, J; Radcliffe, C; Wormald, M; Royle, L; Harvey, D

• Publication status: Published
• Journal: Journal of Immunology
• Volume: 173
• Issue: 11
• Pages: 6831-6840
• Publication date: 2004-12-01
• DOI: 10.4049/jimmunol.173.11.6831
• EISSN: 1550-6606
• ISSN: 0022-1767
• Language: English
• Keywords: Protein Binding; Polysaccharides; Mannose; Glycosylation; Carbohydrate Conformation; Oligosaccharides; Hydrazines; Humans; Immunoglobulin D; Enzyme-Linked Immunosorbent Assay; Models, Molecular; Protein Folding; Immunoglobulin E; Glycoside Hydrolases; Mannose-Binding Lectin; Protein Denaturation