期刊
MOLECULAR IMMUNOLOGY
卷 44, 期 10, 页码 2598-2604出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.molimm.2006.12.011
关键词
IgA nephropathy; IgA; lectins; glycosylation; N-acetylgalactosamine
资金
- NATIONAL CENTER FOR RESEARCH RESOURCES [M01RR000032] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [T32AI007051] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF DENTAL &CRANIOFACIAL RESEARCH [R01DE013694] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES [R24DK064400, P01DK061525, R01DK057750, R01DK071802, R01DK047322] Funding Source: NIH RePORTER
- NCRR NIH HHS [M01 RR000032-43, M01 RR000032, M01 RR 00032] Funding Source: Medline
- NIAID NIH HHS [T32 AI007051] Funding Source: Medline
- NIDCR NIH HHS [R01 DE013694-05, R01 DE013694] Funding Source: Medline
- NIDDK NIH HHS [DK 47322, DK 57750, P01 DK061525-010003, DK 71802, R01 DK057750, P01 DK061525, R01 DK057750-04, DK 61525, DK 64400] Funding Source: Medline
Lectins are proteins with specificity of binding to certain monosaccharides or oligosaccharides. They can detect abnormal glycosylation patterns on immunoglobulins in patients with various chronic inflammatory diseases, including rheumatoid arthritis and IgA nephropathy (IgAN). However, lectins exhibit binding heterogeneity, depending on their source and methods of isolation. To characterize potential differences in recognition of terminal N-acetylgalactosamine (GalNAc) on IgA1, we evaluated the binding characteristics of several commercial preparations of GalNAc-specific lectins using a panel of IgA1 and, as controls, IgA2 and IgG myeloma proteins. These lectins originated from snails Helix aspersa (HAA) and Helix pomatia (HPA), and the plant Vicia villosa (VV). Only HAA and HPA bound exclusively to IgA1, with its O-linked glycans composed of GalNAc, galactose, and sialic acid. In contrast, VV reacted with sugars of both IgA subclasses and IgG, indicating that it also recognized N-linked glycans without GalNAc. Furthermore, HAA and HPA from several manufacturers differed in their ability to bind various IgA1 myeloma proteins and other GalNAc-containing glycoproteins in ELISA and Western blot. For serum samples from IgAN patients, HAA was the optimal lectin to study IgAl glycosylation in ELISA and Western blot assays, including identification of the sites of attachment of the aberrant glycans. The galactose-deficient glycans were site-specific, localized mostly at Thr-228 and/or Ser230. Because of the heterogeneity of GalNAc-specific lectins, they should be carefully characterized with appropriate substrates before undertaking any study. (c) 2007 Elsevier Ltd. All rights reserved.
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