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Glycosylation changes of IgG associated with rheumatoid arthritis can activate complement via the mannose-binding protein.

Abstract：

:The glycosylation of the circulating immunoglobulin-gamma (IgG) antibody molecules changes in rheumatoid arthritis. The extent of the changes correlates with the disease severity and reverses in remission. We demonstrate here that the alteration in glycosylation associated with rheumatoid arthritis can create a new mode for the interaction of IgG with complement through binding to the collagenous lectin mannose-binding protein (MBP). Rheumatoid arthritis is associated with a marked increases in IgG glycoforms that lack galactose (referred to as G0 glycoforms) in the Fc region of the molecule and that terminate in N-acetyl glucosamine (GlcNAc). We show, using nuclear magnetic resonance (NMR) and X-ray data, that these terminal GlcNAc residues become accessible for MBP binding. We further demonstrate that multiple presentation of IgG-G0 glycoforms to MBP results in activation of the complement. This suggests that a contribution to the chronic inflammation of the synovial membrane could arise from the localization of the IgG-G0 glycoforms in the affected joint and from resulting activation of complement.

journal_name

Nat Med

journal_title

Nature medicine

authors

Malhotra R,Wormald MR,Rudd PM,Fischer PB,Dwek RA,Sim RB

doi

10.1038/nm0395-237

subject

Has Abstract

pub_date

1995-03-01 00:00:00

pages

237-43

issue

3

eissn

1078-8956

issn

1546-170X

journal_volume

1

pub_type

杂志文章

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