Evidence map›Paper›PMID 7585040›Full record

ArticleNature medicine1995

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

R Malhotra, M R Wormald, P M Rudd, P B Fischer, R A Dwek, R B Sim

Erratum issuedAbstract read
PubMed Publisher
In one paragraph

Article in Nature medicine, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 273 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
273citing papers in PubMed, 3 pooled it
9.3field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

273 citing papers in PubMed, 3 syntheses or guidelines pooled it, 773 citations in OpenAlex.

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  3. Glycosylation Profile of IgG in Moderate Kidney Dysfunction.Journal of the American Society of Nephrology : JASN · 2016
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213 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

R MalhotraDepartment of Biochemistry, University of Oxford, UK.
M R Wormald
P M Rudd
P B Fischer
R A Dwek
R B Sim
University of Oxford · GBMedical Research Council · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

Complement ActivationArthritis, RheumatoidCarbohydrate SequenceCarrier ProteinsComputer SimulationGlycosylationHumansImmunoglobulin Fc FragmentsImmunoglobulin GMagnetic Resonance SpectroscopyMannose-Binding LectinsModels, MolecularMolecular Sequence DataSynovial FluidCarrier ProteinsImmunoglobulin Fc FragmentsImmunoglobulin GMannose-Binding Lectins

Identifiers

PMID7585040
OpenAlexW2053863608

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.