Xenogeneic Neu5Gc and self-glycan Neu5Ac epitopes are potential immune targets in MS.
Options
BORIS DOI
Date of Publication
March 2020
Publication Type
Article
Division/Institute
Contributor
Oechtering, Johanna | |
Keller, Christian W | |
Peschke, Benjamin | |
Bovin, Nicolai | |
Kappos, Ludwig | |
Cummings, Richard D | |
Kuhle, Jens | |
Lünemann, Jan D |
Subject(s)
Series
Neurology: Neuroimmunology and Neuroinflammation
ISSN or ISBN (if monograph)
2332-7812
Publisher
Wolters Kluwer Health
Language
English
Publisher DOI
PubMed ID
32014849
Description
OBJECTIVE
To explore the repertoire of glycan-specific immunoglobulin G (IgG) antibodies in treatment-naive patients with relapsing-remitting multiple sclerosis (RRMS).
METHODS
A systems-level approach combined with glycan array technologies was used to determine specificities and binding reactivities of glycan-specific IgGs in treatment-naive patients with RRMS compared with patients with noninflammatory and other inflammatory neurologic diseases.
RESULTS
We identified a unique signature of glycan-binding IgG in MS with high reactivities to the dietary xenoglycan N-glycolylneuraminic acid (Neu5Gc) and the self-glycan N-acetylneuraminic acid (Neu5Ac). Increased reactivities of serum IgG toward Neu5Gc and Neu5Ac were additionally observed in an independent, treatment-naive cohort of patients with RRMS.
CONCLUSION
Patients with MS show increased IgG reactivities to structurally related xenogeneic and human neuraminic acids. The discovery of these glycan-specific epitopes as immune targets and potential biomarkers in MS merits further investigation.
To explore the repertoire of glycan-specific immunoglobulin G (IgG) antibodies in treatment-naive patients with relapsing-remitting multiple sclerosis (RRMS).
METHODS
A systems-level approach combined with glycan array technologies was used to determine specificities and binding reactivities of glycan-specific IgGs in treatment-naive patients with RRMS compared with patients with noninflammatory and other inflammatory neurologic diseases.
RESULTS
We identified a unique signature of glycan-binding IgG in MS with high reactivities to the dietary xenoglycan N-glycolylneuraminic acid (Neu5Gc) and the self-glycan N-acetylneuraminic acid (Neu5Ac). Increased reactivities of serum IgG toward Neu5Gc and Neu5Ac were additionally observed in an independent, treatment-naive cohort of patients with RRMS.
CONCLUSION
Patients with MS show increased IgG reactivities to structurally related xenogeneic and human neuraminic acids. The discovery of these glycan-specific epitopes as immune targets and potential biomarkers in MS merits further investigation.
File(s)
| File | File Type | Format | Size | License | Publisher/Copright statement | Content | |
|---|---|---|---|---|---|---|---|
| von Gunten_ Xenogeneic Neu5Gc and self-glycan Neu5Ac.pdf | Adobe PDF | 655.56 KB | published |