Evidence map›Paper›PMID 41449450›Full record

ReviewJournal of translational medicine2025

Antibody glycosylation in neuroimmune diseases.

Kailin Li, Mengchuan Luo, Liqun Xu, Yuzhen Ouyang, Qian Zhou, Wei Xiang, Yijun Ren, Zeyi Wen, Guanzhong Shi, Zhaohui Luo and 1 more

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Journal of translational medicine, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors.

Kailin LiDepartment of Neurology, Xiangya Hospital, Central South University, Changsha, 410008, China.
Mengchuan LuoDepartment of Neurology, Xiangya Hospital, Central South University, Changsha, 410008, China.
Liqun XuDepartment of Neurology, Xiangya Hospital, Central South University, Changsha, 410008, China.
Yuzhen OuyangDepartment of Neurology, Xiangya Hospital, Central South University, Changsha, 410008, China.
Qian ZhouDepartment of Neurology, Xiangya Hospital, Central South University, Changsha, 410008, China.
Wei XiangDepartment of Neurology, Xiangya Hospital, Central South University, Changsha, 410008, China.
Yijun RenDepartment of Neurology, Xiangya Hospital, Central South University, Changsha, 410008, China.
Zeyi WenDepartment of Neurology, Xiangya Hospital, Central South University, Changsha, 410008, China.
Guanzhong ShiDepartment of Neurology, Xiangya Hospital, Central South University, Changsha, 410008, China.
Zhaohui LuoDepartment of Neurology, Xiangya Hospital, Central South University, Changsha, 410008, China. luozhaohui_xy@csu.edu.cn.
Huan YangDepartment of Neurology, Xiangya Hospital, Central South University, Changsha, 410008, China. 403850@csu.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundGlycosylation, a critical post-translational modification of proteins, is particularly evident in immunoglobulins (Ig), also known as antibodies, and plays a significant role in various neuroimmune diseases. Of particular importance is the N-glycosylation of the crystallizable fragment (Fc) of IgG. It has a straightforward structure and directly impacts antibody effector functions, thus making it a focal point in antibody glycosylation studies.

methodsThis review systematically summarizes characteristic IgG glycosylation patterns in neuroimmune disorders, including multiple sclerosis (MS), neuromyelitis optica spectrum disorders (NMOSD), Guillain–Barré syndrome (GBS), chronic inflammatory demyelinating polyradiculoneuropathies (CIDP), and myasthenia gravis (MG).

resultsA prevailing pattern of reduced IgG galactosylation, sialylation, and core fucosylation has been consistently observed across these diseases, and these alterations are intricately linked to a pro-inflammatory shift in antibody functionality. Beyond pathological mechanisms, this review further explores the potential clinical value of IgG glycosylation, emphasizing its applications as a biomarker and as a target for innovative therapeutic strategies, such as the design of engineered therapeutic monoclonal antibodies and the use of glycosidases.

conclusionsThe specific alteration of IgG glycosylation is a hallmark of neuroimmune diseases, contributing to their pathogenesis and offering substantial translational promise. Harnessing this knowledge for the development of glycosylation-based diagnostics and therapeutics represents a significant frontier in the management of neuroimmune diseases.

Indexed as

AntibodiesNervous System DiseasesAnimalsGlycosylationHumansImmunoglobulin GAntibodiesImmunoglobulin GAntibodyAutoimmune diseasesGlycosylationNeuroimmune diseases

Identifiers

PMID41449450
PMCPMC12903309

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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.