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Home / Equine Research Bank / Biomolecules / Glycan Signatures on Neutrophils in an Equine Model for Auto...
Biomolecules2025; 15(10); 1444; doi: 10.3390/biom15101444

Glycan Signatures on Neutrophils in an Equine Model for Autoimmune Uveitis.

Abstract: Glycosylation of surface proteins is a crucial post-translational modification that reflects the activation status of neutrophils, the predominant leukocyte subset in humans and horses. Neutrophils have emerged as active contributors to diseases mediated by the adaptive immune system, such as equine recurrent uveitis (ERU), a sight-threatening disease in horses and a unique model for studying the pathogenesis of autoimmune uveitis in humans. Since changes in surface glycosylation can impact neutrophil function, we were interested in the surface glycosylation landscape on neutrophils from healthy horses and the potential changes in surface glyco-signatures in ERU. Using 35 different plant lectins, we outlined a profile of surface-exposed glycan moieties on equine neutrophils and detected significantly increased O-glycosylation in a diseased state through Jacalin (JAC) binding via flow cytometry. Subsequent molecular weight comparison of JAC pull-down assay data and neutrophil proteomics indicated the surface proteins Integrin beta-2 and CUB domain-containing protein 1 as potential anchors for increased O-glycan levels in ERU. These findings give novel insights into neutrophil surface glycosylation in health and disease and propose O-glycosylation as a possible biomarker for autoimmune uveitis.
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Publication Date: 2025-10-12 PubMed ID: 41154673PubMed Central: PMC12562876DOI: 10.3390/biom15101444Google Scholar: Lookup
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  • Journal Article

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

Overview

  • This study investigates changes in sugar molecule patterns (glycosylation) on the surface of neutrophils, a type of white blood cell, in healthy horses compared to those with equine recurrent uveitis (ERU), an autoimmune eye disease.
  • The research identifies increased O-glycosylation on neutrophils in horses with ERU and proposes it as a potential biomarker for autoimmune uveitis.

Introduction to Key Concepts

  • Neutrophils: These are the most abundant leukocytes (white blood cells) in both humans and horses, playing a crucial role in immune defense.
  • Glycosylation: A biochemical process where sugar molecules (glycans) are attached to proteins, affecting protein function and cell communication. Surface protein glycosylation on neutrophils reflects their activation and functional states.
  • Equine Recurrent Uveitis (ERU): A chronic autoimmune eye disease in horses causing repeated inflammation, leading to vision loss. ERU serves as a natural model to understand autoimmune uveitis in humans.

Research Purpose

  • To characterize the pattern of surface-exposed glycans on equine neutrophils in healthy versus ERU-affected horses.
  • To determine if changes in glycosylation, especially O-glycosylation, correlate with disease state, potentially serving as biomarkers or providing insight into disease mechanisms.

Methods

  • Lectin Profiling: The study used 35 different plant lectins, which are proteins that specifically bind to particular glycan structures, to analyze surface glycan patterns on neutrophils by flow cytometry.
  • Jacalin (JAC) Binding Detection: Jacalin is a lectin that binds specifically to O-glycosylated structures. Increased binding to neutrophils suggested higher O-glycosylation in ERU.
  • Protein Identification: Proteins associated with increased O-glycans were identified through a pull-down assay using Jacalin followed by molecular weight comparison and proteomic analysis.

Key Findings

  • Neutrophils from healthy horses exhibit a specific profile of surface glycans detectable by lectin binding.
  • In horses with ERU, there was a significant increase in O-glycosylation on the neutrophil surface, as indicated by enhanced Jacalin binding.
  • Two surface proteins, Integrin beta-2 and CUB domain-containing protein 1, were identified as likely carriers (anchors) of these increased O-glycans in ERU neutrophils.

Implications of the Study

  • The modification of neutrophil surface proteins by O-glycans may influence neutrophil functions such as adhesion, migration, or inflammation during autoimmune uveitis.
  • O-glycosylation changes on neutrophils can potentially serve as biomarkers for early detection or disease monitoring in autoimmune uveitis.
  • Understanding glycosylation patterns in this equine model may provide insights applicable to human autoimmune uveitis, given the similarities in disease mechanisms.

Conclusion

  • This study provides novel information on the glycosylation landscape of neutrophils in health and autoimmune disease, highlighting increased O-glycosylation as a distinguishing feature in ERU.
  • Future research could explore how these glycosylation changes affect neutrophil behavior and contribute to disease progression, as well as validate O-glycosylation as a clinical biomarker.

Cite This Article

APA
Sprenzel CJ, Amann B, Deeg CA, Degroote RL. (2025). Glycan Signatures on Neutrophils in an Equine Model for Autoimmune Uveitis. Biomolecules, 15(10), 1444. https://doi.org/10.3390/biom15101444

Publication

Biomolecules
ISSN: 2218-273X
NlmUniqueID: 101596414
Country: Switzerland
Language: English
Volume: 15
Issue: 10
PII: 1444

Researcher Affiliations

Sprenzel, Carolin J
  • Chair of Physiology, Department of Veterinary Sciences, Ludwig-Maximilians-University Munich, D-82152 Martinsried, Germany.
Amann, Barbara
  • Chair of Physiology, Department of Veterinary Sciences, Ludwig-Maximilians-University Munich, D-82152 Martinsried, Germany.
Deeg, Cornelia A
  • Chair of Physiology, Department of Veterinary Sciences, Ludwig-Maximilians-University Munich, D-82152 Martinsried, Germany.
Degroote, Roxane L
  • Chair of Physiology, Department of Veterinary Sciences, Ludwig-Maximilians-University Munich, D-82152 Martinsried, Germany.

MeSH Terms

  • Animals
  • Neutrophils / metabolism
  • Horses
  • Uveitis / metabolism
  • Uveitis / veterinary
  • Uveitis / immunology
  • Uveitis / pathology
  • Polysaccharides / metabolism
  • Autoimmune Diseases / metabolism
  • Autoimmune Diseases / veterinary
  • Autoimmune Diseases / immunology
  • Glycosylation
  • Disease Models, Animal
  • Horse Diseases / metabolism
  • Horse Diseases / immunology

Grant Funding

  • DFG DE 719/4-4 (to C.A.D) / Deutsche Forschungsgemeinschaft

Conflict of Interest Statement

The authors declare no conflicts of interest.

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