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Latest Insights into Glycobiology

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".

Deadline for manuscript submissions: 20 May 2026 | Viewed by 3909

Special Issue Editors

Dr. Csaba Váradi

E-Mail Website
Guest Editor
Institute of Chemistry, Faculty of Materials Science and Engineering, University of Miskolc, 3515 Miskolc, Hungary
Interests: liquid-chromatography; mass-spectrometry; glycosylation; biomarker discovery
Prof. Dr. Cheorl-Ho Kim

E-Mail Website
Guest Editor
1. Department of Biological Sciences, College of Science, Sungkyunkwan University, Seoburo 2066, Suwon 16419, Republic of Korea
2. Samsung Advanced Institute of Health Science and Technology (SAIHST), Sungkyunkwan University, Seoul 06351, Republic of Korea
Interests: glycobiology; sialobiology; sialyltransferase; N-glycan; O-glycan; glycolipid; sphingolipid; glycoprotein; surface sugar; ganglioside; sialic acid; sialyl Le antigen; lectin; galectin; siglec; ER-Golgi glyosylation; sugar–receptor interaction; innate immune; xenotransplantation; cell–cell interaction
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Glycobiology, the study of glycans and their roles in biological systems, is experiencing rapid advancements, offering profound insights into health and disease. Recent discoveries highlight the immense structural diversity of glycans and their pivotal functions in cell–cell communication, immune modulation, and molecular recognition. Technological innovations, including high-resolution mass spectrometry and glycan microarrays, have enhanced our ability to analyze glycan structures, driving significant progress in the field. Abnormal glycosylation patterns are increasingly linked to various diseases, such as cancer, neurodegenerative disorders, and infectious diseases, providing new targets for therapeutic interventions and biomarker discovery. Glycans are also recognized for their critical role in modulating immune responses, influencing pathogen recognition and inflammation, thus offering novel pathways for immunotherapy development. Advances in glycoengineering are facilitating the creation of glycoproteins with improved therapeutic properties, which is pivotal in the development of biopharmaceuticals and vaccines. Additionally, glycans are key mediators in host–microbe interactions, essential for understanding microbial colonization and immune evasion. The field of glycobiology is benefiting from interdisciplinary collaborations, integrating genomics, proteomics, and bioinformatics to deepen our understanding of glycan functions. These insights are paving the way for innovative applications in medicine and biotechnology, highlighting the expanding role of glycobiology in addressing complex biological challenges.

Dr. Csaba Váradi
Prof. Dr. Cheorl-Ho Kim
Guest Editors

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Keywords

  • glycosylation
  • biomarkers
  • separation techniques
  • mass spectrometry
  • multivariate data analysis

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Published Papers (4 papers)

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Research

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19 pages, 2591 KB  
Article
Integrated Glyco-Analytical Strategy for Comprehensive Characterization of a Complex Therapeutic Glycoprotein: Fabrazyme
by Mikhail Afonin, Polina Novikova, Andrei Vinalev and Natalia Mesonzhnik
Int. J. Mol. Sci. 2026, 27(8), 3358; https://doi.org/10.3390/ijms27083358 - 8 Apr 2026
Viewed by 218
Abstract
Fabrazyme (agalsidase beta) is a therapeutic enzyme whose clinical efficacy is contingent upon its complex N-glycosylation patterns. Nevertheless, comprehensive glycosylation profiling remains challenging due to high site-specific heterogeneity. To address this, three orthogonal liquid chromatography–mass spectrometry (LC-MS) approaches were employed: (1) released N-glycan [...] Read more.
Fabrazyme (agalsidase beta) is a therapeutic enzyme whose clinical efficacy is contingent upon its complex N-glycosylation patterns. Nevertheless, comprehensive glycosylation profiling remains challenging due to high site-specific heterogeneity. To address this, three orthogonal liquid chromatography–mass spectrometry (LC-MS) approaches were employed: (1) released N-glycan analysis with fluorescence detection and MS annotation, (2) site-specific glycopeptide mapping, and (3) intact protein MS. The released glycan profiling method was validated for reproducibility, intermediate precision, and inter-laboratory transferability, thereby enabling reliable separation and quantification of neutral, phosphorylated, and sialylated species. Glycopeptide mapping revealed distinct site-specific distributions: N108 was found to predominantly carry sialylated complex glycans; N161 was enriched in phosphorylated oligomannose structures; and N184 displayed the highest heterogeneity, including bisphosphorylated and sialylated glycans. Intact protein analysis was performed on both intact and desialylated Fabrazyme, thereby enabling confirmation of glycan assignments. Desialylation reduced spectral complexity, thereby facilitating accurate mass matching with a combinatorial library generated from glycopeptide-level data. The complementary use of these three analytical levels provides a comprehensive view of Fabrazyme glycosylation, offering a robust reference for quality control and biosimilar development. Full article
(This article belongs to the Special Issue Latest Insights into Glycobiology)
16 pages, 2325 KB  
Article
Effects of Catfish Egg Lectin on Cancer Cells Differ According to the Globotriaosylceramide Species They Express
by Shigeki Sugawara, Kohtaro Kikuchi, Takeo Tatsuta, Tsutomu Fujimura and Masahiro Hosono
Int. J. Mol. Sci. 2025, 26(19), 9278; https://doi.org/10.3390/ijms26199278 - 23 Sep 2025
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Abstract
Silurus asotus (Amur catfish) egg lectin (SAL) inhibits cell proliferation and enhances the effects of anticancer drugs by binding to globotriaosylceramide (Gb3) on the cell surface. Gb3 expression is typically increased in seminomas. However, its association with SAL and the underlying mechanisms remain [...] Read more.
Silurus asotus (Amur catfish) egg lectin (SAL) inhibits cell proliferation and enhances the effects of anticancer drugs by binding to globotriaosylceramide (Gb3) on the cell surface. Gb3 expression is typically increased in seminomas. However, its association with SAL and the underlying mechanisms remain unclear. Here, we investigated the effects of SAL on morphology, migratory ability, and integrin expression in JKT-1 cells using chromatography and mass spectrometry. Gb3 was expressed in JKT-1, an established seminoma cell line. SAL did not alter JKT-1 proliferation but increased propidium iodide uptake. Furthermore, SAL induced morphological changes and increased the expression of integrin α2 in JKT-1, but not in HeLa cells. Gb3 expression was detected in JKT-1 and HeLa cells, with high- and low-mobility bands observed. However, the low-mobility bands were more abundant in JKT-1 than in HeLa cells. The main forms of Gb3 in JKT-1 cells were high-mobility d18:1/24:0 and d18:1/24:1 and low-mobility hydroxylated Gb3. Fatty acid 2-hydroxylase was involved in the acyl chain hydroxylation of low-mobility Gb3 in JKT-1 cells and showed 5-fold higher expression in JKT-1 cells than in HeLa cells. Our findings suggest that the antitumor effects of SAL vary according to the specific Gb3 molecular species expressed in cancer cells. Full article
(This article belongs to the Special Issue Latest Insights into Glycobiology)
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14 pages, 1949 KB  
Article
Transparent Machine Learning Reveals Diagnostic Glycan Biomarkers in Subarachnoid Hemorrhage and Vasospasm
by Attila Garami, Máté Czabajszki, Béla Viskolcz, Csaba Oláh and Csaba Váradi
Int. J. Mol. Sci. 2025, 26(16), 7727; https://doi.org/10.3390/ijms26167727 - 10 Aug 2025
Viewed by 1534
Abstract
Subarachnoid hemorrhage (SAH) and its major complication, cerebral vasospasm (CVS), present significant challenges for early diagnosis and risk stratification. In this study, we developed interpretable decision tree models to differentiate between healthy controls, SAH patients, and SAH patients with vasospasm using serum N-glycomic [...] Read more.
Subarachnoid hemorrhage (SAH) and its major complication, cerebral vasospasm (CVS), present significant challenges for early diagnosis and risk stratification. In this study, we developed interpretable decision tree models to differentiate between healthy controls, SAH patients, and SAH patients with vasospasm using serum N-glycomic data. Building on previously published glycomic profiles, we introduced a refined modeling approach combining systematic preprocessing, feature selection, and interpretable machine learning. Our methodology included outlier removal, standard scaling, and a novel correlation-based feature reduction guided by feature importance scores derived from preliminary decision trees. Binary classification tasks (Control vs. SAH and Control vs. CVS, and SAH vs. CVS) were evaluated through stratified repeated cross-validation and hyperparameter optimization. Models achieved high accuracy (up to 0.91) and stable F1-scores across configurations. Key glycans such as FA2(6)G1 (bi-antennary, fucosylated, monogalactosylated), A4G4S3(2) (tetra-antennary, tetra-galactosylated, tri-sialylated), and A3G3S3(5) (tri-antennary, tri-galactosylated, tri-sialylated) emerged as the most discriminative. Visualizations that combine joint feature distributions and decision boundaries provided intuitive insight into the classifier’s logic. These findings support the integration of interpretable glycomics-based models into clinical workflows. Full article
(This article belongs to the Special Issue Latest Insights into Glycobiology)
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Review

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30 pages, 6304 KB  
Review
The α-Gal Epitope (Galα1-3Galβ1-4GlcNAc) as Therapeutic Agent in Cancer Immunotherapy, Vaccine Effectiveness Amplification and Injured Tissue Regeneration
by Uri Galili
Int. J. Mol. Sci. 2026, 27(6), 2737; https://doi.org/10.3390/ijms27062737 - 17 Mar 2026
Viewed by 536
Abstract
The α-gal epitope is synthesized in non-primate mammals and New-World monkeys by the glycosylation enzyme α1,3galactosyltransferase (α1,3GT), encoded by the GGTA1 gene. Ancestral Old-World monkeys and apes synthesizing α-gal epitopes underwent extinction 20–30 million years ago. Their mutated offspring, with the inactivated GGTA1 [...] Read more.
The α-gal epitope is synthesized in non-primate mammals and New-World monkeys by the glycosylation enzyme α1,3galactosyltransferase (α1,3GT), encoded by the GGTA1 gene. Ancestral Old-World monkeys and apes synthesizing α-gal epitopes underwent extinction 20–30 million years ago. Their mutated offspring, with the inactivated GGTA1 gene, survived and produced the natural anti-Gal antibody, specifically binding α-gal epitopes. Anti-Gal protected the surviving offspring from lethal viruses presenting α-gal epitopes, which killed α-gal-synthesizing parental primates. Anti-Gal constitutes ~1% of human immunoglobulins and is also produced in Old-World monkeys and apes. α-Gal epitopes can serve as therapeutic agents in several clinical disciplines: 1. Cancer immunotherapy: Engineering cancer cells to express α-gal epitopes results in anti-Gal binding to these cells and localized activation of the complement system that kills these cancer cells and recruits the antigen-presenting cells (APCs) dendritic cells and macrophages. Anti-Gal bound to cancer cells targets them for robust uptake by APCs, which process internalized tumor antigens (TAs) and transport them to lymph nodes for activation of cytotoxic T-cells. These T-cells kill TA-presenting metastatic tumor cells. Clinical trials demonstrated that such engineering is achieved by intra-tumoral injection of α-gal glycolipids, the use of recombinant α1,3GT, or the use of oncolytic viruses containing the GGTA1 gene. 2. Viral vaccines: Inactivated whole-virus vaccines presenting α-gal epitopes bind anti-Gal, which targets them for extensive uptake by APCs, thereby increasing their immunogenicity by ~100-fold. 3. Injured-tissue regeneration: Anti-Gal binding to α-gal-presenting nanoparticles administered to wounds, into the post-myocardial infarction (MI) injured myocardium and into injured spinal cord, activates the complement system that recruits pro-regenerative macrophages, which orchestrate regeneration by recruiting stem cells and the secretion of pro-regenerative cytokines. All these findings suggest that α-gal/anti-Gal antibody interaction can serve as a novel therapeutic approach, applicable to various clinical settings. Full article
(This article belongs to the Special Issue Latest Insights into Glycobiology)
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