Glycobiology最新文献_第3页

Serum Protein Glycopatterns as Biomarkers for Machine Learning Diagnosis of Major Depressive Disorder. 血清蛋白糖型作为重度抑郁症机器学习诊断的生物标志物。

IF 3.3 3区生物学

Glycobiology Pub Date : 2026-09-21 DOI: 10.1093/glycob/cwag080

Shiyi Wang, Jian Shu, Hanjie Yu, Yue Shi, Chen Zhang, Xinyuan Hu, Zheng Li

{"title":"Serum Protein Glycopatterns as Biomarkers for Machine Learning Diagnosis of Major Depressive Disorder.","authors":"Shiyi Wang, Jian Shu, Hanjie Yu, Yue Shi, Chen Zhang, Xinyuan Hu, Zheng Li","doi":"10.1093/glycob/cwag080","DOIUrl":"https://doi.org/10.1093/glycob/cwag080","url":null,"abstract":"The diagnosis of major depressive disorder (MDD) currently relies on subjective clinical assessment, underscoring the need for objective biomarkers. Glycosylation, a common post-translational modification, is involved in neuroinflammation and immune regulation, both implicated in MDD pathogenesis. This study aimed to identify serum protein glycopatterns as biomarkers for MDD diagnosis and severity stratification. Serum samples from 150 individuals, including healthy volunteers (HV, n = 38), mild-to-moderate MDD (M-MDD, n = 52), and severe MDD (S-MDD, n = 60), were analyzed using lectin microarrays. Thirty-six lectins showed significantly altered binding signals that indicating widespread glycosylation changes between HV, M-MDD, and S-MDD. These features were used to train seven machine-learning models, among which K-nearest neighbours (KNN) performed best, achieving 95.3% ± 2.7% accuracy and an AUC (Micro) of 0.990 ± 0.010 in a nested 5-fold cross-validation framework. In a blinded cohort (n = 71), the KNN model showed accuracies of 0.831, 0.662, and 0.831 for MDD, M-MDD, and S-MDD, respectively. SHAP analysis identified key lectins contributing to classification. These results demonstrated that serum glycopatterns combined with machine learning provided a promising objective tool for MDD diagnosis and severity assessment.","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":" ","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-09-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149012236","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Emerging Paradigms in Glycobiology. 糖生物学的新范式。

IF 3.3 3区生物学

Glycobiology Pub Date : 2026-09-03 DOI: 10.1093/glycob/cwag077

Richard D Cummings

{"title":"Emerging Paradigms in Glycobiology.","authors":"Richard D Cummings","doi":"10.1093/glycob/cwag077","DOIUrl":"https://doi.org/10.1093/glycob/cwag077","url":null,"abstract":"Modern glycobiology is a result of multiple revolutionary and ground-breaking observations that both challenged and eventually changed prior perspectives about the expression and biological roles of glycoconjugates. These sweeping transformations in the field altered concepts that were embedded in what may be termed paradigms. Some prior paradigms included ideas that are still echoed in the current scientific literature, such as glycosylation of proteins is only found on secreted and membrane-associated proteins; glycans do not have clear and specific functions; protein binding to carbohydrates is relatively low affinity and non-specific; and protein glycosylation is relatively random and highly heterogeneous. As prior paradigms reached a crisis in terms of their supportability, they were replaced by new paradigms. The number of such new paradigms is large and documenting them is important. These modern paradigms include the idea that wide-spread modifications of amino acids with different sugars are common, that specific protein glycosylation occurs, the presence of glycoproteins in all cellular compartments, numerous roles of glycans and genes encoding their synthesis in human diseases, and the nature of carbohydrate recognition beyond simple sugars, and many others. Many researchers may not be aware of these emerging paradigms that have been developing in the research community since the 1960s. Here we summarize these new paradigms and some are discussed in detail from an historical perspective. These new paradigms demonstrate the essentiality and novelty of glycans and their biological functions.","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":" ","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-09-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148887117","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Quantitative mapping of glycosaminoglycan secondary structure driven by sulfation and iduronic acid. 硫酸化和伊杜醛酸驱动的糖胺聚糖二级结构的定量图谱。

IF 3.3 3区生物学

Glycobiology Pub Date : 2026-08-23 DOI: 10.1093/glycob/cwag064

Miguel Riopedre-Fernandez, Denys Biriukov, Hector Martinez-Seara

{"title":"Quantitative mapping of glycosaminoglycan secondary structure driven by sulfation and iduronic acid.","authors":"Miguel Riopedre-Fernandez, Denys Biriukov, Hector Martinez-Seara","doi":"10.1093/glycob/cwag064","DOIUrl":"10.1093/glycob/cwag064","url":null,"abstract":"Glycosaminoglycans (GAGs) are extracellular matrix polysaccharides whose sequence variability and chemical modifications, particularly sulfation, generate substantial structural diversity. However, how sulfation patterns and monosaccharide composition encode secondary structure in GAGs is not systematically resolved, and quantitative metrics for classifying these structures are largely lacking. Here, we employ large-scale all-atom molecular dynamics simulations to investigate the molecular origin of secondary structure in sulfated GAGs. We systematically vary sulfation patterns and monosaccharide composition to isolate the factors that promote changes in 3D structure. We show that GAG helical conformations arise from recurrent local compact motifs caused primarily by stabilization of l-iduronic acid in the 1C4 puckering conformation, promoted by 2-O-sulfation or by densely sulfated regions. We also introduce a 2-parameter structural metric that objectively classifies GAG secondary structures and distinguishes heparin helices from related conformations. Together, our results establish a quantitative link between monosaccharide identity, sulfation pattern, and 3D organization of polysaccharide chains, providing a framework for future studies of sequence-structure relationships in GAGs.","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":" ","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-08-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148792233","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Fungal lectins: emerging glyco-immune checkpoint modulators for cancer diagnosis, prognosis, and therapy. 真菌凝集素：用于癌症诊断、预后和治疗的新型糖免疫检查点调节剂。

IF 3.3 3区生物学

Glycobiology Pub Date : 2026-08-23 DOI: 10.1093/glycob/cwag072

Kavita Y Hiremath, Disha Gupta, Maruti J Gurav, Ranit Roy, Amrutha Chidananda, Vishwanath B Chachadi

{"title":"Fungal lectins: emerging glyco-immune checkpoint modulators for cancer diagnosis, prognosis, and therapy.","authors":"Kavita Y Hiremath, Disha Gupta, Maruti J Gurav, Ranit Roy, Amrutha Chidananda, Vishwanath B Chachadi","doi":"10.1093/glycob/cwag072","DOIUrl":"10.1093/glycob/cwag072","url":null,"abstract":"Lectins are non-immunogenic, non-enzymatic proteins distributed across microbes, fungi, plants, invertebrates, and vertebrates. Their carbohydrate-binding specificity forms the basis of diverse biomedical applications, particularly in immunomodulation, prognosis, and diagnosis. Among these, fungal lectins have gained attention as promising biomolecules, although they remain less explored than their plant and animal counterparts. Several fungal lectins, including Aleuria aurantia lectin (AAL), Laetiporus sulphureus lectin (LSL), Marasmius oreades agglutinin (MOA), Agrocybe aegerita galectin (AAG), and Rhizoctonia bataticola lectin (RBL), demonstrate unique biological activities. They regulate immune responses by influencing cytokine expression (e.g. TNF-α, IL-1β, IL-6, IL-10), act on innate and adaptive immune cells, and initiate apoptosis or necrosis via intrinsic and extrinsic pathways. Their diagnostic potential lies in recognizing aberrant glycans such as TF and Tn antigens, while their prognostic relevance is associated with monitoring glycosylation changes during cancer progression. Collectively, fungal lectins represent versatile molecules capable of serving as both functional immunomodulators and sensitive glycan-based probes. Despite extensive in vitro studies, their clinical application remains limited by insufficient in vivo validation and translational research. Advancing fungal lectins into biomedical practice requires systematic evaluation of their safety, specificity, and therapeutic potential. This review consolidates current knowledge on fungal lectins in immunomodulation, prognosis, and diagnostics, and highlights their translational prospects. Future studies should prioritize in vivo evaluation, biosensor integration, and protein engineering approaches to fully exploit fungal lectins as next-generation tools in immunotherapy and precision medicine.","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":" ","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-08-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148905711","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Meeting report on the 2nd GlyCosmos Symposium & Jamboree -community-driven integration of glycan recognition data. 第二届GlyCosmos研讨会暨大会报告-社区驱动的聚糖识别数据整合。

IF 3.3 3区生物学

Glycobiology Pub Date : 2026-08-23 DOI: 10.1093/glycob/cwag055

Yuka Akagi, Chiaki Nagai-Okatani, Eriko Fukuda, Sayaka Fuseya, Masae Hosoda, Chih-Chieh Lin, Kei Miyako, Hiroaki Sakaue, Takashi Sato, Reo Takeda, Issaku Yamada, Kiyoko F Aoki-Kinoshita, Atsushi Kuno

引用次数: 0

Dynamic inter-glycan interactions regulate site-specific N-glycan maturation in human Fcγ receptor III. 动态聚糖间相互作用调节人Fcγ受体III中位点特异性n -聚糖的成熟。

IF 3.3 3区生物学

Glycobiology Pub Date : 2026-08-23 DOI: 10.1093/glycob/cwag075

Yue Zhang, Hirokazu Yagi, Masako Okina, Yutaka Hashimoto, Koichi Kato, Takumi Yamaguchi

{"title":"Dynamic inter-glycan interactions regulate site-specific N-glycan maturation in human Fcγ receptor III.","authors":"Yue Zhang, Hirokazu Yagi, Masako Okina, Yutaka Hashimoto, Koichi Kato, Takumi Yamaguchi","doi":"10.1093/glycob/cwag075","DOIUrl":"10.1093/glycob/cwag075","url":null,"abstract":"Protein N-glycosylation generates diverse glycoforms that influence protein structure and function, yet the molecular rules governing site-specific glycan maturation remain incompletely understood. Accumulating evidence indicates that glycosylation outcomes are shaped by determinants embedded within glycoproteins themselves, beyond enzyme availability alone. Here, we investigate how neighboring glycans modulate site-specific N-glycan maturation in human Fcγ receptor III (FcγRIII). Building on previous glycoproteomic studies showing restricted processing of the N45 glycan in FcγRIII molecules, we combined reciprocal glycosylation-site mutagenesis with molecular dynamics simulations. Introduction of an N64 glycosylation sequon into FcγRIIIa reduced N45 glycan maturation, whereas removal of the N64 sequon from FcγRIIIb produced the reciprocal effect. Simulations using glycan models, analyzed primarily by contact maps and contact frequencies, showed that the N45 glycan dynamically contacts neighboring N64 and N169 glycans. These findings support a model in which the isoform-specific N64 glycan, in addition to the adjacent N169 glycan shared by both FcγRIII isoforms, contributes to reduced N45 glycan maturation by reshaping the local glycan environment around N45.","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":" ","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-08-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13580079/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148963284","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Glyco-Forum.

IF 3.3 3区生物学

Glycobiology Pub Date : 2026-08-23 DOI: 10.1093/glycob/cwag069

引用次数: 0

Functional conservation of divergent peptidase_M60 O-glycopeptidases in enterococcus. 肠球菌中分化肽酶e_m60 o -糖肽酶的功能保护。

IF 3.3 3区生物学

Glycobiology Pub Date : 2026-08-23 DOI: 10.1093/glycob/cwag076

Liam G Mihalynuk, Benjamin Pluvinage, Olivia Canil, Nicole Thompson, Warren Wakarchuk, Alisdair B Boraston

{"title":"Functional conservation of divergent peptidase_M60 O-glycopeptidases in enterococcus.","authors":"Liam G Mihalynuk, Benjamin Pluvinage, Olivia Canil, Nicole Thompson, Warren Wakarchuk, Alisdair B Boraston","doi":"10.1093/glycob/cwag076","DOIUrl":"10.1093/glycob/cwag076","url":null,"abstract":"O-glycopeptidases are proteolytic enzymes that obligately recognize the O-glycans appended to their substrates. Peptidase_M60 proteins comprise a superfamily of putative metal-dependent O-glycopeptidases that were initially described in host-associated bacteria but are now known to be distributed across bacteria occupying both host-associated and environmental niches. Although several members of this superfamily have been shown to possess O-glycopeptidase activity, the family is highly divergent at the amino acid sequence level, making it unclear whether this activity is conserved across all members. Here, we show that two peptidase_M60 enzymes, EfmM60 and EfcM60, from strains of Enterococcus faecium and Enterococcus faecalis, respectively, which are only distantly related at the primary sequence level to previously characterized O-glycopeptidases, exhibit both mucinase and O-glycopeptidase activity. Structural analysis of EfmM60 reveals distinct active-site features relative to previously characterized peptidase_M60 enzymes that provide a molecular basis for its ability to accommodate extended and branched O-glycans. Together, these findings highlight functional conservation within a highly divergent peptidase_M60 family and suggest that enterococcal O-glycopeptidases may contribute to ecological versatility by enabling access to O-glycosylated substrates across diverse biological contexts.","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":" ","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-08-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13580078/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148900362","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

B cell mechanisms underlie IgG glycan alterations in obesity. 肥胖中IgG聚糖改变的B细胞机制

IF 3.3 3区生物学

Glycobiology Pub Date : 2026-08-23 DOI: 10.1093/glycob/cwag070

Jun Peng, Ming Yang, Anika Mijakovac, Ken L Chambliss, Md Nurul Islam, Tamara Štambuk, Domagoj Kifer, Kenian Chen, Iwona Borošak, Helena Deriš, Kristina Nikolić Prpić, Nancy Monson, Ildiko Lingvay, Olga T Gupta, Vlatka Zoldoš, Gordan Lauc, Jacob Hartz, Lin Xu, Chieko Mineo, Philip W Shaul

{"title":"B cell mechanisms underlie IgG glycan alterations in obesity.","authors":"Jun Peng, Ming Yang, Anika Mijakovac, Ken L Chambliss, Md Nurul Islam, Tamara Štambuk, Domagoj Kifer, Kenian Chen, Iwona Borošak, Helena Deriš, Kristina Nikolić Prpić, Nancy Monson, Ildiko Lingvay, Olga T Gupta, Vlatka Zoldoš, Gordan Lauc, Jacob Hartz, Lin Xu, Chieko Mineo, Philip W Shaul","doi":"10.1093/glycob/cwag070","DOIUrl":"10.1093/glycob/cwag070","url":null,"abstract":"Insulin resistance is a major complication of obesity. In adults with obesity insulin resistance is associated with a hyposialylation of the Fc-linked glycan on IgG, and a causal link between IgG hyposialylation and glucose dysregulation has been demonstrated in obese mice. What is unknown is how obesity causes the changes in IgG glycosylation. To avoid factors besides obesity that may influence IgG glycosylation, we sought to fill this knowledge gap by studying adolescents with and without obesity. We demonstrate that in pediatric obesity IgG is hyposialylated and hypogalactosylated, with the changes most apparent in females, and that this is related to an upregulation of B cell WNT3, a GWAS-identified candidate gene for IgG glycosylation whose function in glycan modulation was previously unknown. In parallel, WNT3 is upregulated in B cells from obese mice. Linkage between WNT3 upregulation and decreased IgG galactosylation and sialylation was demonstrated in both a HEK293FS cell model and an ARH-77 B lymphoblast cell line. These observations indicate that obesity causes IgG hypogalactosylation and resulting hyposialylation by previously unrecognized actions of WNT3 which regulate IgG galactosylation in B cells. Better understanding of how obesity alters the unique glycobiology of IgG offers the possibility of identifying additional therapeutic targets in the battle against the insulin resistance that complicates obesity.","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":" ","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-08-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13574287/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148857276","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

The state of Glycobiology research in the African continent: urgent need for reinvigoration. 非洲大陆糖生物学研究的现状：迫切需要振兴。

IF 3.3 3区生物学

Glycobiology Pub Date : 2026-08-23 DOI: 10.1093/glycob/cwag073

Mohammed Auwal Ibrahim, Mohammed Aliyu Usman, Aliyu Dantani Abdullahi, Murtala Bindawa Isah, Auwal Adamu

引用次数: 0