GlycobiologyPub Date : 2026-07-30DOI: 10.1093/glycob/cwag058
Megna Tiwari
{"title":"Glyco you should know.","authors":"Megna Tiwari","doi":"10.1093/glycob/cwag058","DOIUrl":"10.1093/glycob/cwag058","url":null,"abstract":"","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":" ","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-07-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148602178","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}
GlycobiologyPub Date : 2026-06-24DOI: 10.1093/glycob/cwag047
Tetsuya Hirata
{"title":"Glyco you should know.","authors":"Tetsuya Hirata","doi":"10.1093/glycob/cwag047","DOIUrl":"10.1093/glycob/cwag047","url":null,"abstract":"","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":" ","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-06-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148277272","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}
GlycobiologyPub Date : 2026-05-22DOI: 10.1093/glycob/cwag043
Gracie Carlson
{"title":"Glyco you should know.","authors":"Gracie Carlson","doi":"10.1093/glycob/cwag043","DOIUrl":"https://doi.org/10.1093/glycob/cwag043","url":null,"abstract":"","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":"36 7","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-05-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148294792","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}
GlycobiologyPub Date : 2026-05-22DOI: 10.1093/glycob/cwag050
Tingting Zhang, Yongbin Xu, Yupeng Liu, Lingyan Zhu, Jie Chen, Shunchun Wang, Huijun Wang
{"title":"Cell surface Glycans: from recognition technologies and functional editing to medical applications.","authors":"Tingting Zhang, Yongbin Xu, Yupeng Liu, Lingyan Zhu, Jie Chen, Shunchun Wang, Huijun Wang","doi":"10.1093/glycob/cwag050","DOIUrl":"10.1093/glycob/cwag050","url":null,"abstract":"<p><p>Cell-surface glycans play essential roles in cell communication, immune recognition, and disease progression. Their medical applications are supported by two important technological pillars: glycan recognition and glycan editing. This Review focuses on three key directions: recognition technologies, namely, in situ imaging and glycomic profiling, for detecting and profiling glycans; functional editing technologies, including genetic, enzymatic, chemical, and metabolic approaches, for precisely remodelling glycans; and medical applications driven by the synergy between recognition and editing, with a focus on four areas: biomarkers, lectin-based therapies, precision glycan editing, and cancer immunotherapy. Throughout the Review, five representative glycan classes-high-mannose N-glycans, mucin-type O-GalNAc, heparan sulfate, ganglioside GM3, and glycoRNAs-are used as recurring examples wherever possible. This Review offers an integrated perspective to navigate the process by which glycan recognition and editing technologies collectively drive the translation of cell-surface glycan research into clinical practice.</p>","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":" ","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-05-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148338405","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}
GlycobiologyPub Date : 2026-05-22DOI: 10.1093/glycob/cwag038
Sjanie Huang, Iris Harmsen, Moritz Rahm, Takfarinas Kentache, Clara D M van Karnebeek, Afitz Da Silva, Alexey V Pshezhetsky, Emile Van Schaftingen, Alejandro Garanto, Dirk J Lefeber
{"title":"Cellular homeostasis of N-acetylneuraminic acid and non-canonical sialic acids is mediated by human N-acetylneuraminate lyase.","authors":"Sjanie Huang, Iris Harmsen, Moritz Rahm, Takfarinas Kentache, Clara D M van Karnebeek, Afitz Da Silva, Alexey V Pshezhetsky, Emile Van Schaftingen, Alejandro Garanto, Dirk J Lefeber","doi":"10.1093/glycob/cwag038","DOIUrl":"10.1093/glycob/cwag038","url":null,"abstract":"<p><p>Sialic acids are important for cellular communication, with N-acetylneuraminic acid (Neu5Ac) being the canonical form of sialic acid in humans. Presence of non-canonical sialic acids, derived from dietary intake or as metabolic side product, has been linked to immune disorders and cancer. As homeostasis of different sialic acids remains poorly understood in humans, we studied the role of N-acetylneuraminate lyase (NPL) in their catabolism. In vitro expression of NPL in different biological systems revealed broad substrate specificity towards sialic acids and related 2-keto-3-deoxy metabolites. In agreement with the broad substrate specificity, NPL-deficient red blood cells accumulated Neu5Ac and 3-deoxy-d-glycero-d-galacto-nonulosonic acid (KDN). Interestingly, endogenous levels of non-canonical sialic acids, including N-glycolylneuraminic acid (Neu5Gc) and KDN, were depleted in HEK293T cells upon NPL overexpression, while Neu5Ac and CMP-Neu5Ac levels remained stable. This was further confirmed by supplementation with different sialic acids. Detailed analysis of sugar phosphate intermediates of the hexosamine and sialic acid biosynthesis pathways showed strongly elevated ManNAc-6P (N-acetyl-d-mannosamine 6-phosphate) and Neu5Ac-9P, indicating efficient recycling of ManNAc to increase de novo Neu5Ac biosynthesis. However, this recycling was not efficient for Neu5Gc and KDN. While GlcNAc-6P (N-acetyl-d-glucosamine 6-phosphate) levels were slightly elevated, no evidence was found for further metabolism towards GlcN-6P (glucosamine 6-phosphate) and energy production via glycolysis as shown for bacterial neuraminate lyases. In conclusion, human NPL catabolizes a broad range of sialic acids. However, depending on the cellular context, NPL contributes to a net cellular reduction in non-canonical sialic acids, such as KDN, due to a lack of efficient recycling.</p>","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":" ","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-05-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13220900/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147971768","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}
GlycobiologyPub Date : 2026-05-22DOI: 10.1093/glycob/cwag039
Konstantinos Flevaris
{"title":"Glyco you should know.","authors":"Konstantinos Flevaris","doi":"10.1093/glycob/cwag039","DOIUrl":"https://doi.org/10.1093/glycob/cwag039","url":null,"abstract":"","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":"36 7","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-05-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148005204","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}
{"title":"Comprehensive analysis of the skeletal phenotype in Chst14-/- mice: implications for dermatan sulfate in bone structure and strength.","authors":"Yuki Takahashi, Takahiro Yoshizawa, Shuji Mizumoto, Fumiko Ono, Masashi Uehara, Takafumi Watanabe, Shin Shimada, Yuko Nitahara-Kasahara, Shuhei Yamada, Jun Takahashi, Takashi Okada, Tomoki Kosho","doi":"10.1093/glycob/cwag037","DOIUrl":"10.1093/glycob/cwag037","url":null,"abstract":"<p><p>Dermatan sulfate (DS) is a glycosaminoglycan known to contribute to tissue strength through collagen fibril assembly. Musculocontractural Ehlers-Danlos syndrome (mcEDS) caused by pathogenic variants in the gene that encodes carbohydrate sulfotransferase 14 (CHST14) (mcEDS-CHST14) is a representative disorder of DS deficiency. Skeletal lesions, such as progressive spinal deformity and osteoporosis/osteopenia, are significant manifestations of mcEDS-CHST14, which can lead to deterioration in quality of life. To characterize skeletal alterations associated with DS deficiency, we performed comprehensive analyses of the skeletal phenotypes in Chst14 gene-deleted (Chst14-/-) mice. Chst14-/- mice exhibited progressive kyphosis, proximal femoral deformities, and decreased bone strength, as well as reduced trabecular bone mass and structural parameters, from a young age. Qualitative ultrastructural alterations of collagen fibrils in cortical bone were observed in middle-aged Chst14-/- mice by transmission electron microscopy. In addition, cortical bone showed increased expression of receptor activator of NF-κB (Rank), a gene involved in osteoclast differentiation, in middle age. Histomorphometric analyses of cancellous bone demonstrated reduced trabecular structural parameters in Chst14-/- mice, including decreases in bone volume and trabecular number. These findings indicate age-dependent alterations in both cortical and cancellous bone compartments that may contribute to progressive skeletal deformation. The present study provides insight into skeletal alterations associated with mcEDS-CHST14 and highlights a broader role of DS in maintaining bone structure and strength.</p>","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":" ","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-05-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13196589/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147948264","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}
GlycobiologyPub Date : 2026-05-22DOI: 10.1093/glycob/cwag035
Nohelly Derosiers, William Aguilar, Hyeon-Gyu S Lewis, Morgann MacDonald, Avery D Posey
{"title":"Siglec-15 binds mucin-domain glycoproteins with extended glycans and marks an osteoclast-like, matrix remodeling myeloid state in human tumors.","authors":"Nohelly Derosiers, William Aguilar, Hyeon-Gyu S Lewis, Morgann MacDonald, Avery D Posey","doi":"10.1093/glycob/cwag035","DOIUrl":"10.1093/glycob/cwag035","url":null,"abstract":"<p><p>Siglec-15 has emerged as a therapeutic target in cancer, yet the glycan determinants and protein scaffolds that mediate engagement between Siglec-15-expressing myeloid cells and tumor cells remain incompletely defined. Here, we investigated the molecular basis of Siglec-15 recognition of cancer cells and examined transcriptional as well as functional programs associated with Siglec-15 expression in tumor-associated myeloid populations. Using immunoprecipitation-mass spectrometry in the pancreatic cancer cell line AsPC-1, we identified multiple mucin-domain glycoproteins enriched in Siglec-15 pulldowns. Additionally, disruption of glycan structures demonstrated that both complex N-glycans and extended mucin-type O-glycans contribute to optimal Siglec-15 binding. To define the myeloid population associated with Siglec-15 in human tumors, we interrogated publicly available single-cell RNA sequencing datasets and found that SIGLEC15 expression is enriched within a subset of tumor-associated myeloid cells exhibiting transcriptional features linked to osteoclast differentiation and extracellular matrix remodeling. Finally, in a THP-1 coculture model, Siglec-15 was further associated with DAP12-dependent tumor-induced expression of the osteoclast markers ACP5 and MMP9, together with increased release of IL-1β and IL-6. Collectively, these findings identify glycan and glycoprotein features that support Siglec-15 binding to malignant cells and associate SIGLEC15 expression with osteoclast-like and matrix remodeling myeloid programs in human cancers, providing a framework for mechanistic studies of this glyco-immune checkpoint.</p>","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":" ","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-05-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148239157","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}
{"title":"Site-specific N-glycosylation analysis of bovine immunoglobulin M and its secretory form.","authors":"Sudarshan Marihonnaiah, Gnanesh Kumar Belur Shivappa","doi":"10.1093/glycob/cwag040","DOIUrl":"10.1093/glycob/cwag040","url":null,"abstract":"<p><p>Bovine immunoglobulin M (IgM) from serum and colostrum has got considerable attention due to its immunological property against certain human pathogens. N-glycosylation being a key structural modification of IgM wherein glycan diversity exhibits significant role in maintaining its structural integrity and also bio functionalities; glycan heterogeneity in bovine serum and colostrum IgM complexes have not been explored till date. In this study, we have evaluated site-specific glycan heterogeneity of both commercially available bovine serum IgM as well as secretory IgM (sIgM) complex that was purified from bovine colostrum through the generation of N-glycopeptides followed by UHPLC-MS/MS analysis. N-glycosylation sites- N91ST, N260VS, and N307IS in μ heavy chain constant region (IGHM) displayed bi- and tri-antennary complex glycans with varying degree of core fucosylation and sialyation. While N329DT contained mainly oligomannose as well as hybrid glycans, only oligomannose types were present at N490VS. Both N307IS and N490VS indicated differential glycosylation. Glycans of joining chain (JC) were of bi-antennary complex glycans in both serum and colostrum IgM complexes. Glycans processing at individual sites of IGHM and JC were found in part similar to human counterparts yet bovine-specific glycan heterogeneity was observed. Secretory component (SC) of colostrum sIgM revealed mainly LacdiNAc containing bi-antennary complex glycans that differed substantially from human SC containing only LacNAc complex types with both core and terminal fucsoylation. Interestingly, CD5L was found associated with both serum and colostrum IgM complexes. Thus, the insights obtained in the study would form the basis for extended applications of bovine IgM complexes.</p>","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":" ","pages":""},"PeriodicalIF":3.3,"publicationDate":"2026-05-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147963469","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}