GlycobiologyPub Date : 2025-01-24DOI: 10.1093/glycob/cwaf001
Sean A Burnap, Valeria Calvaresi, Gleysin Cabrera, Satomy Pousa, Miladys Limonta, Yassel Ramos, Luis Javier González, David J Harvey, Weston B Struwe
{"title":"Structural and Functional Glycosylation of the Abdala COVID-19 Vaccine.","authors":"Sean A Burnap, Valeria Calvaresi, Gleysin Cabrera, Satomy Pousa, Miladys Limonta, Yassel Ramos, Luis Javier González, David J Harvey, Weston B Struwe","doi":"10.1093/glycob/cwaf001","DOIUrl":"10.1093/glycob/cwaf001","url":null,"abstract":"<p><p>Abdala is a COVID-19 vaccine produced in Pichia pastoris and is based on the receptor-binding domain (RBD) of the SARS-CoV-2 spike. Abdala is currently approved for use in multiple countries with clinical trials confirming its safety and efficacy in preventing severe illness and death. Although P. pastoris is used as an expression system for protein-based vaccines, yeast glycosylation remains largely uncharacterised across immunogens. Here, we characterise N-glycan structures and their site of attachment on Abdala and show how yeast-specific glycosylation decreases binding to the ACE2 receptor and a receptor-binding motif (RBM) targeting antibody compared to the equivalent mammalian-derived RBD. Reduced receptor and antibody binding is attributed to changes in conformational dynamics resulting from N-glycosylation. These data highlight the critical importance of glycosylation in vaccine design and demonstrate how individual glycans can influence host interactions and immune recognition via protein structural dynamics.</p>","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":" ","pages":""},"PeriodicalIF":3.4,"publicationDate":"2025-01-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11758712/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142970488","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 : 2025-01-24DOI: 10.1093/glycob/cwaf004
Emily Kukan
{"title":"Glyco You Should Know.","authors":"Emily Kukan","doi":"10.1093/glycob/cwaf004","DOIUrl":"https://doi.org/10.1093/glycob/cwaf004","url":null,"abstract":"","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":"35 3","pages":""},"PeriodicalIF":3.4,"publicationDate":"2025-01-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143457661","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 : 2025-01-24DOI: 10.1093/glycob/cwaf005
Ruchi Jaiswal, Yimin Liu, Michael Petriello, Xiangmin Zhang, Zhengping Yi, Charlie Fehl
{"title":"A reference dataset of O-GlcNAc proteins in quadriceps skeletal muscle from mice.","authors":"Ruchi Jaiswal, Yimin Liu, Michael Petriello, Xiangmin Zhang, Zhengping Yi, Charlie Fehl","doi":"10.1093/glycob/cwaf005","DOIUrl":"10.1093/glycob/cwaf005","url":null,"abstract":"<p><p>A key nutrient sensing process in all animal tissues is the dynamic attachment of O-linked N-acetylglucosamine (O-GlcNAc). Determining the targets and roles of O-GlcNAc glycoproteins has the potential to reveal insights into healthy and diseased metabolic states. In cell studies, thousands of proteins are known to be O-GlcNAcylated, but reference datasets for most tissue types in animals are lacking. Here, we apply a chemoenzymatic labeling study to compile a high coverage dataset of quadriceps skeletal muscle O-GlcNAc glycoproteins from mice. Our dataset contains over 550 proteins, and > 80% of the dataset matched known O-GlcNAc proteins. This dataset was further annotated via bioinformatics, revealing the distribution, protein interactions, and gene ontology (GO) functions of these skeletal muscle proteins. We compared these quadriceps glycoproteins with a high-coverage O-GlcNAc enrichment profile from mouse hearts and describe the key overlap and differences between these tissue types. Quadriceps muscles can be used for biopsies, so we envision this dataset to have potential biomedical relevance in detecting aberrant glycoproteins in metabolic diseases and physiological studies. This new knowledge adds to the growing collection of tissues with high-coverage O-GlcNAc profiles, which we anticipate will further the systems biology of O-GlcNAc mechanisms, functions, and roles in disease.</p>","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":" ","pages":""},"PeriodicalIF":3.4,"publicationDate":"2025-01-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143382236","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 : 2025-01-16DOI: 10.1093/glycob/cwae098
Adriani L Felix, Suzane M Penno, Francisco F Bezerra, Paulo A S Mourão
{"title":"Fucosylated chondroitin sulfate, an intriguing polysaccharide from sea cucumber: past, present, and future.","authors":"Adriani L Felix, Suzane M Penno, Francisco F Bezerra, Paulo A S Mourão","doi":"10.1093/glycob/cwae098","DOIUrl":"10.1093/glycob/cwae098","url":null,"abstract":"<p><p>Fucosylated chondroitin sulfate (FCS) is a unique polysaccharide, first described nearly four decades ago, and found exclusively in sea cucumbers. It is a component of the extracellular matrix, possibly associated with peculiar properties of the invertebrate tissue. The carbohydrate features a chondroitin sulfate core with branches of sulfated α-Fuc linked to position 3 of the β-GlcA. FCSs from different species of sea cucumbers share a similar chondroitin sulfate core but the structure of the sulfated α-Fuc branches varies significantly. The predominant pattern consists of a single unit of sulfated α-Fuc, though some species exhibit branches with multiple α-Fuc units. This comprehensive review focuses on four major aspects of FCS. Firstly, we describe the initial approaches to elucidate the structure of FCS using classical methods of carbohydrate chemistry. Secondly, we highlight the impact of two-dimensional NMR methods in consolidating and revealing further details about the structure of FCS. These studies were conducted by various researchers across different countries and involving multiple species of sea cucumbers. Thirdly, we summarize the biological activities reported for FCS. Our survey identified 104 publications involving FCS from 42 species of sea cucumbers, reporting 10 types of biological activities. Most studies focused on anticoagulant and antithrombotic activities. Finally, we discuss future perspectives for studies related to FCS. These studies aim to clarify the evolutionary advantage for sea cucumbers in developing such a peculiar fucosylated glycosaminoglycan. Additionally, there is a need to identify the enzymes and genes involved in the metabolism of this unique carbohydrate.</p>","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":" ","pages":""},"PeriodicalIF":3.4,"publicationDate":"2025-01-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142871861","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 : 2025-01-16DOI: 10.1093/glycob/cwae088
Hui-Jun Zhu, Hang-Yan Dong, Cheng-Rui Qian, Qin-Qin Ma, Rui-Shu Li, Min Fu, Ye He, Ping Lu
{"title":"Intact N-glycopeptide analysis of human platelets reveals a Glycostructure important for platelet function.","authors":"Hui-Jun Zhu, Hang-Yan Dong, Cheng-Rui Qian, Qin-Qin Ma, Rui-Shu Li, Min Fu, Ye He, Ping Lu","doi":"10.1093/glycob/cwae088","DOIUrl":"https://doi.org/10.1093/glycob/cwae088","url":null,"abstract":"<p><p>Glycosylation is an important posttranslational modification in platelets, and the glycosylation pattern is critical for platelet function. To date, the exploration of the roles of various glycoforms in specific platelet functions is largely lacking. In this study, a global analysis of intact N-glycopeptides in human platelets was performed to map all the glycopeptides, glycosites and glycans of platelets. The glycopeptides were enriched by the ZIC- hydrophilic interaction chromatography method and then analyzed by Liquid Chromatography-Tandem Mass Spectrometry analysis. A total of 1,425 intact glycopeptides belonging to 190 N-glycoproteins from human platelets were identified. Moreover, 358 glycans modified 328 glycosites from those glycoproteins. Functional analysis revealed that these glycoproteins are involved mainly in processes and pathways related to platelet adhesion. Among the proteins in these adhesion-related annotations, von Willebrand factor, thrombospondin 1and glycoprotein V were found to contain a possible Lewis y structure, and this finding was further verified by immunoprecipitation assays. As a blood group-related antigen, Lewis y was previously reported to exist in human platelets, but its function remains unclear. Since the glycosylation of von Willebrand factor, thrombospondin 1 and glycoprotein V is involved in platelet-collagen adhesion, the importance of Lewis y on platelet function was evaluated by adhesion assays, which demonstrated that the blockade of Lewis y on platelets decreased the adhesion of platelets to collagen I under both static and flow conditions.</p>","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":"35 2","pages":""},"PeriodicalIF":3.4,"publicationDate":"2025-01-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143023063","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 : 2025-01-16DOI: 10.1093/glycob/cwae097
Jose Carlos Paredes Franco, Maria Lucia Sampaio Güther, Michael A J Ferguson
{"title":"Use of Crithidia fasciculata extract for the facile enzymatic synthesis of GDP-L-[3H]Fucose.","authors":"Jose Carlos Paredes Franco, Maria Lucia Sampaio Güther, Michael A J Ferguson","doi":"10.1093/glycob/cwae097","DOIUrl":"10.1093/glycob/cwae097","url":null,"abstract":"<p><p>For studies involving glycosyltransferases and nucleotide sugar transporters, radioactive nucleotide sugars are critical reagents. Of these, GDP-L-[3H]Fucose is currently commercially unavailable. Here, we present a facile approach for the preparation of GDP-[3H]-L-Fucose, using the enzymatic machinery present in the cytosol of the non-infectious and easily cultivated protozoan, Crithidia fasciculata, and its purification by solid phase extraction ion exchange chromatography.</p>","PeriodicalId":12766,"journal":{"name":"Glycobiology","volume":" ","pages":""},"PeriodicalIF":3.4,"publicationDate":"2025-01-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11738170/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142871863","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}