3,248 results match your criteria Glycobiology [Journal]


The Minimum Information Required for a Glycomics Experiment (MIRAGE) Project: LC Guidelines.

Glycobiology 2019 Feb 19. Epub 2019 Feb 19.

Beilstein-Institut, Trakehner Str. 7-9, Frankfurt am Main, Germany.

The Minimum Information Required for A Glycomics Experiment (MIRAGE) is an initiative created by experts in the fields of glycobiology, glycoanalytics and glycoinformatics to design guidelines that improve the reporting and reproducibility of glycoanalytical methods. Previously, the MIRAGE Commission has published guidelines for describing sample preparation methods and the reporting of glycan array and mass spectrometry techniques and data collections. Here, we present the first version of guidelines that aim to improve the quality of the reporting of liquid chromatography (LC) glycan data in the scientific literature. Read More

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http://dx.doi.org/10.1093/glycob/cwz009DOI Listing
February 2019

Expanding CSDB_GT glycosyltransferase database with Escherichia coli.

Glycobiology 2019 Jan 31. Epub 2019 Jan 31.

N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Leninsky Prospect 47, Moscow, Russia.

In 2017, we reported a new database on glycosyltransferase (GT) activities, CSDB_GT (http://csdb.glycoscience.ru/gt. Read More

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http://dx.doi.org/10.1093/glycob/cwz006DOI Listing
January 2019

IgA1 hinge-region clustered glycan fidelity is established early during semi-ordered glycosylation by GalNAc-T2.

Glycobiology 2019 Jan 31. Epub 2019 Jan 31.

Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, Birmingham, AL.

GalNAc-type O-glycans are often added to proteins post-translationally in a clustered manner in repeat regions of proteins, such as mucins and IgA1. Observed IgA1 glycosylation patterns show that glycans occur at similar sites with similar structures. It is not clear how the sites and number of glycans added to IgA1, or other proteins, can follow a conservative process. Read More

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http://dx.doi.org/10.1093/glycob/cwz007DOI Listing
January 2019
1 Read

A strategy for generating cancer-specific monoclonal antibodies to aberrant O-glycoproteins: identification of a novel dysadherin-Tn antibody.

Glycobiology 2019 Feb 6. Epub 2019 Feb 6.

Copenhagen Center for Glycomics, Departments of Cellular and Molecular Medicine and Odontology, Faculty of Health Sciences, University of Copenhagen, Blegdamsvej 3, Copenhagen N, Denmark.

Successful application of potent antibody-based T-cell engaging immunotherapeutic strategies is currently limited mainly to hematological cancers. One major reason is the lack of well-characterized antigens on solid tumors with sufficient cancer specific expression. Aberrantly O-glycosylated proteins contain promising cancer-specific O-glycopeptide epitopes suitable for immunotherapeutic applications, but currently only few examples of such antibody epitopes have been identified. Read More

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http://dx.doi.org/10.1093/glycob/cwz004DOI Listing
February 2019

Mass spectrometry analysis reveals aberrant N-glycans in colorectal cancer tissues.

Glycobiology 2019 Jan 30. Epub 2019 Jan 30.

Jiangsu Key Laboratory of Infection and Immunity, Institutes of Biology and Medical Science, Soochow University, 199 Ren-Ai Road, SuZhou, China.

Aberrant glycosylation is strongly correlated with the development of various cancers. Tumor-associated carbohydrate antigens, including N-glycans, are predominantly expressed on the tumor cell surface. Because the incidence of colorectal cancer is high in China, we investigated aberrant N-glycans from colorectal cancer tissues (CRC) in Chinese patients. Read More

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https://academic.oup.com/glycob/advance-article/doi/10.1093/
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http://dx.doi.org/10.1093/glycob/cwz005DOI Listing
January 2019
2 Reads

Hyaluronan histochemistry-A potential new tool to assess the progress of liver disease from simple steatosis to hepatocellular carcinoma.

Glycobiology 2019 Jan 25. Epub 2019 Jan 25.

University of Eastern Finland, Faculty of Health Sciences, School of Medicine, Institute of Biomedicine, Kuopio, Finland.

Non-alcoholic fatty liver disease is among the most common liver diseases worldwide and one cause of cirrhosis that can result in the development of hepatocellular carcinoma (HCC). Hyaluronan (HA) is a high-molecular-mass glycosaminoglycan with diverse functions in tissue injury and repair, for instance, in inflammation and fibrogenesis. The aim of the present study was to investigate the relationships between the HA synthesizing and degrading enzymes in a spectrum of liver pathologies. Read More

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http://dx.doi.org/10.1093/glycob/cwz002DOI Listing
January 2019

Lectins as possible tools for improved urinary bladder cancer management.

Glycobiology 2019 Jan 25. Epub 2019 Jan 25.

Institute of Cell Biology, Faculty of Medicine, University of Ljubljana, Ljubljana, Slovenia.

Urinary bladder cancer is the ninth most common cancer in developed countries with poor prognosis and outcome for the patient due to the challenging diagnosis and limited treatment possibilities. Bladder cancer arises mainly from urothelial cells lining the lumen. Urothelial cells form a three- to five-layered urothelium, which maintains the blood-urine barrier. Read More

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http://dx.doi.org/10.1093/glycob/cwz001DOI Listing
January 2019
1 Read

CHARMM-GUI Glycan Modeler for Modeling and Simulation of Carbohydrates and Glycoconjugates.

Glycobiology 2019 Jan 25. Epub 2019 Jan 25.

Departments of Biological Sciences and Bioengineering, Lehigh University, Bethlehem, PA, USA.

Characterizing glycans and glycoconjugates in the context of three-dimensional structures is important in understanding their biological roles and developing efficient therapeutic agents. Computational modeling and molecular simulation have become an essential tool complementary to experimental methods. Here, we present a computational tool, Glycan Modeler for in silico N-/O-glycosylation of the target protein and generation of carbohydrate-only systems. Read More

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https://academic.oup.com/glycob/advance-article/doi/10.1093/
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http://dx.doi.org/10.1093/glycob/cwz003DOI Listing
January 2019
3 Reads

Changes in the physico-chemical properties of the xanthan produced by Xanthomonas citri subsp. citri in grapefruit leaf extract.

Glycobiology 2019 Mar;29(3):269-278

Instituto de Ciencia y Tecnología Dr. César Milstein, Fundación Pablo Cassará, Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Saladillo 2468 (C1440FFX), Ciudad de Buenos Aires, Argentina.

Xanthan is a virulence factor produced by Xanthomonas spp. We previously demonstrated that this exopolysaccharide is not only essential for pathogenicity by contributing with bacterial survival but also its pyruvate substituents interfere with some plant defense responses. Deepening our studies about xanthan properties and structure, the aim of this work was to analyze the characteristics of xanthan produced by Xanthomonas in different culture media. Read More

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http://dx.doi.org/10.1093/glycob/cwy114DOI Listing
March 2019
1 Read

Trypanosoma cruzi13C-labeled O-Glycan standards for mass spectrometry.

Glycobiology 2019 Jan 12. Epub 2019 Jan 12.

Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, USA.

Trypanosoma cruzi is a protozoan parasite that causes Chagas disease, a debilitating condition that affectsover 10 million humans in the American continents. In addition to its traditional mode of human entry via the 'kissing bug' in endemic areas, the infection can also be spread in non-endemic countries through blood transfusion, organ transplantation, eating food contaminated with the parasites, and from mother to fetus. Previous NMR-based studies established that the parasite expresses a variety of strain-specific and developmentally-regulated O-glycans that may contribute to virulence. Read More

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http://dx.doi.org/10.1093/glycob/cwy111DOI Listing
January 2019

Alterations in sialic-acid O-acetylation glycoforms during murine erythrocyte development.

Glycobiology 2019 Mar;29(3):222-228

Ragon Institute of MGH, MIT and Harvard, Cambridge, MA, USA.

We used Casd1-deficient mice to confirm that this enzyme is responsible for 9-O-acetylation of sialic acids in vivo. We observed a complete loss of 9-O-acetylation of sialic acid on the surface of myeloid, erythroid and CD4+ T cells in Casd1-deficient mice. Although 9-O-acetylation of sialic acids on multiple hematopoietic lineages was lost, there were no obvious defects in hematopoiesis. Read More

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https://academic.oup.com/glycob/advance-article/doi/10.1093/
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http://dx.doi.org/10.1093/glycob/cwy110DOI Listing
March 2019
7 Reads
3.147 Impact Factor

Absence of a human ortholog of rodent Kupffer cell galactose-binding receptor encoded by the CLEC4f gene.

Glycobiology 2018 Dec 24. Epub 2018 Dec 24.

Department of Life Sciences, Imperial College, London SW7 2AZ United Kingdom.

The murine CLEC4f gene encodes the Kupffer cell receptor, a galactose-binding receptor containing a C-type carbohydrate-recognition domain. Orthologs have been identified in nearly 100 species. The receptors from rat and mouse have previously been characterized and data presented here show that functional CLEC4f protein is expressed in domestic cattle (Bos taurus). Read More

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https://academic.oup.com/glycob/advance-article/doi/10.1093/
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http://dx.doi.org/10.1093/glycob/cwy113DOI Listing
December 2018
4 Reads

Total loss of GM3 synthase activity by a normally processed enzyme in a novel variant and in all ST3GAL5 variants reported to cause a distinct congenital disorder of glycosylation.

Glycobiology 2019 Mar;29(3):229-241

Department of Medicine and Surgery (DMC), University of Insubria, via JH Dunant 5, Varese, Italy.

ST3GAL5-CDG is a rare syndrome which is caused by variant GM3 synthases, the enzyme involved in the biosynthesis of a-b-c-series gangliosides. Here we report a novel homozygous ST3GAL5 variant, p.Gly342Ser, in a patient suffering from failure to thrive, severe hearing, visual, motor, and cognitive impairment, and respiratory chain dysfunction. Read More

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http://dx.doi.org/10.1093/glycob/cwy112DOI Listing

Transcription of human β4-galactosyltransferase 3 is regulated by differential DNA binding of Sp1/Sp3 in SH-SY5Y human neuroblastoma and A549 human lung cancer cell lines.

Glycobiology 2019 Mar;29(3):211-221

Laboratory of Glycobiology, Department of Bioengineering, Nagaoka University of Technology, Nagaoka, Niigata, Japan.

Poor prognosis of neuroblastoma patients has been shown to be associated with increased expression of β4-galactosyltransferase (β4GalT) 3. To address the underlying mechanism of the increased expression of β4GalT3, the transcriptional regulation of the human β4GalT3 gene was investigated in SH-SY5Y human neuroblastoma cell line comparing with A549 human lung cancer cell line, in which the β4GalT3 gene expression was the lowest among four cancer cell lines examined. The core promoter region was identified between nucleotides -69 and -6 relative to the transcriptional start site, and the same region was utilized in both cell lines. Read More

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http://dx.doi.org/10.1093/glycob/cwy109DOI Listing

Active site complementation and hexameric arrangement in the GH family 29; a structure-function study of α-l-fucosidase isoenzyme 1 from Paenibacillus thiaminolyticus.

Glycobiology 2019 01;29(1):59-73

Laboratory of Structure and Function of Biomolecules, Institute of Biotechnology of the Czech Academy of Sciences, v.v.i., Biocev, Vestec, Czech Republic.

α-l-Fucosidase isoenzyme 1 from bacterium Paenibacillus thiaminolyticus is a member of the glycoside hydrolase family GH29 capable of cleaving l-fucose from nonreducing termini of oligosaccharides and glycoconjugates. Here we present the first crystal structure of this protein revealing a novel quaternary state within this family. The protein is in a unique hexameric assembly revealing the first observed case of active site complementation by a residue from an adjacent monomer in this family. Read More

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http://dx.doi.org/10.1093/glycob/cwy078DOI Listing
January 2019
1 Read

Identification of abnormal fucosylated-glycans recognized by LTL in saliva of HBV-induced chronic hepatitis, cirrhosis, and hepatocellular carcinoma.

Glycobiology 2019 Mar;29(3):242-259

Laboratory for Functional Glycomics, College of Life Sciences, Northwest University, Xi'an, China.

The hepatitis B virus (HBV)-induced chronic liver diseases are serious health threats worldwide. There is evidence to display the alterations of salivary N-linked glycans related to the development of HBV-infected liver diseases. Here, we further investigated the alterations of fucosylated N/O-glycans recognized by LTL in saliva from 120 subjects (30 healthy volunteers (HV), 30 patients with hepatitis B (HB), 30 patients with hepatic cirrhosis (HC), and 30 patients with hepatocellular carcinoma (HCC)) using salivary microarrys and MALDI-TOF/TOF-MS. Read More

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http://dx.doi.org/10.1093/glycob/cwy108DOI Listing

In vitro acellular method to reveal O-fucosylation on EGF-like domains.

Glycobiology 2018 Nov 29. Epub 2018 Nov 29.

Univ. Limoges, PEIRENE, EA 7500, Glycosylation and cell differentiation, F-87000 Limoges, France.

A hundred of human proteins have one or more EGF-like domains (EGF-LD) bearing the O-fucosylation consensus motif C2X4(S/T)C3 but to date, only a few of them have been shown to be O-fucosylated. The protein O-fucosyltransferase (POFUT1) specifically recognizes correctly folded EGF-LD of the human EGF (hEGF) type and transfers fucose on serine or threonine residue within the O-fucosylation motif. Here, we propose a strategy for a rapid screening for ability of any EGF-LD to be O-fucosylated, using copper-catalyzed azide-alkyne cycloaddition (CuAAC). Read More

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http://dx.doi.org/10.1093/glycob/cwy106DOI Listing
November 2018
1 Read

Globo-series glycosphingolipids enhance Toll-like receptor 4-mediated inflammation and play a pathophysiological role in diabetic nephropathy.

Glycobiology 2019 Mar;29(3):260-268

Division of Glycopathology, Institute of Molecular Biomembrane and Glycobiology, Tohoku Medical and Pharmaceutical University, Sendai, Japan.

Alteration of glycosphingolipid (GSL) expression plays key roles in the pathogenesis and pathophysiology of many important human diseases, including cancer, diabetes and glycosphingolipidosis. Inflammatory processes are involved in development and progression of diabetic nephropathy, a major complication of type 2 diabetes mellitus. GSLs are known to play roles in inflammatory responses in various diseases, and levels of renal GSLs are elevated in mouse models of diabetic nephropathy; however, little is known regarding the pathophysiological role of these GSLs in this disease process. Read More

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http://dx.doi.org/10.1093/glycob/cwy105DOI Listing

Transcriptional activation of fucosyltransferase (FUT) genes using the CRISPR-dCas9-VPR technology reveals potent N-glycome alterations in colorectal cancer cells.

Glycobiology 2019 02;29(2):137-150

Amsterdam UMC, Vrije Universiteit Amsterdam, Department of Molecular Cell Biology and Immunology, Cancer Center Amsterdam, Amsterdam Infection & Immunity Institute, HZ Amsterdam, the Netherlands.

Aberrant fucosylation in cancer cells is considered as a signature of malignant cell transformation and it is associated with tumor progression, metastasis and resistance to chemotherapy. Specifically, in colorectal cancer cells, increased levels of the fucosylated Lewisx antigen are attributed to the deregulated expression of pertinent fucosyltransferases, like fucosyltransferase 4 (FUT4) and fucosyltransferase 9 (FUT9). However, the lack of experimental models closely mimicking cancer-specific regulation of fucosyltransferase gene expression has, so far, limited our knowledge regarding the substrate specificity of these enzymes and the impact of Lewisx synthesis on the glycome of colorectal cancer cells. Read More

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http://dx.doi.org/10.1093/glycob/cwy096DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6330019PMC
February 2019

A widely compatible expression system for the production of highly O-GlcNAcylated recombinant protein in Escherichia coli.

Glycobiology 2018 12;28(12):949-957

Key Laboratory of Marine Drugs, Ministry of Education, School of Medicine and Pharmacy, Ocean University of China, 5 Yushan Road, Qingdao, China.

O-GlcNAcylation is a ubiquitous and dynamic post-translational modification on serine/threonine residues of nucleocytoplasmic proteins in metazoa, which plays a critical role in numerous physiological and pathological processes. But the O-GlcNAcylation on most proteins is often substoichiometric, which hinders the functional study of the O-GlcNAcylation. This study aimed to improve the production of highly O-GlcNAcylated recombinant proteins in Escherichia coli (E. Read More

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http://dx.doi.org/10.1093/glycob/cwy077DOI Listing
December 2018
12 Reads

UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase is indispensable for oogenesis, oocyte-to-embryo transition, and larval development of the nematode Caenorhabditis elegans.

Glycobiology 2019 02;29(2):163-178

Department of Biology, Faculty of Sciences, Kyushu University, Fukuoka, Japan.

N-linked glycosylation of proteins is the most common post-translational modification of proteins. The enzyme UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase (DPAGT1) catalyses the first step of N-glycosylation, and DPAGT1 knockout is embryonic lethal in mice. In this study, we identified the sole orthologue (algn-7) of the human DPAGT1 in the nematode C. Read More

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http://fdslive.oup.com/www.oup.com/pdf/production_in_progres
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http://dx.doi.org/10.1093/glycob/cwy104DOI Listing
February 2019
10 Reads

An efficient use of X-ray information, homology modeling, molecular dynamics and knowledge-based docking techniques to predict protein-monosaccharide complexes.

Glycobiology 2019 02;29(2):124-136

Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, Intendente Guiraldes 2160, Ciudad Autónoma de Buenos Aires, Argentina.

Unraveling the structure of lectin-carbohydrate complexes is vital for understanding key biological recognition processes and development of glycomimetic drugs. Molecular Docking application to predict them is challenging due to their low affinity, hydrophilic nature and ligand conformational diversity. In the last decade several strategies, such as the inclusion of glycan conformation specific scoring functions or our developed solvent-site biased method, have improved carbohydrate docking performance but significant challenges remain, in particular, those related to receptor conformational diversity. Read More

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https://academic.oup.com/glycob/advance-article/doi/10.1093/
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http://dx.doi.org/10.1093/glycob/cwy102DOI Listing
February 2019
24 Reads

The Lec5 glycosylation mutant links homeobox genes with cholesterol and lipid-linked oligosaccharides.

Glycobiology 2019 02;29(2):106-109

Department of Pharmacology, UT Southwestern Medical Center, 6001 Forest Park Rd., Dallas, TX, USA.

Discovered 40 years ago, the Lec5 glycosylation mutant cell line has a complex recessive genotype and is characterized by accumulation of lipid-linked oligosaccharide assembly intermediates, reduced conversion of polyprenols to dolichols, and an unusual phenotypic dependence upon cell culture conditions such as temperature, plating density and medium quality. The heritable defect in Lec5 is unknown. Here we demonstrate an unexpected epigenetic basis for Lec5, with a surprising linkage to increased expression of homeobox genes, which in turn is associated with increased transcription of cholesterol biosynthesis genes. Read More

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http://dx.doi.org/10.1093/glycob/cwy103DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6330018PMC
February 2019
3.150 Impact Factor

Galectin-9 induces atypical ubiquitination leading to cell death in PC-3 prostate cancer cells.

Glycobiology 2019 01;29(1):22-35

Division of Research Instrument and Equipment, Life Science Research Center, Kagawa, Japan.

Galectin-9 is the most potent inducer of cell death in lymphomas and other malignant cell types among the members of the galectin family. We investigated the mechanism of galectin-9-induced cell death in PC-3 prostate cancer cells in comparison with in Jurkat T cells. Galectin-9 induced apoptotic cell death in Jurkat cells, as typically revealed by DNA ladder formation. Read More

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https://academic.oup.com/glycob/advance-article/doi/10.1093/
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http://dx.doi.org/10.1093/glycob/cwy099DOI Listing
January 2019
2 Reads

Serine-rich repeat protein adhesins from Lactobacillus reuteri display strain specific glycosylation profiles.

Glycobiology 2019 01;29(1):45-58

The Gut Microbes and Health Institute Strategic Programme, Quadram Institute Bioscience, Norwich Research Park, Norwich, UK.

Lactobacillus reuteri is a gut symbiont inhabiting the gastrointestinal tract of numerous vertebrates. The surface-exposed serine-rich repeat protein (SRRP) is a major adhesin in Gram-positive bacteria. Using lectin and sugar nucleotide profiling of wild-type or L. Read More

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https://academic.oup.com/glycob/advance-article/doi/10.1093/
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http://dx.doi.org/10.1093/glycob/cwy100DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6291802PMC
January 2019
5 Reads
3.150 Impact Factor

Elucidation of the O-antigen structure of Escherichia coli O63.

Glycobiology 2019 02;29(2):179-187

Department of Organic Chemistry, Arrhenius Laboratory, Stockholm University, Stockholm, Sweden.

The structure of the O-antigen polysaccharide (PS) from the Shiga-toxin producing Escherichia coli O63 has been elucidated using a combination of bioinformatics, component analyses and NMR spectroscopy. The O-antigen is comprised of tetrasaccharide repeating units with the following structure: →2)-β-d-Quip3N(d-allo-ThrAc)-(1→2)-β-d-Ribf-(1→4)-β-d-Galp-(1→3)-α-d-GlcpNAc-(1→ in which the N-acetylated d-allo-threonine is amide-linked to position 3 of the 3-amino-3-deoxy-d-Quip sugar residue. The presence of a predicted flippase and polymerase encoded in the O63 gene cluster is consistent with the Wzx/Wzy biosynthetic pathway and consequently the biological repeating unit has likely an N-acetyl-d-glucosamine residue at its reducing end. Read More

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https://academic.oup.com/glycob/advance-article/doi/10.1093/
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http://dx.doi.org/10.1093/glycob/cwy098DOI Listing
February 2019
9 Reads

Sequence-to-structure dependence of isolated IgG Fc complex biantennary N-glycans: a molecular dynamics study.

Glycobiology 2019 01;29(1):94-103

Department of Chemistry.

Fc glycosylation of human immunoglobulins G (IgGs) is essential for their structural integrity and activity. Interestingly, the specific nature of the Fc glycoforms is known to modulate the IgG effector function and inflammatory properties. Indeed, while core-fucosylation of IgG Fc-glycans greatly affects the antibody-dependent cell-mediated cytotoxicity function, with obvious repercussions in the design of therapeutic antibodies, sialylation can reverse the antibody inflammatory response, and galactosylation levels have been linked to aging, to the onset of inflammation, and to the predisposition to rheumatoid arthritis. Read More

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http://dx.doi.org/10.1093/glycob/cwy097DOI Listing
January 2019
18 Reads

Oligosaccharyltransferase structures provide novel insight into the mechanism of asparagine-linked glycosylation in prokaryotic and eukaryotic cells.

Glycobiology 2018 Oct 11. Epub 2018 Oct 11.

Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, 364 Plantation Street, Worcester, MA, USA.

Asparagine-linked (N-linked) glycosylation is one of the most common protein modification reactions in eukaryotic cells, occurring upon the majority of proteins that enter the secretory pathway. X-ray crystal structures of the single subunit OSTs from eubacterial and archaebacterial organisms revealed the location of donor and acceptor substrate binding sites and provided the basis for a catalytic mechanism. Cryoelectron microscopy structures of the octameric yeast OST provided substantial insight into the organization and assembly of the multisubunit oligosaccharyltransferases. Read More

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https://academic.oup.com/glycob/advance-article/doi/10.1093/
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http://dx.doi.org/10.1093/glycob/cwy093DOI Listing
October 2018
12 Reads

Society for Glycobiology Awards - 2018.

Authors:

Glycobiology 2018 12;28(12):906-909

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http://dx.doi.org/10.1093/glycob/cwy086DOI Listing
December 2018

Helicobacter pylori induces intracellular galectin-8 aggregation around damaged lysosomes within gastric epithelial cells in a host O-glycan-dependent manner.

Glycobiology 2019 02;29(2):151-162

Institute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan.

Galectin-8, a beta-galactoside-binding lectin, is upregulated in the gastric tissues of rhesus macaques infected with Helicobacter pylori. In this study, we found that H. pylori infection triggers intracellular galectin-8 aggregation in human-derived AGS gastric epithelial cells, and that these aggregates colocalize with lysosomes. Read More

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https://academic.oup.com/glycob/advance-article/doi/10.1093/
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http://dx.doi.org/10.1093/glycob/cwy095DOI Listing
February 2019
5 Reads

Glycoengineered antibodies: towards the next-generation of immunotherapeutics.

Glycobiology 2019 Mar;29(3):199-210

Biotech Development Programme, CMC Science & Intelligence, Merck Serono SpA, an affiliate of Merck KgaA, Darmstadt, Germany. Via Luigi Einaudi, 11. Guidonia Montecelio (Roma), Italy.

Monoclonal antibodies (mAbs) are currently the largest and fastest growing class of biopharmaceuticals, and they address unmet medical needs, e.g., in oncology and in auto-immune diseases. Read More

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https://academic.oup.com/glycob/advance-article/doi/10.1093/
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http://dx.doi.org/10.1093/glycob/cwy092DOI Listing
March 2019
6 Reads

Identification of key amino acid residues determining ligand binding specificity, homodimerization and cellular distribution of human galectin-10.

Glycobiology 2019 01;29(1):85-93

Jilin Province Key Laboratory for Chemistry and Biology of Natural Drugs in Changbai Mountain, The School of Life Sciences, Northeast Normal University, Changchun, China.

Charcot-Leyden crystal protein/Gal-10, abundantly expressed in eosinophils and basophils, is related to several immune diseases. Recently, crystallographic and biochemical studies showed that Gal-10 cannot bind lactose, because a glutamate residue (Glu33) from another monomer blocks the binding site. Moreover, Gal-10 actually forms a novel dimeric structure compared to other galectins. Read More

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http://dx.doi.org/10.1093/glycob/cwy087DOI Listing
January 2019
4 Reads

A pipeline to translate glycosaminoglycan sequences into 3D models. Application to the exploration of glycosaminoglycan conformational space.

Glycobiology 2019 01;29(1):36-44

University Lyon, University Claude Bernard Lyon 1, CNRS, INSA Lyon, CPE, Institute of Molecular and Supramolecular Chemistry and Biochemistry, UMR 5246, Villeurbanne Cedex, France.

Mammalian glycosaminoglycans are linear complex polysaccharides comprising heparan sulfate, heparin, dermatan sulfate, chondroitin sulfate, keratan sulfate and hyaluronic acid. They bind to numerous proteins and these interactions mediate their biological activities. GAG-protein interaction data reported in the literature are curated mostly in MatrixDB database (http://matrixdb. Read More

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http://dx.doi.org/10.1093/glycob/cwy084DOI Listing
January 2019
2 Reads

Galectin-3 binds selectively to the terminal, non-reducing end of β(1→4)-galactans, with overall affinity increasing with chain length.

Glycobiology 2019 01;29(1):74-84

Department of Biochemistry, Molecular Biology & Biophysics, 6-155 Jackson Hall, University of Minnesota, Minneapolis, MN, USA.

Galactans are linear polysaccharides of β(1→4)-linked galactose residues. Although they can antagonize galectin function, the nature of their binding to galectins needs to be better defined to develop them as drugs. Here, we investigated interactions between galectin-3 (Gal-3) and a series of galactans ranging in weight average molecular weight from 670 to 7550 Da. Read More

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https://academic.oup.com/glycob/advance-article/doi/10.1093/
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http://dx.doi.org/10.1093/glycob/cwy085DOI Listing
January 2019
5 Reads

Identity and role of the non-conserved acid/base catalytic residue in the GH29 fucosidase from the spider Nephilingis cruentata.

Glycobiology 2018 12;28(12):925-932

Laboratory of Biochemistry, Instituto Butantan, Sao Paulo, Brazil.

α-l-Fucosidases are widely occurring enzymes that remove fucose residues from N- and O-fucosylated glycoproteins. Comparison of amino acid sequences of fucosidases reveals that although the nucleophile is conserved among all α-l-fucosidases, the position of the acid/base residue is quite variable. Although several site-directed mutation studies have previously been performed on bacterial fucosidases, the only eukaryotic fucosidase so studied was the human fucosidase. Read More

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http://dx.doi.org/10.1093/glycob/cwy083DOI Listing
December 2018
3 Reads

Nature-inspired engineering of an F-type lectin for increased binding strength.

Glycobiology 2018 12;28(12):933-948

Institute of Microbial Technology, Sector 39-A, Chandigarh, India.

Individual lectin-carbohydrate interactions are usually of low affinity. However, high avidity is frequently attained by the multivalent presentation of glycans on biological surfaces coupled with the occurrence of high order lectin oligomers or tandem repeats of lectin domains in the polypeptide. F-type lectins are l-fucose binding lectins with a typical sequence motif, HX(26)RXDX(4)R/K, whose residues participate in l-fucose binding. Read More

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https://academic.oup.com/glycob/advance-article/doi/10.1093/
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http://dx.doi.org/10.1093/glycob/cwy082DOI Listing
December 2018
6 Reads

Sensitized genetic backgrounds reveal differential roles for EGF repeat xylosyltransferases in Drosophila Notch signaling.

Glycobiology 2018 11;28(11):849-859

Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX, USA.

In multicellular organisms, glycosylation regulates various developmental signaling pathways including the Notch pathway. One of the O-linked glycans added to epidermal growth factor-like (EGF) repeats in animal proteins including the Notch receptors is the xylose-xylose-glucose-O oligosaccharide. Drosophila glucoside xylosyltransferase (Gxylt) Shams negatively regulates Notch signaling in specific contexts. Read More

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http://dx.doi.org/10.1093/glycob/cwy080DOI Listing
November 2018
5 Reads

The effect of streptozotocin-induced hyperglycemia on N-and O-linked protein glycosylation in mouse ovary.

Glycobiology 2018 11;28(11):832-840

Department of Molecular Sciences, Macquarie University, North Ryde, Sydney, NSW, Australia.

Post-translational modification of proteins namely glycosylation influences cellular behavior, structural properties and interactions including during ovarian follicle development and atresia. However, little is known about protein glycosylation changes occurring in diabetes mellitus in ovarian tissues despite the well-known influence of diabetes on the outcome of successful embryo implantation. In our study, the use of PGC chromatography-ESI mass spectrometry in negative ion mode enabled the identification of 138 N-glycans and 6 O-glycans on the proteins of Streptozotocin-induced (STZ) diabetic mouse ovarian tissues (n = 3). Read More

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https://academic.oup.com/glycob/advance-article/doi/10.1093/
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http://dx.doi.org/10.1093/glycob/cwy075DOI Listing
November 2018
21 Reads

An F-type lectin domain directs the activity of Streptosporangium roseum alpha-l-fucosidase.

Glycobiology 2018 11;28(11):860-875

Institute of Microbial Technology, Sector 39-A, Chandigarh, India.

F-type lectins are phylogenetically widespread but selectively distributed fucose-binding lectins with L-fucose- and calcium-binding sequence motifs and an F-type lectin fold. Bacterial F-type lectin domains frequently occur in tandem with various protein domains in diverse architectures, indicating a possible role in directing enzyme activities or other biological functions to distinct fucosylated niches. Here, we report the biochemical characterization of a Streptosporangium roseum protein containing an F-type lectin domain in tandem with an NPCBM-associated domain and a family GH 29A alpha-l-fucosidase domain. Read More

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http://dx.doi.org/10.1093/glycob/cwy079DOI Listing
November 2018

Glycosylation profiling of dog serum reveals differences compared to human serum.

Glycobiology 2018 11;28(11):825-831

New England Biolabs Inc., 240 County Road, Ipswich, MA, USA.

Glycosylation is the most common post-translational modification of serum proteins, and changes in the type and abundance of glycans in human serum have been correlated with a growing number of human diseases. While the glycosylation pattern of human serum is well studied, little is known about the profiles of other mammalian species. Here, we report detailed glycosylation profiling of canine serum by hydrophilic interaction chromatography-ultraperformance liquid chromatography (HILIC-UPLC) and mass spectrometry. Read More

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http://dx.doi.org/10.1093/glycob/cwy070DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6192460PMC
November 2018

Acinetobacter baumannii K20 and K21 capsular polysaccharide structures establish roles for UDP-glucose dehydrogenase Ugd2, pyruvyl transferase Ptr2 and two glycosyltransferases.

Glycobiology 2018 11;28(11):876-884

School of Molecular Bioscience, The University of Sydney, Cnr of Maze Cres and Butlin Ave, Darlington Campus, Sydney, Australia.

Infections caused by Acinetobacter baumannii isolates from the major global clones, GC1 and GC2, are difficult to treat with antibiotics, and phage therapy, which requires extensive knowledge of the variation in the surface polysaccharides, is an option under consideration. The gene clusters directing the synthesis of capsular polysaccharide (CPS) in A. baumannii GC1 isolate A388 and GC2 isolate G21 differ by a single glycosyltransferase (gtr) gene. Read More

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https://academic.oup.com/glycob/advance-article/doi/10.1093/
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http://dx.doi.org/10.1093/glycob/cwy074DOI Listing
November 2018
20 Reads

Ligand binding and retention in snake gourd seed lectin (SGSL). A crystallographic, thermodynamic and molecular dynamics study.

Glycobiology 2018 12;28(12):968-977

Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India.

Snake gourd seed lectin (SGSL) is a non-toxic homolog of type II ribosome-inactivating proteins (RIPs) which contain a catalytic domain and a lectin domain. Isothermal titration calorimetry (ITC) measurements of the interactions of the protein with LacNAc, Lac, Gal, Me-α-Gal were carried out and the crystal structures of the native protein and its complex with Lac were determined. The crystal structure of the Me-α-Gal complex has already been determined. Read More

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http://dx.doi.org/10.1093/glycob/cwy072DOI Listing
December 2018

Cancer Immunotherapy.

Glycobiology 2018 09;28(9):638-639

Medical Oncology and Laboratory of Cancer Immunology, University Hospital Basel, Petersgraben 4, Basel, Switzerland.

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http://dx.doi.org/10.1093/glycob/cwy069DOI Listing
September 2018

Members of the GalNAc-T family of enzymes utilize distinct Golgi localization mechanisms.

Glycobiology 2018 11;28(11):841-848

Section on Biological Chemistry, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD, USA.

Mucin-type O-glycosylation is an evolutionarily conserved and essential post-translational protein modification that is initiated in the Golgi apparatus by a family of enzymes known as the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (GalNAc-Ts). GalNAc-Ts are type II membrane proteins which contain short N-terminal tails located in the cytoplasm, a transmembrane domain that crosses the Golgi membrane, to which is connected a stem region that tethers the C-terminal catalytic and lectin domains that reside in the Golgi lumen. Although mucin-type O-glycans have been shown to play critical roles in numerous biological processes, little is known about how the GalNAc-Ts are targeted to their site of action within the Golgi complex. Read More

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http://dx.doi.org/10.1093/glycob/cwy071DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6192461PMC
November 2018

Structural and conformational studies of the heparan sulfate mimetic PI-88.

Glycobiology 2018 10;28(10):731-740

Istituto Scientifico di Chimica e Biochimica "G. Ronzoni", Milan, Italy.

The heparan sulfate mimetic PI-88 is a complex mixture of sulfated oligosaccharides with anti-metastatic and anti-angiogenic activity due to its potent inhibition of heparanase and heparan sulfate-dependent angiogenic growth factors. It was recently in Phase III clinical trials for postresection hepatocellular carcinoma. The major oligosaccharide constituents of PI-88 were prepared for the first time by sulfonation of individually purified phosphorylated oligosaccharides isolated from the PI-88 precursor. Read More

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https://academic.oup.com/glycob/article/28/10/731/5059633
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http://dx.doi.org/10.1093/glycob/cwy068DOI Listing
October 2018
13 Reads

Prognostic role of the sialyltransferase ST6GAL1 in ovarian cancer.

Glycobiology 2018 11;28(11):898-903

Department of Gynecology, University Medical Center Hamburg-Eppendorf, Hamburg, Germany.

Aberrant sialylation of glycoproteins has been detected in many tumors, and upregulation of the beta-galactosamide alpha-2,6-sialyltransferase 1 (ST6GAL1) has been implicated with tumor aggressiveness and chemoresistance in experimental models. In our present study, we aimed to study the prognostic or predictive role of ST6GAL1 in ovarian carcinoma, using two independent ovarian cancer cohorts. ST6GAL1 mRNA levels were retrieved from a publicly available database (n = 517), and ST6GAL1 protein levels were analyzed by western blot analysis in a cohort of 204 ovarian tumor samples. Read More

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http://dx.doi.org/10.1093/glycob/cwy065DOI Listing
November 2018
1 Read

Plasma contact activation by a fucosylated chondroitin sulfate and its structure-activity relationship study.

Glycobiology 2018 10;28(10):754-764

State Key Laboratory of Phytochemistry and Plant Resources in West China, Kunming Institute of Botany, Chinese Academy of Sciences, Kunming, China.

Plasma contact system is the initial part of both the intrinsic coagulation pathway and kallikrein-kinin pathway, which mainly involves three proteins: coagulation factor XII (FXII), prekallikrein (PK) and high-molecular weight kininogen. Fucosylated chondroitin sulfate (FCS) is a unique sulfated glycosaminoglycan (GAG) composed of a chondroitin sulfate-like backbone and sulfated fucose branches. The native FCS was preliminary found to cause undesired activation of the plasma contact system. Read More

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http://dx.doi.org/10.1093/glycob/cwy067DOI Listing
October 2018
13 Reads

KIAA1199 expression and hyaluronan degradation colocalize in multiple sclerosis lesions.

Glycobiology 2018 12;28(12):958-967

Drug Discovery Department, Halozyme Therapeutics, Inc., San Diego, CA, USA.

Modification of hyaluronan (HA) accumulation has been shown to play a key role in regulating inflammatory processes linked to the progression of multiple sclerosis (MS). The aim of this study was to characterize the enzymatic activity involved in HA degradation observed within focal demyelinating lesions in the experimental autoimmune encephalomyelitis (EAE) animal model. EAE was induced in 3-month-old female C57BL/6J mice by immunization with myelin oligodendrocyte glycoprotein 33-35 (MOG33-35) peptide. Read More

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http://dx.doi.org/10.1093/glycob/cwy064DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6243203PMC
December 2018
1 Read

Biophysical analysis of sialic acid recognition by the complement regulator Factor H.

Glycobiology 2018 10;28(10):765-773

Interfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.

Complement factor H (FH), an elongated and substantially glycosylated 20-domain protein, is a soluble regulator of the complement alternative pathway (AP). It contains several glycan binding sites which mediate recognition of α2-3-linked sialic acid (FH domain 20) and glycosaminoglycans (domains 6-8 and 19-20). FH also binds the complement C3-activation product C3b, a powerful opsonin and focal point for the formation of C3-convertases of the AP feedback loop. Read More

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http://dx.doi.org/10.1093/glycob/cwy061DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6142864PMC
October 2018
16 Reads