Publications
302 results found
Damerell D, Ceroni A, Maass K, et al., 2015, Annotation of glycomics MS and MS/MS spectra using the GlycoWorkbench software tool., Methods Mol Biol, Vol: 1273, Pages: 3-15
The GlycoWorkbench software tool allows users to semiautomatically annotate glycomics MS and MS/MS spectra and MS glycoproteomics spectra. The GlycanBuilder software tool is embedded within GlycoWorkbench allowing users to draw glycan structures and export images of the drawn structures. This chapter demonstrates to users how to draw glycan structures within GlycoWorkbench using the GlycanBuilder software tool. This chapter also demonstrates how to use GlycoWorkbench to import MS and MS/MS glycomics spectra and use the cascading annotation feature to annotate both the MS and MS/MS spectra with a single command.
Chen Q, Müller JS, Pang P-C, et al., 2015, Global N-linked Glycosylation is Not Significantly Impaired in Myoblasts in Congenital Myasthenic Syndromes Caused by Defective Glutamine-Fructose-6-Phosphate Transaminase 1 (GFPT1), Biomolecules, Vol: 5, Pages: 2758-2781, ISSN: 2218-273X
Glutamine-fructose-6-phosphate transaminase 1 (GFPT1) is the first enzyme of the hexosamine biosynthetic pathway. It transfers an amino group from glutamine to fructose-6-phosphate to yield glucosamine-6-phosphate, thus providing the precursor for uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) synthesis. UDP-GlcNAc is an essential substrate for all mammalian glycosylation biosynthetic pathways and N-glycan branching is especially sensitive to alterations in the concentration of this sugar nucleotide. It has been reported that GFPT1 mutations lead to a distinct sub-class of congenital myasthenic syndromes (CMS) termed “limb-girdle CMS with tubular aggregates”. CMS are hereditary neuromuscular transmission disorders in which neuromuscular junctions are impaired. To investigate whether alterations in protein glycosylation at the neuromuscular junction might be involved in this impairment, we have employed mass spectrometric strategies to study the N-glycomes of myoblasts and myotubes derived from two healthy controls, three GFPT1 patients, and four patients with other muscular diseases, namely CMS caused by mutations in DOK7, myopathy caused by mutations in MTND5, limb girdle muscular dystrophy type 2A (LGMD2A), and Pompe disease. A comparison of the relative abundances of bi-, tri-, and tetra-antennary N-glycans in each of the cell preparations revealed that all samples exhibited broadly similar levels of branching. Moreover, although some differences were observed in the relative abundances of some of the N-glycan constituents, these variations were modest and were not confined to the GFPT1 samples. Therefore, GFPT1 mutations in CMS patients do not appear to compromise global N-glycosylation in muscle cells.
Macauley MS, Arlian BM, Rillahan CD, et al., 2014, Systemic blockade of sialylation in mice with a global inhibitor of sialyltransferases, Journal of Biological Chemistry, Vol: 289, Pages: 35149-35158, ISSN: 0021-9258
Sialic acid terminates glycans of glycoproteins and glycolipids that play numerous biological roles in health and disease. While genetic tools are available for interrogating the effects of decreased or abolished sialoside expression in mice, pharmacological inhibition of the sialyltransferase family has to date not been possible. We have recently shown that a sialic acid analog, 3F-NeuAc, added to the media of cultured cells shuts down sialylation by a mechanism involving its intracellular conversion to CMP-3F-NeuAc, a competitive inhibitor of all sialyltransferases. Here we show that administering 3F-NeuAc to mice dramatically decreases sialylated glycans in cells of all tissues tested, including: blood, spleen, liver, brain, lung, heart, kidney, and testes. A single dose results in greatly decreased sialoside expression for over 7 weeks in some tissues. While blockade of sialylation with 3F-NeuAc does not affect viability of cultured cells, its use in vivo has a deleterious 'on-target' effect on liver and kidney function. After administration of 3F-NeuAc, liver enzymes in the blood are dramatically altered, and mice develop proteinuria concomitant with dramatic loss of sialic acid in the glomeruli within 4 days, leading to irreversible kidney dysfunction and failure to thrive. These results confirm a critical role for sialosides in liver and kidney function and document the feasibility of pharmacological inhibition of sialyltransferases for in vivo modulation of sialoside expression.
Aoki-Kinoshita K, Agravat S, Aoki NP, et al., 2014, Development of an International Glycan Structure Repository, Joint Meeting of the Society-for-Glycobiology (SFG) and the Japanese-Society-of-Carbohydrate-Research (JSCR), Publisher: OXFORD UNIV PRESS INC, Pages: 1106-1106, ISSN: 0959-6658
Macauley M, Arlian B, Rillahan C, et al., 2014, <i>In vivo</i> blockade of sialylation with a global sialyltransferase inhibitor causes irreversible kidney dysfunction, Joint Meeting of the Society-for-Glycobiology (SFG) and the Japanese-Society-of-Carbohydrate-Research (JSCR), Publisher: OXFORD UNIV PRESS INC, Pages: 1089-1089, ISSN: 0959-6658
Jia N, Barclay WS, Roberts K, et al., 2014, Glycomic characterization of respiratory tract tissues of ferrets IMPLICATIONS FOR ITS USE IN INFLUENZA VIRUS INFECTION STUDIES, Journal of Biological Chemistry, Vol: 289, Pages: 28489-28504, ISSN: 0021-9258
The initial recognition between influenza virus and the host cell is mediated by interactions between the viral surface protein hemagglutinin and sialic acid-terminated glycoconjugates on the host cell surface. The sialic acid residues can be linked to the adjacent monosaccharide by α2–3- or α2–6-type glycosidic bonds. It is this linkage difference that primarily defines the species barrier of the influenza virus infection with α2–3 binding being associated with avian influenza viruses and α2–6 binding being associated with human strains. The ferret has been extensively used as an animal model to study the transmission of influenza. To better understand the validity of this model system, we undertook glycomic characterization of respiratory tissues of ferret, which allows a comparison of potential viral receptors to be made between humans and ferrets. To complement the structural analysis, lectin staining experiments were performed to characterize the regional distributions of glycans along the respiratory tract of ferrets. Finally, the binding between the glycans identified and the hemagglutinins of different strains of influenza viruses was assessed by glycan array experiments. Our data indicated that the respiratory tissues of ferret heterogeneously express both α2–3- and α2–6-linked sialic acids. However, the respiratory tissues of ferret also expressed the Sda epitope (NeuAcα2-3(GalNAcβ1–4)Galβ1–4GlcNAc) and sialylated N,N′-diacetyllactosamine (NeuAcα2–6GalNAcβ1–4GlcNAc), which have not been observed in the human respiratory tract surface epithelium. The presence of the Sda epitope reduces potential binding sites for avian viruses and thus may have implications for the usefulness of the ferret in the study of influenza virus infection.
Sassi A, Fliegauf M, Yang L, et al., 2014, Hypomorphic Homozygous Mutations in Phosphoglucomutase3 Impair Immunity and Increase Serum IGE Levels, 16th Biennial Meeting of the European-Society-for-Immunodeficiencies, Publisher: SPRINGER/PLENUM PUBLISHERS, Pages: S161-S162, ISSN: 0271-9142
Boztug K, Jaervinen PM, Salzer E, et al., 2014, Human JAGN1 Deficiency Causes Disturbed Myeloid Cell Homeostasis and Severe Congenital Neutropenia, 16th Biennial Meeting of the European-Society-for-Immunodeficiencies, Publisher: SPRINGER/PLENUM PUBLISHERS, Pages: S151-S152, ISSN: 0271-9142
Boztug K, Jaervinen PM, Salzer E, et al., 2014, JAGN1 deficiency causes aberrant myeloid cell homeostasis and congenital neutropenia, NATURE GENETICS, Vol: 46, Pages: 1021-+, ISSN: 1061-4036
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- Citations: 88
Wohlschlager T, Butschi A, Grassi P, et al., 2014, Methylated glycans as conserved targets of animal and fungal innate defense, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, Vol: 111, Pages: E2787-E2796, ISSN: 0027-8424
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- Citations: 61
Zhang H, Zhu F, Yang T, et al., 2014, The highly conserved domain of unknown function 1792 has a distinct glycosyltransferase fold, NATURE COMMUNICATIONS, Vol: 5, ISSN: 2041-1723
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- Citations: 52
York WS, Agravat S, Aoki-Kinoshita KF, et al., 2014, MIRAGE: The minimum information required for a glycomics experiment, GLYCOBIOLOGY, Vol: 24, Pages: 402-406, ISSN: 0959-6658
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- Citations: 84
Sassi A, Lazaroski S, Wu G, et al., 2014, Hypomorphic homozygous mutations in phosphoglucomutase 3 (<i>PGM3</i>) impair immunity and increase serum IgE levels, JOURNAL OF ALLERGY AND CLINICAL IMMUNOLOGY, Vol: 133, Pages: 1410-U681, ISSN: 0091-6749
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- Citations: 132
Peng W, Nycholat CM, Mcbride R, et al., 2014, Synthesis of biologically active <i>N</i>- and <i>O</i>-linked glycans with multi-sialylated poly-<i>N</i>-acetyllactosamine extensions using P. damsela a2-6 sialyltransferase, 247th National Spring Meeting of the American-Chemical-Society (ACS), Publisher: AMER CHEMICAL SOC, ISSN: 0065-7727
Jedrzejewski PM, Jimenez del Val I, Constantinou A, et al., 2014, Towards controlling the glycoform: a model framework linking extracellular metabolites to antibody glycosylation, International Journal of Molecular Sciences, Vol: 15, Pages: 4492-4522, ISSN: 1422-0067
Glycoproteins represent the largest group of the growing number of biologically-derived medicines. The associated glycan structures and their distribution are known to have a large impact on pharmacokinetics. A modelling framework was developed to provide a link from the extracellular environment and its effect on intracellular metabolites to the distribution of glycans on the constant region of an antibody product. The main focus of this work is the mechanistic in silico reconstruction of the nucleotide sugar donor (NSD) metabolic network by means of 34 species mass balances and the saturation kinetics rates of the 60 metabolic reactions involved. NSDs are the co-substrates of the glycosylation process in the Golgi apparatus and their simulated dynamic intracellular concentration profiles were linked to an existing model describing the distribution of N-linked glycan structures of the antibody constant region. The modelling framework also describes the growth dynamics of the cell population by means of modified Monod kinetics. Simulation results match well to experimental data from a murine hybridoma cell line. The result is a modelling platform which is able to describe the product glycoform based on extracellular conditions. It represents a first step towards the in silico prediction of the glycoform of a biotherapeutic and provides a platform for the optimisation of bioprocess conditions with respect to product quality.
Murugaesu N, Iravani M, Van Weverwijk A, et al., 2014, An In Vivo Functional Screen Identifies ST6GalNAc2 Sialyltransferase as a Breast Cancer Metastasis Suppressor, CANCER DISCOVERY, Vol: 4, Pages: 304-317, ISSN: 2159-8274
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- Citations: 70
Halder S, Cotmore S, Heimburg-Molinaro J, et al., 2014, Profiling of Glycan Receptors for Minute Virus of Mice in Permissive Cell Lines Towards Understanding the Mechanism of Cell Recognition, PLOS One, Vol: 9, ISSN: 1932-6203
The recognition of sialic acids by two strains of minute virus of mice (MVM), MVMp (prototype) and MVMi (immunosuppressive), is an essential requirement for successful infection. To understand the potential for recognition of different modifications of sialic acid by MVM, three types of capsids, virus-like particles, wild type empty (no DNA) capsids, and DNA packaged virions, were screened on a sialylated glycan microarray (SGM). Both viruses demonstrated a preference for binding to 9-O-methylated sialic acid derivatives, while MVMp showed additional binding to 9-O-acetylated and 9-O-lactoylated sialic acid derivatives, indicating recognition differences. The glycans recognized contained a type-2 Galβ1-4GlcNAc motif (Neu5Acα2-3Galβ1-4GlcNAc or 3′SIA-LN) and were biantennary complex-type N-glycans with the exception of one. To correlate the recognition of the 3′SIA-LN glycan motif as well as the biantennary structures to their natural expression in cell lines permissive for MVMp, MVMi, or both strains, the N- and O-glycans, and polar glycolipids present in three cell lines used for in vitro studies, A9 fibroblasts, EL4 T lymphocytes, and the SV40 transformed NB324K cells, were analyzed by MALDI-TOF/TOF mass spectrometry. The cells showed an abundance of the sialylated glycan motifs recognized by the viruses in the SGM and previous glycan microarrays supporting their role in cellular recognition by MVM. Significantly, the NB324K showed fucosylation at the non-reducing end of their biantennary glycans, suggesting that recognition of these cells is possibly mediated by the Lewis X motif as in 3′SIA-LeX identified in a previous glycan microarray screen.
Campbell MP, Ranzinger R, Luetteke T, et al., 2014, Toolboxes for a standardised and systematic study of glycans, BMC BIOINFORMATICS, Vol: 15, ISSN: 1471-2105
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- Citations: 44
Sahadevan S, Antonopoulos A, Haslam SM, et al., 2014, Unique, Polyfucosylated Glycan-Receptor Interactions Are Essential for Regeneration of <i>Hydra magnipapillata</i>, ACS CHEMICAL BIOLOGY, Vol: 9, Pages: 147-155, ISSN: 1554-8929
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- Citations: 10
Nycholat CM, Peng W, McBride R, et al., 2013, Synthesis of Biologically Active <i>N</i>- and <i>O</i>-Linked Glycans with Multisialylated Poly-<i>N</i>-acetyllactosamine Extensions Using <i>P</i>. <i>damsela</i> α2-6 Sialyltransferase, JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, Vol: 135, Pages: 18280-18283, ISSN: 0002-7863
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- Citations: 44
Roberts B, Antonopoulos A, Haslam SM, et al., 2013, Novel expression of <i>Haemonchus contortus</i> vaccine candidate aminopeptidase H11 using the free-living nematode <i>Caenorhabditis elegans</i>, VETERINARY RESEARCH, Vol: 44, ISSN: 0928-4249
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- Citations: 37
Sassi A, Lazaroski S, Wu G, et al., 2013, Hypomorphic, Homozygous Mutations In Phosphoglucomutase-3 Impair Immunity And Increase Serum IgE Levels, UK-Primary-Immunodeficiency-Network (UK PIN) Meeting, Publisher: WILEY-BLACKWELL, Pages: 2-2, ISSN: 0009-9104
Boztug K, Jaervinen PM, Salzer E, et al., 2013, Deficiency Of JAGN 1 Causes Severe Congenital Neutropeni a Associated With Defective Secretory Pathway and Aberrant Myeloid Cell Homeostasis, 55th Annual Meeting of the American-Society-of-Hematology, Publisher: AMER SOC HEMATOLOGY, ISSN: 0006-4971
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- Citations: 1
Chan RWY, Karamanska R, Van Poucke S, et al., 2013, Infection of swine <i>ex vivo</i> tissues with avian viruses including H7N9 and correlation with glycomic analysis, INFLUENZA AND OTHER RESPIRATORY VIRUSES, Vol: 7, Pages: 1269-1282, ISSN: 1750-2640
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- Citations: 26
Lo C, Antonopoulos A, Dell A, et al., 2013, Surface coupling of P-selectin glycoprotein ligand-1 onto mesenchymal stem cells enables leukocyte-like cell tethering and rolling, Annual Conference of the Society-for-Glycobiology, Publisher: OXFORD UNIV PRESS INC, Pages: 1411-1411, ISSN: 0959-6658
Haslam S, Panico M, Morris H, et al., 2013, Glycomics and glycoproteomics-providing new biological insights, Annual Conference of the Society-for-Glycobiology, Publisher: OXFORD UNIV PRESS INC, Pages: 1330-1330, ISSN: 0959-6658
Nita-Lazar M, Ravindran C, Giomarelli B, et al., 2013, Zebrafish galectins bind to the infectious hematopoietic necrosis virus (IHNV) glycoprotein and modulate adhesion to the host cell surface, Annual Conference of the Society-for-Glycobiology, Publisher: OXFORD UNIV PRESS INC, Pages: 1343-1343, ISSN: 0959-6658
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- Citations: 1
Choo MSF, Castangia R, Openshaw ME, et al., 2013, Identification and Characterisation of Lewis Antigens on Ovarian Cancer N-glycans using MALDI-QIT-TOF, Annual Conference of the Society-for-Glycobiology, Publisher: OXFORD UNIV PRESS INC, Pages: 1360-1360, ISSN: 0959-6658
Lo CY, Antonopoulos A, Dell A, et al., 2013, The use of surface immobilization of P-selectin glycoprotein ligand-1 on mesenchymal stem cells to facilitate selectin mediated cell tethering and rolling, BIOMATERIALS, Vol: 34, Pages: 8213-8222, ISSN: 0142-9612
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- Citations: 34
Nicholls JM, Moss RB, Haslam SM, 2013, The use of sialidase therapy for respiratory viral infections, ANTIVIRAL RESEARCH, Vol: 98, Pages: 401-409, ISSN: 0166-3542
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- Citations: 28
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