Publications
330 results found
Murugaesu N, Iravani M, Johnson D, et al., 2012, An in vivo functional screen to identify metastasis suppressor genes, CANCER RESEARCH, Vol: 72, ISSN: 0008-5472
Antonopoulos A, Demotte N, Stroobant V, et al., 2012, Loss of Effector Function of Human Cytolytic T Lymphocytes Is Accompanied by Major Alterations in <i>N</i>- and <i>O</i>-Glycosylation, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 287, Pages: 11240-11251
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- Citations: 32
Clark GF, Grassi P, Pang P, et al., 2012, Tumor Biomarker Glycoproteins in the Seminal Plasma of Healthy Human Males Are Endogenous Ligands for DC-SIGN, Molecular & Cellular Proteomics, Vol: 11
DC-SIGN is an immune C-type lectin that is expressed on both immature and mature dendritic cells associated with peripheral and lymphoid tissues in humans. It is a pattern recognition receptor that binds to several pathogens including HIV-1, Ebola virus, Mycobacterium tuberculosis, Candida albicans, Helicobacter pylori, and Schistosoma mansoni. Evidence is now mounting that DC-SIGN also recognizes endogenous glycoproteins, and that such interactions play a major role in maintaining immune homeostasis in humans and mice. Autoantigens (neoantigens) are produced for the first time in the human testes and other organs of the male urogenital tract under androgenic stimulus during puberty. Such antigens trigger autoimmune orchitis if the immune response is not tightly regulated within this system. Endogenous ligands for DC-SIGN could play a role in modulating such responses. Human seminal plasma glycoproteins express a high level of terminal Lewisx and Lewisy carbohydrate antigens. These epitopes react specifically with the lectin domains of DC-SIGN. However, because the expression of these sequences is necessary but not sufficient for interaction with DC-SIGN, this study was undertaken to determine if any seminal plasma glycoproteins are also endogenous ligands for DC-SIGN. Glycoproteins bearing terminal Lewisx and Lewisy sequences were initially isolated by lectin affinity chromatography. Protein sequencing established that three tumor biomarker glycoproteins (clusterin, galectin-3 binding glycoprotein, prostatic acid phosphatase) and protein C inhibitor were purified by using this affinity method. The binding of DC-SIGN to these seminal plasma glycoproteins was demonstrated in both Western blot and immunoprecipitation studies. These findings have confirmed that human seminal plasma contains endogenous glycoprotein ligands for DC-SIGN that could play a role in maintaining immune homeostasis both in the male urogenital tract and the vagina after coitus.
North SJ, von Gunten S, Antonopoulos A, et al., 2012, Glycomic analysis of human mast cells, eosinophils and basophils, GLYCOBIOLOGY, Vol: 22, Pages: 12-22, ISSN: 0959-6658
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- Citations: 25
Nacev BA, Grassi P, Dell A, et al., 2011, The Antifungal Drug Itraconazole Inhibits Vascular Endothelial Growth Factor Receptor 2 (VEGFR2) Glycosylation, Trafficking, and Signaling in Endothelial Cells, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 286, Pages: 44045-44056
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- Citations: 87
Sun W, Grassi P, Engstrom A, et al., 2011, N-glycans of Human Protein C Inhibitor: Tissue-Specific Expression and Function, PLOS ONE, Vol: 6, ISSN: 1932-6203
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- Citations: 22
Meyer BH, Zolghadr B, Peyfoon E, et al., 2011, Sulfoquinovose synthase - an important enzyme in the N-glycosylation pathway of Sulfolobus acidocaldarius, MOLECULAR MICROBIOLOGY, Vol: 82, Pages: 1150-1163, ISSN: 0950-382X
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- Citations: 61
Carney K, Chan W-Y, Sanapu-Reddy P, et al., 2011, Transcripts encoding ligands of the epidermal growth factor receptor are differentially expressed by CD4<SUP>+</SUP> T cell subsets, dependent on antigen experience, Annual Congress of the British-Society-for-Immunology, Publisher: WILEY-BLACKWELL, Pages: 60-60, ISSN: 0019-2805
Stansell E, Canis K, Huang I-C, et al., 2011, O-Glycosylation of the Envelope Glycoprotein of the Human Immunodeficiency Virus, Annual Conference of the Society-for-Glycobiology, Publisher: OXFORD UNIV PRESS INC, Pages: 1454-1454, ISSN: 0959-6658
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- Citations: 1
Hitchen P, Peyfoon E, Meyer B, et al., 2011, Structural Characterisation of <i>Sulfolobus</i> Glycoproteins by Mass Spectrometry, Annual Conference of the Society-for-Glycobiology, Publisher: OXFORD UNIV PRESS INC, Pages: 1461-1461, ISSN: 0959-6658
Ventura V, Sarah N, Hitchen P, et al., 2011, Structural Characterisation of Burkholderia pseudomallei 576 O-Antigen by Mass Spectrometry, Annual Conference of the Society-for-Glycobiology, Publisher: OXFORD UNIV PRESS INC, Pages: 1498-1498, ISSN: 0959-6658
Antonopoulos A, North SJ, Haslam SM, et al., 2011, Glycosylation of mouse and human immune cells: insights emerging from N-glycomics analyses, BIOCHEMICAL SOCIETY TRANSACTIONS, Vol: 39, Pages: 1334-1340, ISSN: 0300-5127
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- Citations: 35
Pang P, Chiu PCN, Lee C, et al., 2011, Human Sperm Binding Is Mediated by the Sialyl-Lewisx Oligosaccharide on the Zona Pellucida, Science, Vol: 333, Pages: 1761-1764
Human fertilization begins when spermatozoa bind to the extracellular matrix coating of the oocyte, known as the zona pellucida (ZP). One spermatozoan then penetrates this matrix and fuses with the egg cell, generating a zygote. Although carbohydrate sequences on the ZP have been implicated in sperm binding, the nature of the ligand was unknown. Here, ultrasensitive mass spectrometric analyses revealed that the sialyl-Lewisx sequence [NeuAcα2-3Galβ1-4(Fucα1-3)GlcNAc], a well-known selectin ligand, is the most abundant terminal sequence on the N- and O-glycans of human ZP. Sperm-ZP binding was largely inhibited by glycoconjugates terminated with sialyl-Lewisx sequences or by antibodies directed against this sequence. Thus, the sialyl-Lewisx sequence represents the major carbohydrate ligand for human sperm-egg binding.
Wang W, Hale C, Goulding D, et al., 2011, <i>Mannosidase</i> <i>2</i>, <i>alpha 1</i> Deficiency Is Associated with Ricin Resistance in Embryonic Stem (ES) Cells, PLOS ONE, Vol: 6, ISSN: 1932-6203
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- Citations: 52
Redelinghuys P, Antonopoulos A, Liu Y, et al., 2011, Early murine T-lymphocyte activation is accompanied by a switch from N-glycolyl- to N-acetyl-neuraminic acid and generation of ligands for siglec-E, J.Biol.Chem., Vol: 286, Pages: 34522-34532
It is well established that murine T-lymphocyte activation is accompanied by major changes in cell-surface sialylation, potentially influencing interactions with sialic acid-binding immunoglobulin-like lectins (siglecs). In the present study, we analysed early activation of murine CD4+ and CD8+ T-lymphocytes at 24 h. We observed a striking and selective up-regulation in the binding of a recombinant soluble form of siglec E, an inhibitory siglec which is expressed on several myeloid cell types including antigen presenting dendritic cells. In contrast, much lower levels of T cell binding were observed with other siglecs, including sialoadhesin, CD22, and siglec-F and the plant lectins Maackia amurensis leukoagglutinin and Sambucus nigra agglutinin. By mass spectrometry, the sialic acid content of 24-h-activated CD4+ and CD8+ T-lymphocytes exhibited an increased proportion of N-acetyl-neuraminic acid (NeuAc) to N glycolyl-neuraminic acid (NeuGc) in N-glycans. Reduced levels of NeuGc on the surface of activated T cells were demonstrated using an antibody specific for NeuGc and the expression levels of the gene encoding NeuAc to NeuGc converting enzyme, CMP-NeuAc hydroxylase, were also reduced. Siglec-E bound a wide range of sialylated structures in glycan arrays, had a preference for NeuAc versus NeuGc-terminated sequences and could recognise a set of sialoglycoproteins that included CD45, in lysates from activated T-lymphocytes. Collectively, these results show that early in T cell activation, glycan remodelling involves a switch from NeuGc- to NeuAc-terminating oligosaccharides on cell surface glycoproteins. This is associated with a strong up-regulation of siglec-E ligands which may be important in promoting cellular interactions between early-activated T-lymphocytes and myeloid cells expressing this inhibitory receptor
Nystroem K, Le Gall-Recule G, Grassi P, et al., 2011, Histo-Blood Group Antigens Act as Attachment Factors of Rabbit Hemorrhagic Disease Virus Infection in a Virus Strain-Dependent Manner, PLOS PATHOGENS, Vol: 7, ISSN: 1553-7366
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- Citations: 89
Silva J-P, Lelianova VG, Ermolyuk YS, et al., 2011, Latrophilin 1 and its endogenous ligand Lasso/teneurin-2 form a high-affinity transsynaptic receptor pair with signaling capabilities, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, Vol: 108, Pages: 12113-12118, ISSN: 0027-8424
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- Citations: 180
Graham SA, Antonopoulos A, Hitchen PG, et al., 2011, Identification of Neutrophil Granule Glycoproteins as Lewis<SUP>x</SUP>-containing Ligands Cleared by the Scavenger Receptor C-type Lectin, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 286, Pages: 24336-24349
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- Citations: 30
Hayee B, Antonopoulos A, Murphy EJ, et al., 2011, <i>G6PC3</i> mutations are associated with a major defect of glycosylation: a novel mechanism for neutrophil dysfunction, GLYCOBIOLOGY, Vol: 21, Pages: 914-924, ISSN: 0959-6658
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- Citations: 69
Barthel SR, Antonopoulos A, Cedeno-Laurent F, et al., 2011, Peracetylated 4-Fluoro-glucosamine Reduces the Content and Repertoire of <i>N</i>- and <i>O</i>-Glycans without Direct Incorporation, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 286, Pages: 21717-21731
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- Citations: 55
Blomme B, Van Steenkiste C, Grassi P, et al., 2011, Alterations of serum protein <i>N</i>-glycosylation in two mouse models of chronic liver disease are hepatocyte and not B cell driven, AMERICAN JOURNAL OF PHYSIOLOGY-GASTROINTESTINAL AND LIVER PHYSIOLOGY, Vol: 300, Pages: G833-G842, ISSN: 0193-1857
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- Citations: 23
von der Lieth C-W, Freire AA, Blank D, et al., 2011, EUROCarbDB: An open-access platform for glycoinformatics, GLYCOBIOLOGY, Vol: 21, Pages: 493-502, ISSN: 0959-6658
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- Citations: 85
Campomenosi P, Cinquetti R, Tallarita E, et al., 2011, Comparison of the baculovirus-insect cell and <i>Pichia pastoris</i> heterologous systems for the expression of the human tumor suppressor protein RNASET2, BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY, Vol: 58, Pages: 39-49, ISSN: 0885-4513
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- Citations: 10
Powlesland AS, Marcela Barrio M, Mordoh J, et al., 2011, Glycoproteomic characterization of carriers of the CD15/Lewis<SUP>x</SUP> epitope on Hodgkin's Reed-Sternberg cells, BMC BIOCHEMISTRY, Vol: 12, ISSN: 1471-2091
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- Citations: 12
Lee C, Chiu PCN, Pang P, et al., 2011, Glycosylation Failure Extends to Glycoproteins in Gestational Diabetes Mellitus: Evidence From Reduced α2-6 Sialylation and Impaired Immunomodulatory Activities of Pregnancy-Related Glycodelin-A, Diabetes, Vol: 60, Pages: 909-917
OBJECTIVE Gestational diabetes mellitus (GDM) is a common metabolic disorder of pregnancy. Patients with GDM are at risk for high fetal mortality and gestational complications associated with reduced immune tolerance and abnormal carbohydrate metabolism. Glycodelin-A (GdA) is an abundant decidual glycoprotein with glycosylation-dependent immunomodulatory activities. We hypothesized that aberrant carbohydrate metabolism in GDM was associated with changes in glycosylation of GdA, leading to defective immunomodulatory activities.RESEARCH DESIGN AND METHODS GdA in the amniotic fluid from women with normal (NGdA) and GDM (DGdA) pregnancies was purified by affinity chromatography. Structural analysis of protein glycosylation was preformed by lectin-binding assay and mass spectrometry. Cytotoxicity, cell death, cytokine secretion, and GdA binding of the GdA-treated lymphocytes and natural killer (NK) cells were determined. The sialidase activity in the placental tissue from normal and GDM patients was measured.RESULTS GDM affected the glycosylation but not the protein core of GdA. Specifically, DGdA had a lower abundance of α2-6–sialylated and high-mannose glycans and a higher abundance of glycans with Sda (NeuAcα2-3[GalNAcβ1-4]Gal) epitopes compared with NGdA. DGdA had reduced immuosuppressive activities in terms of cytotoxicity on lymphocytes, inhibitory activities on interleukin (IL)-2 secretion by lymphocytes, stimulatory activities on IL-6 secretion by NK cells, and binding to these cells. Desialylation abolished the immunomodulation and binding of NGdA. Placental sialidase activity was increased in GDM patients, which may account for the reduced sialic acid content of DGdA.CONCLUSIONS Taken together, this study provides the first direct evidence for altered enzymatic glycosylation and impaired bioactivity of GdA in GDM patients.
Ismail MN, Stone EL, Panico M, et al., 2011, High-sensitivity <i>O</i>-glycomic analysis of mice deficient in core 2 β1,6-<i>N</i>-acetylglucosaminyltransferases, GLYCOBIOLOGY, Vol: 21, Pages: 82-98, ISSN: 0959-6658
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- Citations: 38
Stansell E, Canis K, Haslam SM, et al., 2011, Simian Immunodeficiency Virus from the Sooty Mangabey and Rhesus Macaque Is Modified with O-Linked Carbohydrate, JOURNAL OF VIROLOGY, Vol: 85, Pages: 582-595, ISSN: 0022-538X
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- Citations: 20
Sun W, Parry S, Ubhayasekera W, et al., 2010, Further insight into the roles of the glycans attached to human blood protein C inhibitor, BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, Vol: 403, Pages: 198-202, ISSN: 0006-291X
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- Citations: 5
Ngugi SA, Ventura VV, Qazi O, et al., 2010, Lipopolysaccharide from <i>Burkholderia thailandensis</i> E264 provides protection in a murine model of melioidosis, VACCINE, Vol: 28, Pages: 7551-7555, ISSN: 0264-410X
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- Citations: 34
Magalhaes A, Gomes J, Ismail MN, et al., 2010, Fut2-Null Mice Display An Altered Gastric Mucosa Glycosylation Profile and Modified <i>Helicobacter pylori</i> Adhesion, Annual Conference of the Society-for-Glycobiology, Publisher: OXFORD UNIV PRESS INC, Pages: 1460-1461, ISSN: 0959-6658
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- Citations: 1
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