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Glycobiology

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https://www.readbyqxmd.com/read/28531294/tatsushi-toda-and-tamao-endo-win-107th-japan-academy-prize
#1
Motoi Kanagawa, Hiroshi Manya
No abstract text is available yet for this article.
May 22, 2017: Glycobiology
https://www.readbyqxmd.com/read/28510705/crystal-structure-of-octocoral-lectin-sll-2-complexed-with-forssman-antigen-tetrasaccharide
#2
Akiko Kita, Mitsuru Jimbo, Ryuichi Sakai, Yukio Morimoto, Ryota Takeuchi, Hiroshi Tanaka, Takashi Takahashi, Kunio Miki
A symbiosis-related lectin, SLL-2, from the octocoral Sinularia lochmodes, distributes densely on the cell surface of microalgae, Symbiodinium sp., an endosymbiotic dinoflagellate of the coral, and is also shown to be a chemical cue that transforms dinoflagellates into a non-motile (coccoid) symbiotic state. SLL-2 binds to the sugar chain of the molecule similar to Forssman antigen pentasaccharide (GalNAcα1-3GalNAcβ1-3 Galα1-4 Galβ1-4Glc) on the surface of microalgae with high affinity. Here we report the crystal structure of the complex between SLL-2 and Forssman antigen tetrasaccharide (GalNAcα1-3GalNAcβ1-3 Galα1-4 Galβ) at 3...
May 16, 2017: Glycobiology
https://www.readbyqxmd.com/read/28510654/asn-linked-oligosaccharide-chain-of-a-crenarchaeon-pyrobaculum-calidifontis-is-reminiscent-of-the-eukaryotic-high-mannose-type-glycan
#3
Daisuke Fujinami, Yuya Taguchi, Daisuke Kohda
Pyrobaculum calidifontis is a hyperthermophilic archaeon that belongs to the phylum Crenarchaeota. In contrast to the phylum Euryarchaeota, only the N-glycan structure of the genus Sulfolobus is known in Crenarchaeota. Here, we enriched glycoproteins from cultured P. calidifontis cells, by ConA lectin chromatography. The MASCOT search identified proteins with at least one potential N-glycosylation site. The MS/MS analysis of twelve small tryptic glycopeptides confirmed the canonical N-glycosylation consensus in P...
May 16, 2017: Glycobiology
https://www.readbyqxmd.com/read/28498962/an-iterative-glycosyltransferase-ents-catalyzes-transfer-and-extension-of-o-and-s-linked-monosaccharide-in-enterocin-96
#4
Rupa Nagar, Alka Rao
Glycosyltransferases are essential tools for in vitro-glycoengineering. Bacteria harbor an unexplored variety of protein glycosyltransferases. Here, we describe a peptide glycosyltransferase (EntS) encoded by ORF0417 of Enterococcus faecalis TX0104. EntS di-glycosylates linear peptide of enterocin 96- a known antibacterial, in vitro. It is capable of transferring as well as extending the glycan onto the peptide in an iterative sequential dissociative manner. It can catalyze multiple linkages: Glc/Gal(-O)Ser/Thr, Glc/Gal(-S)Cys and Glc/Gal(β)Glc/Gal(-O/S)Ser/Thr/Cys, in one pot...
May 12, 2017: Glycobiology
https://www.readbyqxmd.com/read/28486620/what-is-special-about-200-kda-hyaluronan-that-activates-hyaluronan-receptor-signaling
#5
Paul H Weigel, Bruce A Baggenstoss
The polydispersity of hyaluronan (HA) presents challenges for analyzing its solution properties, such as the relationship between mass and particle size. The broad mass range of natural HA (≤50-fold) makes molecular characterization difficult and ambiguous compared to molecules with known molecular weights (e.g., proteins). Biophysical studies show that large >MDa HA behaves like a random coil, whereas very small (e.g., 10 kDa) HA behaves like a rod. However, the mass range for this conformational transition is not easily determined in natural polydisperse HA...
May 9, 2017: Glycobiology
https://www.readbyqxmd.com/read/28486580/enterocyte-glycosylation-is-responsive-to-changes-in-extracellular-conditions-implications-for-membrane-functions
#6
Dayoung Park, Gege Xu, Mariana Barboza, Ishita M Shah, Maurice Wong, Helen Raybould, David A Mills, Carlito B Lebrilla
Epithelial cells in the lining of the intestines play critical roles in maintaining homeostasis while challenged by dynamic and sudden changes in luminal contents. Given the high density of glycosylation that encompasses their extracellular surface, environmental changes may lead to extensive reorganization of membrane-associated glycans. However, neither the molecular details nor the consequences of conditional glycan changes are well understood. Here we assessed the sensitivity of Caco-2 and HT-29 membrane N-glycosylation to variations in (i) dietary elements; (ii) microbial fermentation products; and (ii) cell culture parameters relevant to intestinal epithelial cell growth and survival...
May 9, 2017: Glycobiology
https://www.readbyqxmd.com/read/28460072/exploring-the-structure-of-fucosylated-chondroitin-sulfate-through-bottom-up-nuclear-magnetic-resonance-and-electrospray-ionization-high-resolution-mass-spectrometry-approaches
#7
Gustavo Rc Santos, Ana Co Porto, Paulo Ag Soares, Eduardo Vilanova, Paulo As Mourão
Fucosylated chondroitin sulfate (FCS) from sea cucumbers is composed of a chondroitin sulfate (CS) central core and branches of sulfated fucose. The structure of this complex glycosaminoglycan is usually investigated via nuclear magnetic resonance (NMR) analyses of the intact molecule, ergo through a top-down approach, which often yield spectra with intricate sets of signals. Here we employed a bottom-up approach to analyze the FCSs from the sea cucumbers Isostichopus badionotus and Ludwigothurea grisea from their basic constituents, viz...
April 28, 2017: Glycobiology
https://www.readbyqxmd.com/read/28460052/the-direct-and-indirect-effects-of-glycans-on-immune-function
#8
Linda G Baum, Brian A Cobb
The biological impact of glycans is as diverse and complex as the impact of proteins on biology. Familiar roles include those as a protein folding checkpoint in the endoplasmic reticulum and as a modulator of the serum half-life of secreted glycoproteins, but it has become clear over the last several decades that glycans are key signaling moieties, participate in cell-cell interactions and modulate the function of individual proteins, to name but a few examples. In the immune system, the majority of microbial "patterns" are glycans or glycoconjugates, while virtually all cell surface receptors are glycoproteins, and antibody glycosylation critically influences antibody function...
April 28, 2017: Glycobiology
https://www.readbyqxmd.com/read/28460017/structural-and-genetic-analyses-of-glycan-o-acetylation-in-a-bacterial-protein-glycosylation-system-evidence-for-differential-effects-on-glycan-chain-length
#9
Jan Haug Anonsen, Bente Børud, Åshild Vik, Raimonda Viburiene, Michael Koomey
O-acetylation is a common modification of bacterial glycoconjugates. By modifying oligosaccharide structure and chemistry, O-acetylation has important consequences for biotic and abiotic recognition events and thus bacterial fitness in general. Previous studies of the broad-spectrum O-linked protein glycosylation in pathogenic Neisseria species (including N. gonorrhoeae and N. meningitidis) have revealed O-acetylation of some of their diverse glycoforms and identified the committed acetylase, PglI. Herein, we extend these observations by using mass spectrometry to examine a complete set of all glycan variants identified to date...
April 28, 2017: Glycobiology
https://www.readbyqxmd.com/read/28430973/biological-functions-of-fucose-in-mammals
#10
Michael Schneider, Esam Al-Shareffi, Robert S Haltiwanger
Fucose is a 6-deoxy hexose in the L-configuration found in a large variety of different organisms. In mammals, fucose is incorporated into N-glycans, O-glycans and glycolipids by thirteen fucosyltransferases, all of which utilize the nucleotide charged form, GDP-fucose, to modify targets. Three of the fucosyltransferases, FUT8, FUT12/POFUT1, and FUT13/POFUT2, are essential for proper development in mice. Fucose modifications have also been implicated in many other biological functions including immunity and cancer...
April 18, 2017: Glycobiology
https://www.readbyqxmd.com/read/28419225/epitope-mapping-of-a-new-anti-tn-antibody-detecting-gastric-cancer-cells
#11
Nina Persson, Nicolai Stuhr-Hansen, Christian Risinger, Stefan Mereiter, António Polónia, Karol Polom, András Kovács, Franco Roviello, Celso Reis, Charlotte Welinder, Lena Danielsson, Bo Jansson, Ola Blixt
Here we introduce a novel scFv antibody, G2-D11, specific for two adjacent Tn-antigens (GalNAc -Ser/Thr) binding equally to three dimeric forms of the epitope, Ser-Thr, Thr-Thr and Thr-Ser. Compared to other anti-Tn reagents, the binding of G2-D11 is minimally influenced by the peptide structure, which indicates a high degree of carbohydrate epitope dominance and a low influence from the protein backbone. With a high affinity (KDapp = 1.3 × 10-8M) and no cross-reactivity to either sialyl-Tn epitope or blood group A antigens, scFv G2-D11 is an excellent candidate for a well-defined anti-Tn-antigen reagent...
April 13, 2017: Glycobiology
https://www.readbyqxmd.com/read/28402541/a-gene-cluster-at-an-unusual-chromosomal-location-responsible-for-the-novel-o-antigen-synthesis-in-escherichia-coli-o62-by-the-abc-transporter-dependent-pathway
#12
Xi Hou, Andrei V Perepelov, Xi Guo, Sof'ya N Senchenkova, Alexander S Shashkov, Bin Liu, Yuriy A Knirel, Lei Wang
The O-antigen is a part of the outer membrane of Gram-negative bacteria and is related to bacterial virulence. It is one of the most variable cell constituents, and its structural diversity is almost entirely due to genetic variation of the O-antigen gene cluster. In this study, the O-antigen structure of Escherichia coli O62 was elucidated by chemical analysis and nuclear magnetic resonance spectroscopy, but showing not consistent with the O-antigen gene cluster between conserved genes galF and gnd reported earlier...
April 10, 2017: Glycobiology
https://www.readbyqxmd.com/read/28369504/siglec-8-and-siglec-9-binding-specificities-and-endogenous-airway-ligand-distributions-and-properties
#13
Huifeng Yu, Anabel Gonzalez-Gil, Yadong Wei, Steve M Fernandes, Ryan N Porell, Katarina Vajn, James C Paulson, Corwin M Nycholat, Ronald L Schnaar
Siglecs are transmembrane sialoglycan binding proteins, most of which are expressed on leukocyte subsets and have inhibitory motifs that translate cell surface ligation into immune suppression. In humans, Siglec-8 on eosinophils, mast cells and basophils and Siglec-9 on neutrophils, monocytes and some T-cells, mediate immune cell death, inhibition of immune mediator release and/or enhancement of anti-inflammatory mediator release. Endogenous sialoglycan ligands in tissues, mostly uncharacterized, engage siglecs on leukocytes to inhibit inflammation...
March 20, 2017: Glycobiology
https://www.readbyqxmd.com/read/28369425/the-%C3%AE-reducing-end-in-%C3%AE-2-8-polysialic-acid-constitutes-a-unique-structural-motif
#14
Hugo F Azurmendi, Marcos D Battistel, Jasmin Zarb, Flora Lichaa, Alejandro Negrete Virgen, Joseph Shiloach, Darón I Freedberg
Over the years, structural characterizations of α(2-8)-polysialic acid (PolySia) in solution have produced inconclusive results. Efforts for obtaining detailed information in this important antigen have focused primarily on the α-linked residues and not on the distinctive characteristics of the terminal ones. The thermodynamically preferred anomeric configuration for the reducing end of sialic acids is β, which has the [I]CO2- group equatorial and the OH ([I]OH2) axial, while for all other residues the CO2- group is axial...
March 20, 2017: Glycobiology
https://www.readbyqxmd.com/read/28334971/expanding-glycosaminoglycan-chemical-space-towards-the-creation-of-sulfated-analogs-novel-polymers-and-chimeric-constructs
#15
Rachel S Lane, Kalib St Ange, Behnam Zolghadr, Xinyue Liu, Christina Schäffer, Robert J Linhardt, Paul L DeAngelis
Glycosaminoglycans (GAGs) have therapeutic potential in areas ranging from angiogenesis, inflammation, hemostasis and cancer. GAG bioactivity is conferred by intrinsic structural features, such as disaccharide composition, glycosidic linkages and sulfation pattern. Unfortunately, the in vitro enzymatic synthesis of defined GAGs is quite restricted by a limited understanding of current GAG synthases and modifying enzymes. Our work provides insights into GAG-active enzymes through the creation of sulfated oligosaccharides, a new polysaccharide and chimeric polymers...
March 17, 2017: Glycobiology
https://www.readbyqxmd.com/read/28334865/structure-of-human-pofut1-its-requirement-in-ligand-independent-oncogenic-notch-signaling-and-functional-effects-of-dowling-degos-mutations
#16
Brian J McMillan, Brandon Zimmerman, Emily D Egan, Michael Lofgren, Xiang Xu, Anthony Hesser, Stephen C Blacklow
Protein O-fucosyltransferase-1 (POFUT1), which transfers fucose residues to acceptor sites on serine and threonine residues of epidermal growth factor-like repeats of recipient proteins, is essential for Notch signal transduction in mammals. Here, we examine the consequences of POFUT1 loss on the oncogenic signaling associated with certain leukemia-associated mutations of human Notch1, report the structures of human POFUT1 in free and GDP-fucose bound states, and assess the effects of Dowling-Degos mutations on human POFUT1 function...
March 17, 2017: Glycobiology
https://www.readbyqxmd.com/read/28369326/gfsa-is-a-%C3%AE-1-5-galactofuranosyltransferase-involved-in-the-biosynthesis-of-the-galactofuran-side-chain-of-fungal-type-galactomannan-in-aspergillus-fumigatus
#17
Yukako Katafuchi, Qiushi Li, Yutaka Tanaka, Saki Shinozuka, Yohei Kawamitsu, Minoru Izumi, Keisuke Ekino, Keiji Mizuki, Kaoru Takegawa, Nobuyuki Shibata, Masatoshi Goto, Yoshiyuki Nomura, Kazuyoshi Ohta, Takuji Oka
Previously, we reported that GfsA is a novel galactofuranosyltransferase involved in the biosynthesis of O-glycan, the proper maintenance of fungal morphology, the formation of conidia and anti-fungal resistance in Aspergillus nidulans and A. fumigatus (Komachi Y et al., 2013. GfsA encodes a novel galactofuranosyltransferase involved in biosynthesis of galactofuranose antigen of O-glycan in Aspergillus nidulans and Aspergillus fumigatus. Mol. Microbiol. 90:1054-1073). In the present paper, to gain an in depth-understanding of the enzymatic functions of GfsA in A...
June 1, 2017: Glycobiology
https://www.readbyqxmd.com/read/28334934/a-pseudaminic-acid-or-a-legionaminic-acid-derivative-transferase-is-strain-specifically-implicated-in-the-general-protein-o-glycosylation-system-of-the-periodontal-pathogen-tannerella-forsythia
#18
Markus B Tomek, Bettina Janesch, Daniel Maresch, Markus Windwarder, Friedrich Altmann, Paul Messner, Christina Schäffer
The occurrence of nonulosonic acids in bacteria is wide-spread and linked to pathogenicity. However, the knowledge of cognate nonulosonic acid transferases is scarce. In the periodontopathogen Tannerella forsythia, several proposed virulence factors carry strain-specifically either a pseudaminic or a legionaminic acid derivative as terminal sugar on an otherwise structurally identical, protein-bound oligosaccharide. This study aims to shed light on the transfer of either nonulosonic acid derivative on a proximal N-acetylmannosaminuronic acid residue within the O-glycan structure, exemplified with the bacterium's abundant S-layer glycoproteins...
June 1, 2017: Glycobiology
https://www.readbyqxmd.com/read/28204532/characterization-of-the-single-subunit-oligosaccharyltransferase-stt3a-from-trypanosoma-brucei-using-synthetic-peptides-and-lipid-linked-oligosaccharide-analogs
#19
Ana S Ramírez, Jérémy Boilevin, Rasomoy Biswas, Bee Ha Gan, Daniel Janser, Markus Aebi, Tamis Darbre, Jean-Louis Reymond, Kaspar P Locher
The initial transfer of a complex glycan in protein N-glycosylation is catalyzed by oligosaccharyltransferase (OST), which is generally a multisubunit membrane protein complex in the endoplasmic reticulum but a single-subunit enzyme (ssOST) in some protists. To investigate the reaction mechanism of ssOST, we recombinantly expressed, purified and characterized the STT3A protein from Trypanosoma brucei (TbSTT3A). We analyzed the in vitro activity of TbSTT3A by synthesizing fluorescently labeled acceptor peptides as well as lipid-linked oligosaccharide (LLO) analogs containing a chitobiose moiety coupled to oligoprenyl carriers of distinct lengths (C10, C15, C20 and C25) and with different double bond stereochemistry...
June 1, 2017: Glycobiology
https://www.readbyqxmd.com/read/28138013/hyaluronan-synthase-assembles-hyaluronan-on-a-glcnac-%C3%AE-1-4-n-glcnac-%C3%AE-1%C3%A2-udp-primer-and-hyaluronan-retains-this-residual-chitin-oligomer-as-a-cap-at-the-nonreducing-end
#20
Paul H Weigel, Bruce A Baggenstoss, Jennifer L Washburn
Class I hyaluronan synthases (HAS) assemble [GlcNAc(β1,4)GlcUA(β1,3)]n-UDP at the reducing end and also make chitin. Streptococcus equisimilis HAS (SeHAS) also synthesizes chitin-UDP oligosaccharides, (GlcNAc-β1,4)n-GlcNAc(α1→)UDP (Weigel et al. 2015). Here we determined if HAS uses chitin-UDPs as primers to initiate HA synthesis, leaving the non-HA primer at the nonreducing (NR) end. HA made by SeHAS membranes was purified, digested with streptomyces lyase, and hydrophobic oligomers were enriched by solid phase extraction and analyzed by MALDI-TOF MS...
June 1, 2017: Glycobiology
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