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Anastasiya A Kasimova, Johanna J Kenyon, Nikolay P Arbatsky, Alexander S Shashkov, Anastasiya V Popova, Mikhail M Shneider, Yuriy A Knirel, Ruth M Hall
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 synthesis of capsular polysaccharide (CPS) in A. baumannii GC1 isolate A388 and GC2 isolate G21 differ by a single glycosyltransferase (gtr) gene. They include genes encoding a novel UDP-glucose dehydrogenase (Ugd2) and a putative pyruvyltransferase (Ptr2)...
August 9, 2018: Glycobiology
Thyageshwar Chandran, Nukathoti Sivaji, Avadhesha Surolia, Mamannamana Vijayan
Snake gourd seed lectin (SGSL) is a non-toxic homologue 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. While the crystal structure showed the presence of two-sugar binding sites, one on each of the two domains of the lectin chain, ITC measurements indicated the presence of only one binding site...
August 6, 2018: Glycobiology
Oliver M Pearce, Heinz Läubli
No abstract text is available yet for this article.
August 6, 2018: Glycobiology
Jessica L Becker, Duy T Tran, Lawrence A Tabak
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...
August 6, 2018: Glycobiology
(no author information available yet)
No abstract text is available yet for this article.
August 2, 2018: Glycobiology
Stefano Elli, Eduardo Stancanelli, Paul N Handley, Anthony Carroll, Elena Urso, Marco Guerrini, Vito Ferro
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 post-resection 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. PI-88 and its components were subjected to detailed 1D and 2D NMR spectroscopic analysis...
July 25, 2018: Glycobiology
Beatrice Wichert, Karin Milde-Langosch, Vladimir Galatenko, Barbara Schmalfeldt, Leticia Oliveira-Ferrer
Aberrant sialylation of glycoproteins has been detected in many tumours, and up-regulation of the beta-galactosamide alpha-2,6-sialyltransferase 1 (ST6GAL1) has been implicated with tumour 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 analysed by western blot analysis in a cohort of 204 ovarian tumour samples...
July 16, 2018: Glycobiology
Lisha Lin, Li Xu, Chuang Xiao, Lutan Zhou, Na Gao, Mingyi Wu, Jinhua Zhao
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, prekallikrein, and high molecular weight kininogen. Fucosylated chondroitin sulfate (FCS) is a unique sulfated glycosaminoglycan composed of a chondroitin sulfate-like backbone and sulfated fucose branches. The native FCS was preliminary found to cause undesired activation of plasma contact system. How the unusual glycosaminoglycan plays the roles in this process remains to be clarified...
July 16, 2018: Glycobiology
Mathieu Marella, Laurence Jadin, Gilbert A Keller, Barry J Sugarman, Gregory I Frost, H Michael Shepard
Objective: 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. Methods: EAE was induced in 3-month-old female C57BL/6J mice by immunization with myelin oligodendrocyte glycoprotein 33-35 (MOG33-35) peptide...
July 7, 2018: Glycobiology
Chinmayi R Kaundinya, Handanahal S Savithri, K Krishnamurthy Rao, Petety V Balaji
The gene epsN of Bacillus subtilis 168 was cloned and overexpressed in E. coli. Purified recombinant EpsN is shown to be a PLP-dependent aminotransferase by absorption spectroscopy, L-cycloserine inhibition and reverse phase HPLC studies. EpsN catalyses the conversion of UDP-2,6-dideoxy 2-acetamido 4-keto glucose to UDP-2,6-dideoxy 2-acetamido 4-amino glucose. Lys190 was found by sequence comparison and site-directed mutagenesis to form Schiff base with PLP. Mutagenesis studies showed that, in addition to Lys190, Ser185, Glu164, Gly58 and Thr59 are essential for aminotransferase activity...
July 6, 2018: Glycobiology
Christoph Q Schmidt, Agnes L Hipgrave Ederveen, Markus J Harder, Manfred Wuhrer, Thilo Stehle, Bärbel S Blaum
Complement factor H (FH), an elongated and substantially glycosylated twenty-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. In freely circulating FH the C3b binding site in domains 19-20 is occluded, a phenomenon that is not fully understood and could be mediated by an intramolecular interaction between FH's intrinsic sialylated glycosylation and its own sialic acid binding site...
July 4, 2018: Glycobiology
Xin-Xin Xu, Sheng-Tao Li, Ning Wang, Toshihiko Kitajima, Takehiko Yoko-O, Morihisa Fujita, Hideki Nakanishi, Xiao-Dong Gao
In eukaryotes, the biosynthesis of a highly conserved dolichol-linked oligosaccharide (DLO) precursor, Glc3Man9GlcNAc2-pyrophosphate-dolichol (-PP-Dol) begins on the cytoplasmic face of the endoplasmic reticulum (ER) and ends within the lumen. Two functionally distinguished heteromeric glycosyltransferase (GTase) complexes are responsible for the cytosolic DLO assembly. Alg1, a β-1, 4 mannosyltransferase (MTase) physically interacts with Alg2 and Alg11 proteins to form the multienzyme complex which catalyzes the addition of all five mannose to generate the Man5GlcNAc2-PP-Dol intermediate...
June 25, 2018: Glycobiology
Akitsugu Suga, Masamichi Nagae, Yoshiki Yamaguchi
Asparagine-linked glycans (N-glycans) are attached onto nascent glycoproteins in the endoplasmic reticulum (ER) and subsequently processed by a set of processing enzymes in the ER and Golgi apparatus. Accumulating evidence has shown that not all N-glycans on glycoproteins are uniformly processed into mature forms (hybrid- and complex-types in mammals) through the endoplasmic reticulum and Golgi apparatus, and a certain set of glycans remains unprocessed as an 'immature' form (high mannose-type in mammals). Much attention has been paid to environmental factors regulating N-glycoprotein maturation, such as the expression levels of glycosyltransferases/glycosidases...
June 21, 2018: Glycobiology
Anabel Gonzalez-Gil, Ryan N Porell, Steve M Fernandes, Yadong Wei, Huifeng Yu, Daniela J Carroll, Ryan McBride, James C Paulson, Michael Tiemeyer, Kazuhiro Aoki, Bruce S Bochner, Ronald L Schnaar
Human siglecs are a family of 14 sialic acid binding proteins, most expressed on subsets of immune cells where they regulate immune responses. Siglec-8 is expressed selectively on human allergic inflammatory cells - primarily eosinophils and mast cells - where engagement causes eosinophil apoptosis and inhibits mast cell mediator release. Evidence supports a model in which human eosinophils and mast cells bind to Siglec-8 sialoglycan ligands on inflammatory target tissues to resolve allergic inflammation and limit tissue damage...
June 19, 2018: Glycobiology
Laurino Carmen, Vadala Maria, Julio Cesar Morales-Medina, Annamaria Vallelunga, Beniamino Palmieri, Tommaso Iannitti
Duchenne Muscular dystrophy (DMD) is an inherited fatal X-linked myogenic disorder with a prevalence of 1 in 3500 male live births. It affects voluntary muscles, and heart and breathing muscles. DMD is characterised by continuous degeneration and regeneration cycles resulting in extensive fibrosis and a progressive reduction in muscle mass. Since the identification of a reduction in dystrophin protein as the cause of this disorder, numerous innovative and experimental therapies, focusing on increasing the levels of dystrophin, have been proposed, but the clinical improvement has been unsatisfactory...
June 19, 2018: Glycobiology
Victoria Ortega, Jacquelyn A Stone, Erik M Contreras, Ronald M Iorio, Hector C Aguilar
Glycosylation is a biologically important protein modification process by which a carbohydrate chain is enzymatically added to a protein at a specific amino acid residue. This process plays roles in many cellular functions, including intracellular trafficking, cell-cell signaling, protein folding, and receptor binding. While glycosylation is a common host cell process, it is utilized by many pathogens as well. Protein glycosylation is widely employed by viruses for both host invasion and evasion of host immune responses...
June 6, 2018: Glycobiology
Tarsis F Gesteira, Vivien J Coulson-Thomas
Heparan sulfate (HS) is a sulfated polysaccharide that plays a key role in morphogenesis, physiology and pathogenesis. The biosynthesis of HS takes place in the Golgi apparatus by a group of enzymes that polymerize, epimerize and sulfate the sugar chain. This biosynthetic process introduces varying degrees of sulfate substitution, which are tightly regulated and directly dictate binding specificity to different cytokines, morphogens and growth factors. Here we report the use of molecular dynamics simulations to investigate the dynamics of substrate recognition of two glycosaminoglycan (GAG) sulfotransferases, N-deacetylase-N-sulfotransferase and 2-O-sulfotransferase to the HS chain during the biosynthetic process...
June 6, 2018: Glycobiology
Xiaoqing Zhang, Huan Nie, Joshua Whited, Dan Wang, Yu Li, Xue-Long Sun
Sialic acids (SAs) are nine-carbon monosaccharides existing at the terminal location of glycan structures on the cell surface and secreted glycoconjugates. The expression levels and linkages of SAs on cells and tissues, collectively known as sialoform, present the hallmark of the cells and tissues of different systems and conditions. Accordingly, detecting or profiling cell surface sialoforms is very critical for understanding the function of cell surface glycans and glycoconjugates and even the molecular mechanisms of their underlying biological processes...
May 24, 2018: Glycobiology
Martin Dalziel, Stephen A Beers, Mark S Cragg, Max Crispin
Since the turn of the century, cancer therapy has undergone a transformation in terms of new treatment modalities and renewed optimism in achieving long-lived tumour control and even cure. This is, in large part, thanks to the widespread incorporation of monoclonal antibodies (mAbs) into standard treatment regimens. These new therapies have, across many settings, significantly contributed to improved clinical responses, patient quality of life and survival. Moreover, the flexibility of the antibody platform has led to the development of a wide range of innovative and combinatorial therapies that continue to augment the clinician's armoury...
May 24, 2018: Glycobiology
Jenny L Johnson, Mark B Jones, Brian A Cobb
Inhibition of peripheral inflammatory disease by carbohydrate antigens derived from normal gut microbiota has been demonstrated for the GI tract, brain, peritoneum, and most recently the airway. We have demonstrated that polysaccharide A (PSA) from the commensal organism Bacteroides fragilis activates CD4+ T cells upon presentation by the class II major histocompatibility complex, and that these PSA-experienced T cells prevent the development of lung inflammation in murine models. While the PSA-responding T cells themselves are not canonical FoxP3+ regulatory T cells (Tregs), their ability to prevent inflammation is dependent upon the suppressive cytokine IL-10...
December 1, 2018: Glycobiology
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