The plant secretory pathway for the trafficking of cell wall polysaccharides and glycoproteins
Plant endomembranes are required for the biosynthesis and secretion of complex cell wall matrix polysaccharides, glycoproteins and proteoglycans. To define the biochemical roadmap that guides the synthesis and deposition of these cell wall components it is first necessary to outline the localization of the biosynthetic and modifying enzymes involved, as well as the distribution of the intermediate and final constituents of the cell wall. Thus far, a comprehensive understanding of cell wall matrix components has been hampered by the multiplicity of trafficking routes in the secretory pathway, and the diverse biosynthetic ro...
Source: Glycobiology - September 30, 2016 Category: Biology Authors: Kim, S.-J., Brandizzi, F. Tags: Review Source Type: research
Plant protein glycosylation
Protein glycosylation is an essential co- and post-translational modification of secretory and membrane proteins in all eukaryotes. The initial steps of N-glycosylation and N-glycan processing are highly conserved between plants, mammals and yeast. In contrast, late N-glycan maturation steps in the Golgi differ significantly in plants giving rise to complex N-glycans with β1,2-linked xylose, core α1,3-linked fucose and Lewis A-type structures. While the essential role of N-glycan modifications on distinct mammalian glycoproteins is already well documented, we have only begun to decipher the biological function o...
Source: Glycobiology - September 30, 2016 Category: Biology Authors: Strasser, R. Tags: Review Source Type: research
The inside and outside: topological issues in plant cell wall biosynthesis and the roles of nucleotide sugar transporters
The cell wall is a complex extracellular matrix composed primarily of polysaccharides. Noncellulosic polysaccharides, glycoproteins and proteoglycans are synthesized in the Golgi apparatus by glycosyltransferases (GTs), which use nucleotide sugars as donors to glycosylate nascent glycan and glycoprotein acceptors that are subsequently exported to the extracellular space. Many nucleotide sugars are synthesized in the cytosol, leading to a topological issue because the active sites of most GTs are located in the Golgi lumen. Nucleotide sugar transporters (NSTs) overcome this problem by translocating nucleoside diphosphate su...
Source: Glycobiology - September 30, 2016 Category: Biology Authors: Temple, H., Saez-Aguayo, S., Reyes, F. C., Orellana, A. Tags: Review Source Type: research
Plant glycobiology: a current snap shot!
(Source: Glycobiology)
Source: Glycobiology - September 30, 2016 Category: Biology Authors: Doblin, M. S., Mohnen, D., Bacic, A. Tags: INTRODUCTION TO SPECIAL ISSUE Source Type: research
The minimum information required for a glycomics experiment (MIRAGE) project: sample preparation guidelines for reliable reporting of glycomics datasets
The minimum information required for a glycomics experiment (MIRAGE) project was established in 2011 to provide guidelines to aid in data reporting from all types of experiments in glycomics research including mass spectrometry (MS), liquid chromatography, glycan arrays, data handling and sample preparation. MIRAGE is a concerted effort of the wider glycomics community that considers the adaptation of reporting guidelines as an important step towards critical evaluation and dissemination of datasets as well as broadening of experimental techniques worldwide. The MIRAGE Commission published reporting guidelines for MS ...
Source: Glycobiology - September 30, 2016 Category: Biology Authors: Struwe, W. B., Agravat, S., Aoki-Kinoshita, K. F., Campbell, M. P., Costello, C. E., Dell, A., Ten Feizi, , Haslam, S. M., Karlsson, N. G., Khoo, K.-H., Kolarich, D., Liu, Y., McBride, R., Novotny, M. V., Packer, N. H., Paulson, J. C., Rapp, E., Ranzinge Tags: Technical Note Source Type: research
Meeting and Course Announcements
(Source: Glycobiology)
Source: Glycobiology - September 30, 2016 Category: Biology Tags: Glyco-Forum Source Type: research
Subscription Page
(Source: Glycobiology)
Source: Glycobiology - September 30, 2016 Category: Biology Tags: Original articles Source Type: research
Editorial Board
(Source: Glycobiology)
Source: Glycobiology - September 30, 2016 Category: Biology Tags: Original articles Source Type: research
Contents Page
(Source: Glycobiology)
Source: Glycobiology - September 30, 2016 Category: Biology Tags: Original articles Source Type: research
Intra- and intermolecular interactions of human galectin-3: assessment by full-assignment-based NMR
Galectin-3 is an adhesion/growth-regulatory protein with a modular design comprising an N-terminal tail (NT, residues 1–111) and the conserved carbohydrate recognition domain (CRD, residues 112–250). The chimera-type galectin interacts with both glycan and peptide motifs. Complete 13C/15N-assignment of the human protein makes NMR-based analysis of its structure beyond the CRD possible. Using two synthetic NT polypeptides covering residues 1–50 and 51–107, evidence for transient secondary structure was found with helical conformation from residues 5 to 15 as well as proline-mediated, multi-turn struc...
Source: Glycobiology - September 8, 2016 Category: Biology Authors: Ippel, H., Miller, M. C., Vertesy, S., Zheng, Y., Canada, F. J., Suylen, D., Umemoto, K., Romano, C., Hackeng, T., Tai, G., Leffler, H., Kopitz, J., Andre, S., Kübler, D., Jimenez-Barbero, J., Oscarson, S., Gabius, H.-J., Mayo, K. H. Tags: Original Article Source Type: research
Characterization of an fungal L-fucokinase involved in Mortierella alpina GDP-L-fucose salvage pathway
GDP-l-fucose functions as a biological donor for fucosyltransferases, which are required for the catalysis of l-fucose to various acceptor molecules including oligosaccharides, glycoproteins and glycolipids. Mortierella alpina is one of the highest lipid-producing fungi and can biosynthesis GDP-l-fucose in the de novo pathway. Analysis of the M. alpina genome suggests that there is a gene encoding l-fucokinase (FUK) for the conversion of fucose to l-fucose-1-phosphate in the GDP-l-fucose salvage pathway, which has never been found in fungi before. This gene was characterized to explore its role in GDP-l-fucose synthesis. T...
Source: Glycobiology - September 8, 2016 Category: Biology Authors: Wang, H., Zhang, C., Chen, H., Yang, Q., Zhou, X., Gu, Z., Zhang, H., Chen, W., Chen, Y. Q. Tags: Original Article Source Type: research
The fucosidase-pool of Emticicia oligotrophica: Biochemical characterization and transfucosylation potential
Three novel bacterial α-l-fucosidases, which cleave terminal fucosyl residues from glycoconjugates are reported in this work. Originating from the recently discovered bacterium Emticicia oligotrophica, recombinant fucosidase isoforms designated as Eo0918, Eo3066 and Eo3812 were shown to have the highest activity between pH 6.0 and 7.0 and temperature optima between 30 and 45°C. All enzymes catalyzed the hydrolysis of the model substrate pNP-α-l-fucose and revealed significantly different regiospecificities towards fucose-containing oligosaccharides: Eo0918 liberated exclusively α1,6-linked fucose and ...
Source: Glycobiology - September 8, 2016 Category: Biology Authors: Liu, S., Kulinich, A., Cai, Z. P., Ma, H. Y., Du, Y. M., Lv, Y. M., Liu, L., Voglmeir, J. Tags: Original Article Source Type: research
Conservation of anatomically restricted glycosaminoglycan structures in divergent nematode species
Heparan sulfates (HS) are glycosaminoglycans of the extracellular matrices and characterized by complex modification patterns owing to sulfations, epimerization, and acetylation. Distinct HS modification patterns have been shown to modulate protein–protein interactions during development in general and of the nervous system in particular. This has led to the heparan sulfate code hypothesis, which posits that specifically modified HS epitopes are distributed in a tissue and cell-specific fashion to orchestrate neural circuit formation. Whether an HS code exists in vivo, how specific or how evolutionarily conserved the...
Source: Glycobiology - September 8, 2016 Category: Biology Authors: Attreed, M., Saied-Santiago, K., Bülow, H. E. Tags: Original Article Source Type: research
Computational analysis of interactions in structurally available protein-glycosaminoglycan complexes
Glycosaminoglycans represent a class of linear anionic periodic polysaccharides, which play a key role in a variety of biological processes in the extracellular matrix via interactions with their protein targets. Computationally, glycosaminoglycans are very challenging due to their high flexibility, periodicity and electrostatics-driven nature of the interactions with their protein counterparts. In this work, we carry out a detailed computational characterization of the interactions in protein–glycosaminoglycan complexes from the Protein Data Bank (PDB), which are split into two subsets accounting for their intrinsic...
Source: Glycobiology - September 8, 2016 Category: Biology Authors: Samsonov, S. A., Pisabarro, M. T. Tags: Computational Biology Source Type: research
The NEU1-selective sialidase inhibitor, C9-butyl-amide-DANA, blocks sialidase activity and NEU1-mediated bioactivities in human lung in vitro and murine lung in vivo
Neuraminidase-1 (NEU1) is the predominant sialidase expressed in human airway epithelia and lung microvascular endothelia where it mediates multiple biological processes. We tested whether the NEU1-selective sialidase inhibitor, C9-butyl-amide-2-deoxy-2,3-dehydro-N-acetylneuraminic acid (C9-BA-DANA), inhibits one or more established NEU1-mediated bioactivities in human lung cells. We established the IC50 values of C9-BA-DANA for total sialidase activity in human airway epithelia, lung microvascular endothelia and lung fibroblasts to be 3.74 µM, 13.0 µM and 4.82 µM, respectively. In human airway epithelia,...
Source: Glycobiology - September 8, 2016 Category: Biology Authors: Hyun, S. W., Liu, A., Liu, Z., Cross, A. S., Verceles, A. C., Magesh, S., Kommagalla, Y., Kona, C., Ando, H., Luzina, I. G., Atamas, S. P., Piepenbrink, K. H., Sundberg, E. J., Guang, W., Ishida, H., Lillehoj, E. P., Goldblum, S. E. Tags: Cell Biology Source Type: research
