scholarly journals Production of perdeuterated fucose from glyco-engineered bacteria

Glycobiology ◽  
2020 ◽  
Author(s):  
Lukas Gajdos ◽  
V Trevor Forsyth ◽  
Matthew P Blakeley ◽  
Michael Haertlein ◽  
Anne Imberty ◽  
...  
Keyword(s):  
Deuterium Oxide ◽  
Resonance Spectroscopy ◽  
Carbohydrate Binding ◽  
Biological Processes ◽  
Biophysical Studies ◽  
Protein Receptors ◽  
Final Yield ◽  
Algal Polysaccharides ◽  
Engineered Bacteria ◽  
Carbohydrate Binding Site

Abstract l-Fucose and l-fucose-containing polysaccharides, glycoproteins or glycolipids play an important role in a variety of biological processes. l-Fucose-containing glycoconjugates have been implicated in many diseases including cancer and rheumatoid arthritis. Interest in fucose and its derivatives is growing in cancer research, glyco-immunology, and the study of host–pathogen interactions. l-Fucose can be extracted from bacterial and algal polysaccharides or produced (bio)synthetically. While deuterated glucose and galactose are available, and are of high interest for metabolic studies and biophysical studies, deuterated fucose is not easily available. Here, we describe the production of perdeuterated l-fucose, using glyco-engineered Escherichia coli in a bioreactor with the use of a deuterium oxide-based growth medium and a deuterated carbon source. The final yield was 0.2 g L−1 of deuterated sugar, which was fully characterized by mass spectrometry and nuclear magnetic resonance spectroscopy. We anticipate that the perdeuterated fucose produced in this way will have numerous applications in structural biology where techniques such as NMR, solution neutron scattering and neutron crystallography are widely used. In the case of neutron macromolecular crystallography, the availability of perdeuterated fucose can be exploited in identifying the details of its interaction with protein receptors and notably the hydrogen bonding network around the carbohydrate binding site.

scholarly journals Are D-manno-configured Amadori products ligands of the bacterial lectin FimH?

2015 ◽  
Vol 11 ◽  
pp. 1096-1104 ◽  
Author(s):  
Tobias-Elias Gloe ◽  
Insa Stamer ◽  
Cornelia Hojnik ◽  
Tanja M Wrodnigg ◽  
Thisbe K Lindhorst
Keyword(s):  
Molecular Docking ◽  
Binding Site ◽  
Bacterial Adhesion ◽  
Carbohydrate Binding ◽  
Amadori Products ◽  
E Coli ◽  
Type D ◽  
Amadori Rearrangement ◽  
Carbohydrate Binding Site

The Amadori rearrangement was employed for the synthesis ofC-glycosyl-type D-mannoside analogues, namely 1-propargylamino- and 1-phenylamino-1-deoxy-α-D-manno-heptopyranose. They were investigated as ligands of type 1-fimbriatedE. colibacteria by means of molecular docking and bacterial adhesion studies. It turns out that Amadori rearrangement products have a limited activity as inhibitors of bacterial adhesion because the β-C-glycosidically linked aglycone considerably hampers complexation within the carbohydrate binding site of the type 1-fimbrial lectin FimH.

scholarly journals Lectins at Interfaces—An Atomic Force Microscopy and Multi-Parameter-Surface Plasmon Resonance Study

Materials ◽  
2018 ◽  
Vol 11 (12) ◽  
pp. 2348 ◽  
Author(s):  
Katrin Niegelhell ◽  
Thomas Ganner ◽  
Harald Plank ◽  
Evelyn Jantscher-Krenn ◽  
Stefan Spirk
Keyword(s):  
Atomic Force Microscopy ◽  
Surface Plasmon Resonance ◽  
Protein Adsorption ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Resonance Spectroscopy ◽  
Carbohydrate Binding ◽  
Force Microscopy ◽  
Atomic Force ◽  
Slow Kinetics

Lectins are a diverse class of carbohydrate binding proteins with pivotal roles in cell communication and signaling in many (patho)physiologic processes in the human body, making them promising targets in drug development, for instance, in cancer or infectious diseases. Other applications of lectins employ their ability to recognize specific glycan epitopes in biosensors and glycan microarrays. While a lot of research has focused on lectin interaction with specific carbohydrates, the interaction potential of lectins with different types of surfaces has not been addressed extensively. Here, we screen the interaction of two specific plant lectins, Concanavalin A and Ulex Europaeus Agglutinin-I with different nanoscopic thin films. As a control, the same experiments were performed with Bovine Serum Albumin, a widely used marker for non-specific protein adsorption. In order to test the preferred type of interaction during adsorption, hydrophobic, hydrophilic and charged polymer films were explored, such as polystyrene, cellulose, N,-N,-N-trimethylchitosan chloride and gold, and characterized in terms of wettability, surface free energy, zeta potential and morphology. Atomic force microscopy images of surfaces after protein adsorption correlated very well with the observed mass of adsorbed protein. Surface plasmon resonance spectroscopy studies revealed low adsorbed amounts and slow kinetics for all of the investigated proteins for hydrophilic surfaces, making those resistant to non-specific interactions. As a consequence, they may serve as favorable supports for biosensors, since the use of blocking agents is not necessary.

scholarly journals Structure of Dioclea virgata lectin: Relations between carbohydrate binding site and nitric oxide production

Biochimie ◽  
2012 ◽  
Vol 94 (3) ◽  
pp. 900-906 ◽  
Author(s):  
Raphael Batista da Nóbrega ◽  
Bruno A.M. Rocha ◽  
Carlos Alberto A. Gadelha ◽  
Tatiane Santi-Gadelha ◽  
Alana F. Pires ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Binding Site ◽  
Carbohydrate Binding ◽  
Nitric Oxide Production ◽  
Oxide Production ◽  
Carbohydrate Binding Site

scholarly journals Rhizobactin B is the preferred siderophore by a novel Pseudomonas isolate to obtain iron from dissolved organic matter in peatlands

BioMetals ◽  
2020 ◽  
Vol 33 (6) ◽  
pp. 415-433
Author(s):  
Stefan Kügler ◽  
Rebecca E. Cooper ◽  
Johanna Boessneck ◽  
Kirsten Küsel ◽  
Thomas Wichard
Keyword(s):  
Organic Matter ◽  
Dissolved Organic Matter ◽  
Ligand Exchange ◽  
High Resolution Mass Spectrometry ◽  
Iron Acquisition ◽  
Water Extract ◽  
Resonance Spectroscopy ◽  
Biological Processes ◽  
Polycarboxylic Acid ◽  
Chelating Compounds

AbstractBacteria often release diverse iron-chelating compounds called siderophores to scavenge iron from the environment for many essential biological processes. In peatlands, where the biogeochemical cycle of iron and dissolved organic matter (DOM) are coupled, bacterial iron acquisition can be challenging even at high total iron concentrations. We found that the bacterium Pseudomonas sp. FEN, isolated from an Fe-rich peatland in the Northern Bavarian Fichtelgebirge (Germany), released an unprecedented siderophore for its genus. High-resolution mass spectrometry (HR-MS) using metal isotope-coded profiling (MICP), MS/MS experiments, and nuclear magnetic resonance spectroscopy (NMR) identified the amino polycarboxylic acid rhizobactin and a novel derivative at even higher amounts, which was named rhizobactin B. Interestingly, pyoverdine-like siderophores, typical for this genus, were not detected. With peat water extract (PWE), studies revealed that rhizobactin B could acquire Fe complexed by DOM, potentially through a TonB-dependent transporter, implying a higher Fe binding constant of rhizobactin B than DOM. The further uptake of Fe-rhizobactin B by Pseudomonas sp. FEN suggested its role as a siderophore. Rhizobactin B can complex several other metals, including Al, Cu, Mo, and Zn. The study demonstrates that the utilization of rhizobactin B can increase the Fe availability for Pseudomonas sp. FEN through ligand exchange with Fe-DOM, which has implications for the biogeochemical cycling of Fe in this peatland.

scholarly journals Low or No Inhibitory Potency of the Canonical Galectin Carbohydrate-binding Site by Pectins and Galactomannans

2016 ◽  
Vol 291 (25) ◽  
pp. 13318-13334 ◽  
Author(s):  
John Stegmayr ◽  
Adriana Lepur ◽  
Barbro Kahl-Knutson ◽  
Matilde Aguilar-Moncayo ◽  
Anatole A. Klyosov ◽  
...  
Keyword(s):  
Binding Site ◽  
Carbohydrate Binding ◽  
Inhibitory Potency ◽  
Carbohydrate Binding Site

scholarly journals 1P059 Typical structure of carbohydrate binding site

2004 ◽  
Vol 44 (supplement) ◽  
pp. S44
Author(s):  
C. Shionyu-Mitsuyama ◽  
T. Shirai
Keyword(s):  
Binding Site ◽  
Carbohydrate Binding ◽  
Typical Structure ◽  
Carbohydrate Binding Site

The system ABXYM in nuclear magnetic resonance spectroscopy. Analysis of 3,4-dehydroprolinamide spectra by ABXYM and ABCDE methods

1969 ◽  
Vol 22 (4) ◽  
pp. 725 ◽  
Author(s):  
TJ Batterham ◽  
NV Riggs ◽  
AV Robertson ◽  
WRJ Simpson
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Deuterium Oxide ◽  
Resonance Spectroscopy ◽  
Coupling Constant ◽  
Spectroscopy Analysis ◽  
Satisfactory Explanation ◽  
Iterative Computation ◽  
Wide Range ◽  
Spectral Patterns

The wide range of deceptive simplicities observed in spectra of 3,4- dehydro-prolinamide in different solvents makes analysis extremely difficult. The power of an approach using ABXYM tables combined with iterative computation is demonstrated to obtain accurate parameters for spectra of saturated solutions in deutero-chloroform and deuterium oxide. A detailed study of the effects of small changes in parameters on the observed spectral patterns provides a satisfactory explanation for each case of deceptive simplicity and, in particular, gives reasons for the added simplicity of spectra measured at 100 Mc/s. A trans- homoallylic coupling constant (J2,5) of 5.8 c/s was observed and a synergistic four-bond coupling through the heteroatom is suggested to explain its magnitude. The stereochemistry of pyrrolines and similar heterocycles is discussed in the light of this large trans-coupling.

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