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1. (Article ID: 4540)
 
Jacobson JM, Kitov PI, Bundle DR
The synthesis of a multivalent heterobifunctional ligand for specific interaction with Shiga toxin 2 produced by E. coli O157:H7
Carbohydrate Research 378 (2013) 4-14
 

Hemolytic uremic syndrome is a potentially fatal complication of food poisoning caused by Escherichia coli O157:H7, especially those strains that produce the Stx2 Shiga toxin. Multivalent inhibitors based on the Pk trisaccharide are most effective against Stx1 the less dangerous of the two Shiga toxins. Inhibitors containing a terminal 2-acetamido-2-deoxy-α-D-galactopyranosyl residue in place of the terminal α-D-galactopyranosyl residue of Pk trisaccharide have been shown to exhibit preferential binding to Stx2. A multivalent heterobifunctional Pk analog containing 2-acetamido-2-deoxy-α-D-galactopyranose has been synthesized in a format that facilitates the ablation of toxin activity via supramolecular complex formation between Stx and the endogenous protein, Human serum amyloid P component (HuSAP).

Escherichia coli O157:H7, Glycomics, Shiga Toxin 2, Pk trisaccharide, Toxin inhibitors, Trisaccharide synthesis, Heterobifunctional ligand

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2. (Article ID: 4541)
 
Jana M, Misra AK
Straightforward synthesis of a tetrasaccharide repeating unit corresponding to the O-antigen of Escherichia coli O16
Beilstein Journal of Organic Chemistry 9 (2013) 1757-1762
 

A straightforward synthesis of the tetrasaccharide repeating unit of the O-antigen of Escherichia coli O16 has been achieved following a sequential glycosylation strategy. A minimum number of steps was used for the synthesis of the target compound involving a one-pot glycosylation and a protecting group manipulation. All intermediate reactions afford their products in high yield, and the glycosylation steps are stereoselective.

Lipopolysaccharide, tetrasaccharide, O-antigen, Escherichia coli, glycosylation

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3. (Article ID: 4542)
 
Jarrell KF, Jones GM, Kandiba L, Nair DB, Eichler J
S-layer glycoproteins and flagellins: reporters of archaeal posttranslational modifications
Archaea 2010 (2010) ID612948
 

Many archaeal proteins undergo posttranslational modifications. S-layer proteins and flagellins have been used successfully to study a variety of these modifications, including N-linked glycosylation, signal peptide removal and lipid modification. Use of these well-characterized reporter proteins in the genetically tractable model organisms, Haloferax volcanii, Methanococcus voltae and Methanococcus maripaludis, has allowed dissection of the pathways and characterization of many of the enzymes responsible for these modifications. Such studies have identified archaeal-specific variations in signal peptidase activity not found in the other domains of life, as well as the enzymes responsible for assembly and biosynthesis of novel N-linked glycans. In vitro assays for some of these enzymes have already been developed. N-linked glycosylation is not essential for either Hfx. volcanii or the Methanococcus species, an observation that allowed researchers to analyze the role played by glycosylation in the function of both S-layers and flagellins, by generating mutants possessing these reporters with only partial attached glycans or lacking glycan altogether. In future studies, it will be possible to consider questions related to the heterogeneity associated with given modifications, such as differential or modulated glycosylation.

biosynthesis, modification, glycosylation, Haloferax, Flagellin, reporter, Archaeal Proteins, Methanococcus, N-linked glycan, S-layer glycoproteins

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4. (Article ID: 7310)
 
Miyazaki T, Matsumoto Y, Matsuda K, Kurakata Y, Matsuo I, Ito Y, Nishikawa A, Tonozuka T
Heterologous expression and characterization of processing α-glucosidase I from Aspergillus brasiliensis ATCC 9642
Glycoconjugate Journal 28(8-9) (2011) 563–571
 

A gene for processing α-glucosidase I from a filamentous fungus, Aspergillus brasiliensis (formerly called Aspergillus niger) ATCC 9642 was cloned and fused to a glutathione S-transferase tag. The active construct with the highest production level was a truncation mutant deleting the first 16 residues of the hydrophobic N-terminal domain. This fusion enzyme hydrolyzed pyridylaminated (PA-) oligosaccharides Glc(3)Man(9)GlcNAc(2)-PA and Glc(3)Man(4)-PA and the products were identified as Glc(2)Man(9)GlcNAc(2)-PA and Glc(2)Man(4)-PA, respectively. Saturation curves were obtained for both Glc(3)Man(9)GlcNAc(2)-PA and Glc(3)Man(4)-PA, and the K (m) values for both substrates were estimated in the micromolar range. When 1 μM Glc(3)Man(4)-PA was used as a substrate, the inhibitors kojibiose and 1-deoxynojirimycin had similar effects on the enzyme; at 20 μM concentration, both inhibitors reduced activity by 50%.

N-Linked oligosaccharide, Aspergillus brasiliensis, Processing α-glucosidase I, Pyridylaminated oligosaccharide, Kojibiose

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