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1. (Article ID: 4891)
 
Larrouy-Maumus G, Clements A, Filloux A, McCarthy RR, Mostowy S
Direct detection of lipid A on intact Gram-negative bacteria by MALDI-TOF mass spectrometry
Journal of Microbiological Methods 120 (2016) 68-71
 

The purification and characterization of Gram-negative bacterial lipid A is tedious and time-consuming. Herein we report a rapid and sensitive method to identify lipid A directly on intact bacteria without any chemical treatment or purification, using an atypical solvent system to solubilize the matrix combined with MALDI-TOF mass spectrometry.

lipid A, mass spectrometry, Gram-negative bacteria, endotoxins

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2. (Article ID: 4892)
 
L'vov VL, Filatov AV, Perepelov AV, Shpirt AM, Shashkov AS, Chizhov AO, Knirel YA
Solvolysis with trifluoroacetic acid: an efficient method for selective cleavage of polysaccharides
Mendeleev Communications 26(4) (2016) 279-281
 

Solvolysis of polysaccharides with trifluoroacetic acid is efficient for selective cleavage of certain glycosidic linkages. This method was successfully used for structure elucidation of polysaccharides and obtaining oligosaccharides from polysaccharides for construction of glycoconjugate vaccines in cases of O-specific polysaccharides of bacteria Enterobacter cloacae and Shigella flexneri.

Shigella flexneri, glycoconjugate vaccines, polysaccharides, O-specific polysaccharides, solvolysis, Enterobacter cloacae

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3. (Article ID: 4893)
 
Soliman SE, Kovác P
Synthesis of a Conjugation-Ready, Phosphorylated, Tetrasaccharide Fragment of the O-PS of Vibrio cholerae O139
Journal of Organic Chemistry 80(22) (2016) 11227-11232
 

A new pathway to the tetrasaccharide α-Colp-(1→2)-4,6-P-β-d-Galp-(1→3)-[α-Colp-(1→4)]-β-d-GlcpNAc-1-(OCH2CH2)3NH2 has been developed. Glycosylation of 8-azido-3,6-dioxaoctyl 4,6-O-benzylidene-2-deoxy-2-trichloroacetamido-β-d-glucopyranoside with 3,4,6-tri-O-acetyl-2-O-bromoacetyl-α-d-galactopyranosyl bromide afforded the β-linked disaccharide. Debromoacetylation followed by reductive opening of the benzylidene acetal afforded the disaccharide diol acceptor. Halide-assisted glycosylation with 2,4-di-O-benzyl-α-colitosyl bromide gave the 1,2-cis-coupling product. Deacetylation followed by regioselective phosphorylation gave isomeric (R,S)-(P)-4(II),6(II)-cyclic phosphates, which were globally deprotected by one-step catalytic (Pd/C) hydrogenation/hydrogenolysis. The target tetrasaccharide, obtained in high overall yield, is amenable for conjugation to proteins.

synthesis, carbohydrates, tetrasaccharide, O-polysaccharide, Vibrio cholerae

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4. (Article ID: 7291)
 
Hopkins D, Gomathinayagam S, Rittenhour AM, Du M, Hoyt E, Karaveg K, Mitchell T, Nett JH, Sharkey NJ, Stadheim TA, Li H, Hamilton SR
Elimination of β-mannose glycan structures in Pichia pastoris
Glycobiology 12(21) (2011) 1616-1626
 

The methylotrophic yeast, Pichia pastoris, is an important organism used for the production of therapeutic proteins. However, the presence of fungal-like glycans, such as those containing β-mannose (Man) linkages, can elicit an immune response or bind to Man receptors, thus reducing their efficacy. Recent studies have confirmed that P. pastoris has four genes from the β-mannosyl transferase (BMT) family and that Bmt2p is responsible for the majority of β-Man linkages on glycans. While expressing recombinant human erythropoietin (rhEPO) in a developmental glycoengineered strain devoid of BMT2 gene expression, cross-reactivity was observed with an antibody raised against host cell antigens. Treatment of the rhEPO with protein N-glycosidase F eliminated cross-reactivity, indicating that the antigen was associated with the glycan. Thorough analysis of the glycan profile of rhEPO demonstrated the presence of low amounts of α-1,2-mannosidase resistant high-Man glycoforms. In an attempt to eliminate the α-mannosidase resistant glycoforms, we used a systemic approach to genetically knock-out the remaining members of the BMT family culminating in a quadruple bmt2,4,1,3 knock-out strain. Data presented here conclude that the additive elimination of Bmt2p, Bmt3p and Bmt1p activities are required for total abolition of β-Man-associated glycans and their related antigenicity. Taken together, the elimination of β-Man containing glycoforms represents an important step forward for the Pichia production platform as a suitable system for the production of therapeutic glycoproteins.

N-glycosylation, Pichia pastoris, β-linked mannose, β-mannosyl transferase, mannosidase

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