Mass-Analysis-Peptides-Number-Glycopeptides-Mass-Fragmentation-Oxonium-Ion-Tetrasaccharide-g
The glycan was purified, following extensive pronase digestion of flagellar filaments, by size-exclusion and anion-exchange chromatography. NMR spectroscopy revealed that the glycan had the Sug-4-beta-ManNAc3NAmA6Thr-4-beta-GlcNAc3NAcA-3-beta-GalNAc-Asn where Sug is a This oligosaccharide has significant similarity to the oligosaccharide that was found previously in Methanococcus voltae.Evidence for a LOS and a capsular polysaccharide in Capnocytophaga canimorsus.Renzi F(1), Ittig SJ(2), Sadovskaya I(3), Hess E(1), Lauber F(1), Dol M(1), Shin Capnocytophaga canimorsus is a dog's and cat's oral commensal which can cause fatal human infections upon bites or scratches. Seebio 2'-fucosyllactose start with flu-like symptoms but can rapidly evolve in fatal septicaemia with a mortality as high as %. Here we present the discovery of a polysaccharide capsule (CPS) at the surface of C.
canimorsus 5 (Cc5), a strain isolated from a fulminant septicaemia. We provide genetic and chemical data showing that this capsule is related to the lipooligosaccharide (LOS) and probably composed of the same polysaccharide units. A CPS was also found in nine out of nine other strains of C. canimorsus. In addition, the genomes of three of these strains, sequenced previously, contain genes similar to those encoding CPS biosynthesis in Cc5. Thus, the presence of a CPS is likely to be a common property of C. canimorsus.
The CPS and not the LOS confers protection against the bactericidal effect of human serum and phagocytosis by macrophages. An antiserum raised against the capsule increased the killing of C. canimorsus by human serum thus showing that anti-capsule antibodies have a protective role. Obtain today provide a new major element in the understanding of the pathogenesis of C. canimorsus.Abnormalities in the glycosylation of IgG and its clinical utility.It is approximately ten years since the first detailed analysis of the variation in oligosaccharide structures attached to human serum IgG was published [1].
This study also showed that the percentage incidence of agalactosyl structures on the bi-antennary oligosaccharide complex linked to the Fc region, was increased in patients with rheumatoid arthritis. 2'-Fucose lactose [2], published in abstract from only, had also suggested that this was the case but was never followed up. In this review the considerable amount of work that has explored the clinical relevance of abnormalities in the glycosylation of IgG is analysed Metabolic labelling of oligosaccharide chains of glycoproteins in a rat myoblast cell line and its lectin resistant mutants.We have determined the experimental conditions under which optimum hydrolysis of the various oligosaccharides of membrane glycopeptides can be achieved in a permanent line of rat skeletal myoblasts and its wheat germ agglutinin resistant mutants. The labelled glycopeptides were isolated by extensive pronase digestion of whole cells. Labelling studies demonstrated that label from fucose and galactose remained largely in these two sugars, while glucosamine labelled sialic acid and N-acetylglucosamine. Mannose label was found in both mannose and Effect of acceptor carbohydrates on oligosaccharide and polysaccharide synthesis by dextransucrase DsrM from Weissella cibaria.
Edmonton, Canada; Hubei University of Technology, College of Bioengineering and Edmonton, Canada; Hubei University of Technology, College of Bioengineering and The digestibility of isomalto-oligosaccharides (IMO) as well as their metabolism by gut microbiota depends on the degree of polymerization and the ratio of α-(1→4) to α-(1→6) linkages. Both parameters are influenced by the method of production. Commercial IMO are produced by transglycosylation of starch hydrolysates, or by transglycosylation with dextransucrase and sucrose as glucosyl-donor and maltose as glucosyl-acceptor. This study aimed to quantitatively and qualitatively assess the acceptor reaction with dextransucrase. α-Glucans were selected by systematic variation of degree of polymerization and linkage type; the dextransucrase DsrM from Weissella cibaria M was used as biocatalyst. The efficiency of α-glucans as acceptor carbohydrates decreased in the order DP2DP3DP1; among disaccharides, the efficiency decreased in the order α-(1→6)α-(1→4)α-(1→3); the α-(1→2) linked kojibiose did not support oligosaccharide formation. Equimolar addition of efficient acceptor molecules and sucrose shifted the dextransucrase reaction to oligosaccharides as virtually exclusive product.
DsrM readily extended a commercial IMO preparation by adding α-(1→6)-linked glucose moieties.
