CSDB: Search results

References to other databases: GTC:G75274QJ, GlycomeDB:10895
Structural formula & atomic coordinates
Sweet-II 3D model
Show glycosyltransferases

Journal NLM ID: 2985121R
Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology

An anomeric phosphodiester linkage formed by a glycosyl phosphate unit and a hydroxyl group of another monosaccharide is found in many glycopolymers of the outer membrane in bacteria (e.g., capsular polysaccharides and lipopolysaccharides), yeasts and protozoa. The polymers (phosphoglycans) composed of glycosyl phosphate (or oligoglycosyl phosphate) repeating units could be chemically classified as poly(glycosyl phosphates). Their importance as immunologically active components of the cell wall and/or capsule of numerous microorganisms upholds the need to develop routes for the chemical preparation of these biopolymers. In this paper, we (1) present a review of the primary structures (known to date) of natural phosphoglycans from various sources, which contain glycosyl phosphate units, and (2) discuss different approaches and recent achievements in the synthesis of glycosyl phosphosaccharides and poly(glycosyl phosphates).

synthesis, structure, polysaccharides, Phosphoglycans, Anomeric phosphodiesters

NCBI PubMed ID: 17092493
Publication DOI: 10.1016/j.carres.2006.10.006
Journal NLM ID: 0043535
Publisher: Elsevier
Correspondence: a.v.nikolaev@dundee.ac.uk
Institutions: College of Life Sciences, Division of Biological Chemistry and Molecular Microbiology, University of Dundee, Dundee DD1 5EH, UK.

In the Yersinia pseudotuberculosis serotyping scheme, 21 serotypes are present originating from about 30 different O-factors distributed within the species. With regard to the chemical structures of lipopolysaccharides (LPSs) and the genetic basis of their biosynthesis, a number, but not all, of Y. pseudotuberculosis strains representing different serotypes have been investigated. In order to present an overall picture of the relationship between genetics and structures, we have been working on the genetics and structures of various Y. pseudotuberculosis O-specific polysaccharides (OPSs). Here, we present a structural and genetic analysis of the Y. pseudotuberculosis serotype O:11 OPS. Our results showed that this OPS structure has the same backbone as that of Y. pseudotuberculosis O:1b, but with a 6d-l-Altf side-branch instead of Parf. The 3' end of the gene cluster is the same as that for O:1b and has the genes for synthesis of the backbone and for processing the completed repeat unit. The 5' end has genes for synthesis of 6d-l-Altf and its transfer to the repeating unit backbone. The pathway for the synthesis of the 6d-l-Altf appears to be different from that for 6d-l-Altp in Y. enterocolitica O:3. The chemical structure of the O:11 repeating unit is

structure, O-specific polysaccharide, Yersinia pseudotuberculosis, O-specific polysaccharides, 6-Deoxy-L-altrofuranose, biosynthetic gene cluster

NCBI PubMed ID: 19505680
Journal NLM ID: 0043535
Publisher: Elsevier
Correspondence: oholst@fz-borstel.de (O. Holst)
Institutions: Division of Microbiology, School of Molecular and Microbial Biosciences, University of Sydney, Australia
Methods: 13C NMR, 1H NMR, NMR-2D, methylation, GC-MS, sugar analysis, NMR-1D, genetic methods

Lipid A of Francisella tularensis subsp. novicida contains a galactosamine (GalN) residue linked to its 1-phosphate group. As shown in the preceding paper, this GalN unit is transferred to lipid A from the precursor undecaprenyl phosphate-β-D-GalN. A small portion of the free lipid A of Francisella novicida is further modified with a glucose residue at position-6'. We now demonstrate that the two F. novicida homologues of Escherichia coli ArnC, designated FlmF1 and FlmF2, are essential for lipid A modification with glucose and GalN, respectively. Recombinant FlmF1 expressed in E. coli selectively condenses undecaprenyl phosphate and UDP-glucose in vitro to form undecaprenyl phosphate-glucose. Recombinant FlmF2 selectively catalyzes the condensation of undecaprenyl phosphate and UDP-N-acetylgalactosamine to generate undecaprenyl phosphate-N-acetylgalactosamine. On the basis of an analysis of the lipid A composition of flmF1 and flmF2 mutants of F. novicida, we conclude that FlmF1 generates the donor substrate for the modification of F. novicida free lipid A with glucose, whereas FlmF2 generates the immediate precursor of the GalN donor substrate, undecaprenyl phosphate-β-D-GalN. A novel deacetylase, present in membranes of F. novicida, removes the acetyl group from undecaprenyl phosphate-N-acetylgalactosamine to yield undecaprenyl phosphate-β-D-GalN. This deacetylase may have an analogous function to the deformylase that generates undecaprenyl phosphate-4-amino-4-deoxy-α-L-arabinose from undecaprenyl phosphate-4-deoxy-4-formylamino-α-L-arabinose in polymyxin-resistant strains of E. coli and Salmonella typhimurium.

Escherichia coli, lipid A, Salmonella typhimurium, Francisella tularensis, Francisella novicida, UDP-glucose, Electrospray Ionization, acetyltransferases

NCBI PubMed ID: 19166326
Publication DOI: 10.1021/bi802212t
Journal NLM ID: 0370623
Publisher: American Chemical Society
Correspondence: raetz@biochem.duke.edu
Institutions: Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710, USA
Methods: TLC, ESI-MS, genetic methods, biochemical methods, LC-ESI-MS

Proteus species are well-known opportunistic pathogens frequently associated with skin wound and urinary tract infections in humans and animals. O antigen diversity is important for bacteria to adapt to different hosts and environments, and has been used to identify serotypes of Proteus isolates. At present, 80 Proteus O-serotypes have been reported. Although the O antigen structures of most Proteus serotypes have been identified, the genetic features of these O antigens have not been well characterized. The O antigen gene clusters of Proteus species are located between the cpxA and secB genes. In this study, we identified 55 O antigen gene clusters of different Proteus serotypes. All clusters contain both the wzx and wzy genes and exhibit a high degree of heterogeneity. Potential functions of O antigen-related genes were proposed based on their similarity to genes in available databases. The O antigen gene clusters and structures were compared, and a number of glycosyltransferases were assigned to glycosidic linkages. In addition, an O serotype-specific suspension array was developed for detecting 31 Proteus serotypes frequently isolated from clinical specimens. To our knowledge, this is the first comprehensive report to describe the genetic features of Proteus O antigens and to develop a molecular technique to identify different Proteus serotypes.

O-antigen, gene cluster, Proteus, glycosyltransferases, serotyping, genomics, genetic diversity, serotype-specific

NCBI PubMed ID: 28817637
Publication DOI: 10.1371/journal.pone.0183267
Journal NLM ID: 101285081
Publisher: San Francisco, CA: Public Library of Science
Correspondence: Lei Wang
Institutions: N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, TEDA Institute of Biological Sciences and Biotechnology, Nankai University, Tianjin, P. R. China, Tianjin Research Center for Functional Genomics and Biochips, TEDA College, Nankai University, Tianjin, P. R. China, Tianjin Key Laboratory of Microbial Functional Genomics, TEDA College, Nankai University, Tianjin, P. R. China, Key Laboratory of Molecular Microbiology and Technology of the Ministry of Education, TEDA College, Nankai University, Tianjin, P. R. China, Department of Immunobiology of Bacteria, Department of General Microbiology Institute of Microbiology, Biotechnology and Immunology, Faculty of Biology and Environmental Protection, University of Lodz, Lodz, Poland
Methods: PCR, DNA sequencing, genetic methods, function analysis of gene clusters, serotyping