CSDB: Search results

References to other databases: GTC:G41320EP, GlycomeDB:4544
Structural formula & atomic coordinates
Sweet-II 3D model
Show glycosyltransferases

No abstract available

NCBI PubMed ID: 6155983
Publication DOI: 10.1139/o80-016
Journal NLM ID: 0421034
Institutions: Division of Biological Sciences, National Research Council of Canada, Ottawa, Ontario, Canada KIA OR6, The Channing Laboratory, Harvard Medical School, and the Department of Medicine, Peter Bent Brigham Hospital, Boston, Massachusetts 021 I5
Methods: 13C NMR, methylation, GLC-MS, partial acid hydrolysis, sugar analysis, GLC, immunodiffusion assays, optical rotation measurement

Rabbits immunized with group B type III, group C, and Streptococcus pneumoniae type XIV streptococcal vaccines developed autoantibodies reactive with autologous and isologous erythrocytes and human O-positive erythrocytes at reduced temperatures. The cold agglutinin antibodies were present in both the immunoglobulin M (IgM) and IgG fractions of group C streptococcal antiserum and in the IgM fraction of group B type III and S. pneumoniae type XIV antisera. BALB/c, CF1, and local strains of mice immunized with group B type III and S. pneumoniae type XIV streptococcal vaccines also produced a cold agglutinin antibody reactive with rabbit and human erythrocytes. The cold agglutinin antibodies were reactive with saccharide compounds representative of the determinants present on the individual bacterial carbohydrate structures, individual vaccine preparations, and isolated polysaccharides. The group C antibodies in rabbits were reactive with sugar ligands in the following order: N-acetylgalactosamine greater than melibiose greater than lactose greater than galactose greater than glucose. Group B type III and S. pneumoniae type XIV cold agglutinin antibodies in rabbit antisera, however, displayed reactivities different from group C antibodies and from each other. Group B type III antibodies reacted with galactose greater than lactose greater than N-acetylgalactosamine greater than glucose greater than rhamnose; S. pneumoniae type XIV antibodies reacted with lactose greater than melibiose greater than galactose greater than glucose greater than N-acetylgalactosamine. The same relative ligand specificity was observed for the cold agglutinin antibodies in S. pneumoniae type XIV mouse antisera. The cold agglutinin antibodies in group B type III and S. pneumoniae type XIV antiserum reacted with erythrocytes at higher temperatures (up to 31 degrees C) than did group C antibodies (up to 14 degrees C). In addition, S. pneumoniae type XIV antibodies did not discriminate between I- or i-bearing human erythrocytes to a significant extent. The results obtained provide substantial evidence that autoreactive cold agglutinin antibodies produced by immunization with these vaccines represent subpopulations of bacterial carbohydrate-specific antibodies that cross-react with mammalian carbohydrate structures.

NCBI PubMed ID: 6345390
Journal NLM ID: 0246127
Publisher: American Society for Microbiology

Structural patterns of bacterial capsular antigens including capsular polysaccharides and exoglycans are given in this review. In addition, the immunological activity of capsular antigens and their role in type specificity of bacteria are discussed.

structure, capsular polysaccharides, bacterial capsular antigens, bacterial exoglycans, immunological activity, type specificity

NCBI PubMed ID: 17009947
Publication DOI: 10.1134/S000629790609001X
Journal NLM ID: 0376536
Publisher: Nauka/Interperiodica
Correspondence: ovoys@physiol.komisc.ru
Institutions: Institute of Physiology, Komi Science Center, Urals Branch of the Russian Academy of Sciences, Syktyvkar 167982, Russia

The capsular polysaccharide (CPS) represents a key virulence factor for most encapsulated streptococci. Streptococcus suis and Group B Streptococcus (GBS) are both well-encapsulated pathogens of clinical importance in veterinary and/or human medicine and responsible for invasive systemic diseases. S. suis and GBS are the only Gram-positive bacteria which express a sialylated CPS at their surface. An important difference between these two sialylated CPSs is the linkage between the side-chain terminal galactose and sialic acid, being α-2,6 for S. suis but α-2,3 for GBS. It is still unclear how sialic acid may affect CPS production and, consequently, the pathogenesis of the disease caused by these two bacterial pathogens. Here, we investigated the role of sialic acid and the putative effect of sialic acid linkage modification in CPS synthesis using inter-species allelic exchange mutagenesis. To this aim, a new molecular biogenetic approach to express CPS with modified sialic acid linkage was developed. We showed that sialic acid (and its α-2,6 linkage) is crucial for S. suis CPS synthesis, whereas for GBS, CPS synthesis may occur in presence of an α-2,6 sialyltransferase or in absence of sialic acid moiety. To evaluate the effect of the CPS composition/structure on sialyltransferase activity, two distinct capsular serotypes within each bacterial species were compared (S. suis serotypes 2 and 14 and GBS serotypes III and V). It was demonstrated that the observed differences in sialyltransferase activity and specificity between S. suis and GBS were serotype unrestricted. This is the first time that a study investigates the interspecies exchange of capsular sialyltransferase genes in Gram-positive bacteria. The obtained mutants represent novel tools that could be used to further investigate the immunomodulatory properties of sialylated CPSs. Finally, in spite of common CPS structural characteristics and similarities in the cps loci, sialic acid exerts differential control of CPS expression by S. suis and GBS.

phenotype, capsular polysaccharide, group B Streptococcus, infectious disease, specificity, sialyltransferase, Streptococcus suis, 3 sialic acid, 6 sialic acid, alpha-2

NCBI PubMed ID: 29666608
Publication DOI: 10.3389/fmicb.2018.00545
Journal NLM ID: 101548977
Publisher: Lausanne: Frontiers Research Foundation
Correspondence: mariela.segura@umontreal.ca
Institutions: Faculty of Veterinary Medicine, Swine and Poultry Infectious Disease Research Centre, University of Montreal, Saint-Hyacinthe, QC, Canada, Division of Bacterial and Parasitic Diseases, National Institute of Animal Health, National Agriculture and Food Research Organization, Tsukuba, Japan, The United Graduate School of Veterinary Sciences, Gifu University, Gifu, Japan, Saint-Hyacinthe Research and Development Centre, Agriculture and Agri-Food Canada, Saint-Hyacinthe, QC, Canada
Methods: gel filtration, 13C NMR, 1H NMR, NMR-2D, DNA techniques, genetic methods, SEC-MALS, RT-PCR, statistical analysis, transmission electron microscopy, hydrophobicity test

Glycosylation is a ubiquitous process that is universally conserved in nature. The various products of glycosylation, such as polysaccharides, glycoproteins, and glycolipids, perform a myriad of intra- and extracellular functions. The multitude of roles performed by these molecules is reflected in the significant diversity of glycan structures and linkages found in eukaryotes and prokaryotes. Importantly, glycosylation is highly relevant for the virulence of many bacterial pathogens. Various surface-associated glycoconjugates have been identified in bacteria that promote infectious behavior and survival in the host through motility, adhesion, molecular mimicry, and immune system manipulation. Interestingly, bacterial glycosylation systems that produce these virulence factors frequently feature rare monosaccharides and unusual glycosylation mechanisms. Owing to their marked difference from human glycosylation, bacterial glycosylation systems constitute promising antibacterial targets. With the rise of antibiotic resistance and depletion of the antibiotic pipeline, novel drug targets are urgently needed. Bacteria-specific glycosylation systems are especially promising for antivirulence therapies that do not eliminate a bacterial population, but rather alleviate its pathogenesis. In this review, we describe a selection of unique glycosylation systems in bacterial pathogens and their role in bacterial homeostasis and infection, with a focus on virulence factors. In addition, recent advances to inhibit the enzymes involved in these glycosylation systems and target the bacterial glycan structures directly will be highlighted. Together, this review provides an overview of the current status and promise for the future of using bacterial glycosylation to develop novel antibacterial strategies.

glycosylation, pathogenic bacteria, metabolic oligosaccharide engineering, antibacterial strategies, antivirulence

NCBI PubMed ID: 34630370
Publication DOI: 10.3389/fmicb.2021.745702
Journal NLM ID: 101548977
Publisher: Lausanne: Frontiers Research Foundation
Correspondence: Marthe T.C. Walvoort
Institutions: Faculty of Science and Engineering, Stratingh Institute for Chemistry, University of Groningen, Groningen, The Netherlands