Show legend Show as text

Structure type: monomer
Contained glycoepitopes: IEDB_136044,IEDB_136095,IEDB_136906,IEDB_137472,IEDB_141794,IEDB_151528,IEDB_190606,SB_165,SB_166,SB_187,SB_195,SB_7,SB_88

• Article ID: 17
  Blixt O, Van Die I, Norberg T, van den Eijnden DH "High-level expression of the Neisseria meningitidis lgtA gene in Escherichia coli and characterization of the encoded N-acetylglucosaminyltransferase as a useful catalyst in the synthesis of GlcNAcb1→3Gal and GalNAcb1-3Gal linkages" - Glycobiology 9(10) (1999) 1061-1071
  

  We have expressed the Neisseria meningitidis lgtA gene at a high level in Escherichia coli. The encoded β-N-acetylglucosaminyltransferase, referred to as LgtA, which in the bacterium is involved in the synthesis of the lacto-N-neo-tetraose structural element of the bacterial lipooligosaccharide, was obtained in an enzymatically highly active form. This glycosyltransferase appeared to be unusual in that it displays a broad acceptor specificity toward both α- and β-galactosides, whether structurally related to N- or O-protein-, or lipid-linked oligosaccharides. Product analysis by one- and two-dimensional 400 MHz 1H- and 13C NMR spectroscopy reveals that LgtA catalyzes the introduction of GlcNAc from UDP-GlcNAc in a β1→3-linkage to accepting Gal residues. The enzyme can thus be characterized as a UDP-GlcNAc:Gal α/β-R β 3-N-acetylglucosaminyltransferase. Although lactose is a highly preferred acceptor substrate the recombinant enzyme also acts efficiently on monomeric and dimeric N-acetyllactosamine revealing its potential value in the synthesis of polylactosaminoglycan structures in enzyme assisted procedures. Furthermore, LgtA shows a high donor promiscuity toward UDP-GalNAc, but not toward other UDP-sugars, and can catalyze the introduction of GalNAc in β1→3-linkage to α- or β-Gal in the acceptor structures at moderate rates. LgtA therefore shows promise to be a useful catalyst in the preparative synthesis of both GlcNAc β1→3 Gal and GalNAc β1→3 Gal linkages.

  oligosaccharide, enzyme-assisted-synthesis, recombinant glycosyltransferase, glycosidic linkage, polylactosaminoglycan, recombinant glycosyltrasferase

  NCBI PubMed ID: 10521543
  Publication DOI: 10.1093/glycob/9.10.1061
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Institutions: Department of Chemistry, Swedish University of Agricultural Sciences, Uppsala, Sweden, Department of Medical Chemistry, Vrije Universiteit, Van der Boechorstraat 7, 1081 BT Amsterdam, The Netherlands
  Methods: 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, enzyme-assisted synthesis, DNA techniques, glycosyltransferase assays, kinetics assays
  
   
  
  Neisseria meningitidis, Escherichia coli
  CSDB ID 1627 (all data & tools)

Show legend Show as text

Structure type: polymer chemical repeating unit
Compound class: EPS
Contained glycoepitopes: IEDB_135614,IEDB_136044,IEDB_137472,IEDB_141794,IEDB_141806,IEDB_142487,IEDB_142488,IEDB_146664,IEDB_153543,IEDB_158555,IEDB_190606,IEDB_241101,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_6,SB_7,SB_88

• Article ID: 287
  Keller M, Roxlau A, Weng WM, Schmidt M, Quandt J, Niehaus K, Jording D, Arnold W, Puhler A "Molecular analysis of the Rhizobium meliloti mucR gene regulating the biosynthesis of the exopolysaccharides succinoglycan and galactoglucan" - Molecular Plant-Microbe Interactions 8 (1995) 267-277
  

  The Rhizobium meliloti Tn5 mutant Rm3131, producing galactoglucan (EPS II) instead of succinoglycan (EPS I), was complemented by a 3.6-kb EcoRI-fragment of the Rhizobium meliloti genome. Sequencing of this fragment revealed six open reading frames (ORFs). The ORF found to be affected in the mutant Rm3131 codes for a putative protein of 15.7 kDa and forms a monocistronic transcriptional unit. Further genetic analysis revealed that the gene mutated in Rm3131 is identical to the previously described R. meliloti mucR gene (H. Zhan, S.B. Levery, C. C. Lee, and J.A. Leigh, 1989, Proc. Natl. Acad. Sci. USA 86:3055-3059). By hybridization it was shown that a mucR homologous gene is present in several rhizobacteria. The deduced amino acid sequence of MucR showed nearly 80% identity to the Agrobacterium tumefaciens Ros protein, a negative regulator of vir genes and necessary for succinoglycan production. MucR contains like Ros a putative zinc finger sequence of the C2H2 type. Transcriptional fusions of genes for EPS I and EPS II synthesis, the so-called exo and exp genes, with the marker gene lacZ were used to delineate the role of mucR for exo and exp gene expression. It was found that exp genes are negatively regulated by MucR on the transcriptional level, whereas a posttranscriptional regulation by MucR is assumed for exo genes. Furthermore, mucR is negatively regulating its own transcription.

  symbiosis, exopolysaccharide synthesis, gene regulation

  NCBI PubMed ID: 7756693
  Publication DOI: 10.1094/MPMI-8-0267
  Journal NLM ID: 9107902
  Institutions: Lehrstuhl für Genetik, Fakultät für Biologie, Universität Bielefeld, Federal Republic of Germany
  Methods: 13C NMR, DNA sequencing, DNA techniques, genetic methods, enzyme assay
  
   
  
  Rhizobium meliloti Rm2011
  CSDB ID 7191 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: O-glycoprotein
Contained glycoepitopes: IEDB_136044,IEDB_136906,IEDB_137472,IEDB_141794,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_153217,IEDB_190606,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_7,SB_88

• Article ID: 468
  Schäffer C, Messner P "Surface-layer glycoproteins: an example for the diversity of bacterial glycosylation with promising impacts on nanobiotechnology" - Glycobiology 14(8) (2004) 31R-42R
  

  Bacterial cell surface layers, referred to simply as S-layers, have been described for all major phylogenetic groups of bacteria, which may indicate their pivotal role for a bacterium in its natural habitat. They have the unique ability to assemble into two-dimensional crystalline arrays that completely cover the bacterial cells. Glycosylation represents the most frequent modification of S-layer proteins. S-layer glycoproteins constitute a class of glycoconjugates first isolated in the mid-1970s, but S-layer glycoprotein research is still being regarded as an 'exotic field of glycobiology,' possibly because of its 'noneukaryotic' character. Extensive work over the past 30 years provided evidence of an enormous diversity of S-layer glycoproteins that have been created in nature over 3 billion years of prokaryotic evolution. These glycoconjugates are substantially different from eukaryotic glycoproteins, with regard to both composition and structure; nevertheless, some general structural concepts may be deduced. The awareness of the high application potential of S-layer glycoproteins, especially in combination with their intrinsic cell surface display feature, in the field of modern nanobiotechnology as a base for glycoengineering has recently led to the investigation of the S-layer protein glycosylation process at the molecular level, which has lagged behind the structural studies due to the lack of suitable molecular tools. From that work an even more interesting picture of this class of glycoconjugates is emerging. The availability of purified enzymes from S-layer glycan biosynthesis pathways exhibiting increased stabilities and/or rare sugar specificities in conjunction with preliminary genomic data on S-layer glycan biosynthesis clusters will pave the way for the rational design of S-layer neoglycoproteins.

  LPS, bacterial glycosylation, genomic glycosylation loci, glycan diversity, glycoengineering, S-layer nanoglycobiology

  NCBI PubMed ID: 15044388
  Publication DOI: 10.1093/glycob/cwh064
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Correspondence: paul.messner@boka.ac.at
  Institutions: Center for NanoBiotechnology, University of Applied Life Sciences and Natural Resources, Gregor-Mendel-Strasse 33, A-1180 Wien, Austria
  
   
  
  Halobacterium halobium R1M1
  CSDB ID 31631 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: LOS
Contained glycoepitopes: IEDB_130650,IEDB_130651,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_141794,IEDB_141807,IEDB_144987,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_221845,IEDB_742247,SB_165,SB_166,SB_187,SB_195,SB_31,SB_62,SB_7,SB_88

• Article ID: 1298
  Yang QL, Gotschlich EC "Variation of gonococcal lipooligosaccharide structure is due to alterations in poly-G tracts in lgt genes encoding glycosyl transferases" - Journal of Experimental Medicine 183 (1996) 323-327
  

  The lipooligosaccharide (LOS) expressed by gonococci spontaneously varies its structure at high frequency, but the underlying genetic mechanism has not been described. We have previously reported that the genes encoding the glycosyl transferases responsible for the biosynthesis of the variable alpha chain of the LOS of Neisseria gonorrhoeae are located in a locus containing five genes, lgtA, lgtB, lgtC, lgtD, and lgtE. Sequence analysis showed that lgtA, lgtC, and lgtD contained poly-G tracts within the coding frames, leading to the hypothesis that shifts in the number of guanosine residues in the poly-G tracts might be responsible for the high frequency variation in structure of gonococcal LOS. We now provide experimental evidence confirming this hypothesis

  structure, Lipooligosaccharide, gene, LOS, tract, variation, transferase, lgt, glycosyl, alteration, gonococcal, transferases, glycosyl transferases

  NCBI PubMed ID: 8551240
  Journal NLM ID: 2985109R
  Publisher: Rockefeller University Press
  Institutions: Laboratory of Bacterial Pathogenesis and Immunology, Rockefeller University, New York, NY, USA
  
   
  
  Neisseria gonorrhoeae 1291b
  CSDB ID 6048 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: K-antigen
Contained glycoepitopes: IEDB_115136,IEDB_136044,IEDB_136095,IEDB_136906,IEDB_137472,IEDB_140630,IEDB_141794,IEDB_151528,IEDB_190606,IEDB_423153,SB_165,SB_166,SB_187,SB_195,SB_7,SB_88

• Article ID: 2176
  Beynon LM, Dutton GGS, Richards JC "Structure of the amino acid-containing capsular polysaccharide from Escherichia coli O8:K49:H21" - Carbohydrate Research 205 (1990) 347-359
  

  The structure of the capsular antigen of E. coli K49 and the oligosaccharides derived from it by partial acid hydrolysis were studied by 1D- and 2D-n.m.r. spectroscopy, g.l.c.-c.i.-mass spectrometry, and methylation analysis. The K49 polysaccharide consists of the repeating unit →4)-β-D-GlcpA-(1→6)-β-D-Galp-(1→6)-β-D-Glcp-(1→3)-β-D-GalpNAc-(1→. The glucuronic acid residues are substituted, in the apparent molar ratio of 4:1, with L-threonine and L-serine linked amidically to the carboxyl group.

  NCBI PubMed ID: 2276143
  Publication DOI: 10.1016/0008-6215(90)80152-s
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: Department of Chemistry, University of British Columbia, Vancouver, Canada
  Methods: 13C NMR, 1H NMR, methylation, GLC-MS, NMR-2D, partial acid hydrolysis, HF solvolysis, sugar analysis, GLC, methanolysis, CI-MS
  
   
  
  Escherichia coli K49
  CSDB ID 2635 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: K-antigen
Contained glycoepitopes: IEDB_115136,IEDB_130648,IEDB_136044,IEDB_136095,IEDB_136906,IEDB_137472,IEDB_137473,IEDB_140630,IEDB_141794,IEDB_142488,IEDB_146664,IEDB_151528,IEDB_190606,IEDB_423153,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_7,SB_88

• Article ID: 2176
  Beynon LM, Dutton GGS, Richards JC "Structure of the amino acid-containing capsular polysaccharide from Escherichia coli O8:K49:H21" - Carbohydrate Research 205 (1990) 347-359
  

  The structure of the capsular antigen of E. coli K49 and the oligosaccharides derived from it by partial acid hydrolysis were studied by 1D- and 2D-n.m.r. spectroscopy, g.l.c.-c.i.-mass spectrometry, and methylation analysis. The K49 polysaccharide consists of the repeating unit →4)-β-D-GlcpA-(1→6)-β-D-Galp-(1→6)-β-D-Glcp-(1→3)-β-D-GalpNAc-(1→. The glucuronic acid residues are substituted, in the apparent molar ratio of 4:1, with L-threonine and L-serine linked amidically to the carboxyl group.

  NCBI PubMed ID: 2276143
  Publication DOI: 10.1016/0008-6215(90)80152-s
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: Department of Chemistry, University of British Columbia, Vancouver, Canada
  Methods: 13C NMR, 1H NMR, methylation, GLC-MS, NMR-2D, partial acid hydrolysis, HF solvolysis, sugar analysis, GLC, methanolysis, CI-MS
  
   
  
  Escherichia coli K49
  CSDB ID 2637 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_114703,IEDB_120354,IEDB_123890,IEDB_130646,IEDB_135813,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_1391962,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142488,IEDB_143794,IEDB_144998,IEDB_144999,IEDB_145003,IEDB_146664,IEDB_150899,IEDB_151528,IEDB_151531,IEDB_167070,IEDB_190606,IEDB_241103,IEDB_241107,IEDB_241118,IEDB_885811,IEDB_983931,SB_137,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_29,SB_30,SB_7,SB_88

• Article ID: 2970
  Gmeiner J "The ribitol-phosphate-containing lipopolysaccharide from Proteus mirabilis, strain D52. Investigations of O-specific chains" - European Journal of Biochemistry 74 (1977) 171-180
  

  A soluble hydrophilic lipopolysaccharide, termed lipopolysaccharide II, isolated from Proteus mirabilis, strain D52 contained N-acetylglucosamine, glucose, galactose, ribitol phosphate and ethanolamine phosphate as constituents of the O-specific polysaccharide. Periodate oxidation studies were carried out on the polymer before and after dephosphorylation with hydrofluoric acid and on oligosaccharides derived from the polymer by partial acid hydrolysis. The results obtained indicate that the polysaccharide chain consists of the chemical repeating unit Gal-1,3(4)-GlcNAc-1,3-Glc-1,3-GlcNAc-, where GlcNAc stands for N-acetylglucosamine. Whereas the galactose residue is substituted at C-3 by ribitol phosphate, the glucose is substituted by ethanolamine phosphate at C-6.

  NCBI PubMed ID: 323005
  Journal NLM ID: 0107600
  Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
  
   
  
  Proteus mirabilis D52
  CSDB ID 122439 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure
Compound class: LPS
Contained glycoepitopes: IEDB_130701,IEDB_135513,IEDB_136044,IEDB_136093,IEDB_136095,IEDB_136105,IEDB_136906,IEDB_137472,IEDB_137485,IEDB_137486,IEDB_1394181,IEDB_1394182,IEDB_141794,IEDB_141798,IEDB_144983,IEDB_151528,IEDB_152206,IEDB_190606,IEDB_225177,IEDB_885823,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_44,SB_67,SB_7,SB_72,SB_88

• Article ID: 3093
  Pappas RS, Sweetman BJ, Ray S, Hellerqvist CG "Monomer sequence determination of carbohydrates using fast-atom bombardment mass spectrometry of periodate-oxidized acetate ester derivatives" - Carbohydrate Research 197 (1990) 1-14
  

  A derivatization method, adapted from that of Angel et al. (ref. 10), for sequencing sugar residues in partially degraded poly- and oligo-saccharides using positive-ion f.a.b.-m.s. is described. Derivative selection provides sequence information by directing fragmentation exclusively to both sides of glycosidic oxygen atoms and, in the case of opened rings, between glycosidic carbon and ring oxygen atoms. Polysaccharides or oligosaccharides are subjected to sequential periodate oxidation, borodeuteride reduction, and acetylation. The derivatized polysaccharides are then subjected to partial degradation, acetylation, and high-performance liquid chromatography (h.p.l.c.) purification. F.a.b.-m.s. data obtained on model compounds, using 3-nitrobenzyl alcohol as matrix for f.a.b.-m.s., demonstrated direction of fragmentation to both sides of the glycosidic oxygen atom in unoxidized residues, and to both sides of the acetal oxygen atoms in oxidized residues. Oligosaccharide linkage and sequence may thus be determined by observing fragmentation from both the reducing and non-reducing ends of the molecule. Two Salmonella lipopolysaccharides, derivatized by this procedure, were partially hydrolyzed and then acetylated. Analysis of the h.p.l.c.-purified oligosaccharide derivatives by f.a.b.-m.s. demonstrated the applicability of the technique for sequencing nmol quantities of branched structures.

  Publication DOI: 10.1016/0008-6215(90)84125-E
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: Department of Biochemistry, Vanderbilt University, School of Medicine Nashville, Tennessee 37232, USA
  Methods: FAB-MS, HPLC
  
   
  
  Salmonella typhimurium LT2
  CSDB ID 115840 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure
Compound class: LPS
Contained glycoepitopes: IEDB_130660,IEDB_130701,IEDB_136044,IEDB_136095,IEDB_136105,IEDB_136906,IEDB_137472,IEDB_137485,IEDB_1394181,IEDB_1394182,IEDB_139420,IEDB_139421,IEDB_141794,IEDB_141798,IEDB_144983,IEDB_151528,IEDB_152206,IEDB_174033,IEDB_190606,IEDB_225177,IEDB_885823,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_44,SB_67,SB_7,SB_72,SB_88

• Article ID: 3093
  Pappas RS, Sweetman BJ, Ray S, Hellerqvist CG "Monomer sequence determination of carbohydrates using fast-atom bombardment mass spectrometry of periodate-oxidized acetate ester derivatives" - Carbohydrate Research 197 (1990) 1-14
  

  A derivatization method, adapted from that of Angel et al. (ref. 10), for sequencing sugar residues in partially degraded poly- and oligo-saccharides using positive-ion f.a.b.-m.s. is described. Derivative selection provides sequence information by directing fragmentation exclusively to both sides of glycosidic oxygen atoms and, in the case of opened rings, between glycosidic carbon and ring oxygen atoms. Polysaccharides or oligosaccharides are subjected to sequential periodate oxidation, borodeuteride reduction, and acetylation. The derivatized polysaccharides are then subjected to partial degradation, acetylation, and high-performance liquid chromatography (h.p.l.c.) purification. F.a.b.-m.s. data obtained on model compounds, using 3-nitrobenzyl alcohol as matrix for f.a.b.-m.s., demonstrated direction of fragmentation to both sides of the glycosidic oxygen atom in unoxidized residues, and to both sides of the acetal oxygen atoms in oxidized residues. Oligosaccharide linkage and sequence may thus be determined by observing fragmentation from both the reducing and non-reducing ends of the molecule. Two Salmonella lipopolysaccharides, derivatized by this procedure, were partially hydrolyzed and then acetylated. Analysis of the h.p.l.c.-purified oligosaccharide derivatives by f.a.b.-m.s. demonstrated the applicability of the technique for sequencing nmol quantities of branched structures.

  Publication DOI: 10.1016/0008-6215(90)84125-E
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: Department of Biochemistry, Vanderbilt University, School of Medicine Nashville, Tennessee 37232, USA
  Methods: FAB-MS, HPLC
  
   
  
  Salmonella strasbourg
  CSDB ID 115841 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Trivial name: core region
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_115013,IEDB_120354,IEDB_123890,IEDB_130645,IEDB_130648,IEDB_130650,IEDB_130651,IEDB_130670,IEDB_131186,IEDB_134624,IEDB_135813,IEDB_135818,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137473,IEDB_138950,IEDB_1391961,IEDB_1391964,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_140529,IEDB_141495,IEDB_141584,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_144987,IEDB_144998,IEDB_146664,IEDB_149558,IEDB_151528,IEDB_151531,IEDB_152217,IEDB_153201,IEDB_156493,IEDB_167069,IEDB_167072,IEDB_190606,IEDB_2189047,IEDB_221845,IEDB_241097,IEDB_418765,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_419431,IEDB_423106,IEDB_742245,IEDB_742246,IEDB_742247,IEDB_742248,IEDB_742249,IEDB_885822,IEDB_918313,IEDB_918314,IEDB_918316,IEDB_983931,SB_163,SB_165,SB_166,SB_167,SB_176,SB_178,SB_187,SB_192,SB_195,SB_31,SB_6,SB_62,SB_7,SB_87,SB_88

• Article ID: 3623
  Knirel YA, Kochetkov NK "The structure of lipopolysaccharides of gram-negative bacteria. II. The structure of the core region" - Biochemistry (Moscow) 58(2) (1993) 84-99
  

  This review summarizes data on the structure of the core of bacterial lipopolysaccharides (LPS), an oligosaccharide which binds the lipid moiety of LPS to the O-antigenic polysaccharide chain. Both S-strains with complete LPS and R-mutants having various defects of core biosynthesis are considered. The role of the core in the functioning of the outer membrane and in the manifestation of antigenic specificity of LPS is discussed.

  Lipopolysaccharide, antigen, lipopolysaccharides, LPS, structure, core, bacteria, core region, region, Gram-negative bacteria, gram negative bacteria, Gram-negative, review, outer membrane, bacterial lipopolysaccharide

  Journal NLM ID: 0376536
  Publisher: Nauka/Interperiodica
  Institutions: N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow (Russian Federation)
  
   
  
  Neisseria gonorrhoeae JW31R
  CSDB ID 24966 (all data & tools)

Show legend Show as text

Structure type: polymer chemical repeating unit
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_130660,IEDB_130701,IEDB_136044,IEDB_136105,IEDB_136906,IEDB_137472,IEDB_1394181,IEDB_1394182,IEDB_139421,IEDB_141794,IEDB_144983,IEDB_151528,IEDB_152206,IEDB_174033,IEDB_190606,IEDB_225177,IEDB_885823,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_44,SB_67,SB_7,SB_72,SB_88

• Article ID: 3635
  Fukuda M, Egami F, Hammerling G, Luderitz O, Bagdian G, Staub AM "A reinvestigation of the anomeric configuration of mannose in the antigens of Salmonella groups B, D and E" - European Journal of Biochemistry 20(3) (1971) 438-441
  

  The anomeric configuration of mannose is a in the 0 antigens of Salmonella groups Band D, and b in group E, i.e. directly opposite to what was anticipated earlier from data obtained with mannosidase from rat epididymis. The present results were obtained with the aid of a-mannosidase from jack bean meal and of purified a- and b-mannosidases from a marine gastropod, which were allowed to act upon the disaccharides mannosyl-rhamnose isolated from partial hydrolysates of the respective antigens. The new findings, however, do not alter the validity of previous conclusions.

  antigen, chemistry, analysis, group, antigens, immunology, Salmonella, Salmonella typhimurium, chromatography, Mannose, configuration, reinvestigation, anomeric, anomeric configuration, Glycoside Hydrolases, D, Mollusca, Plant Extracts

  NCBI PubMed ID: 4931954
  Journal NLM ID: 0107600
  Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
  Institutions: Department of Biophysics and Biochemistry, Faculty of Science, Univwersity of Tokyo.
  Methods: biochemical methods
  
   
  
  Salmonella typhi D1
  CSDB ID 23601 (all data & tools)

Show legend Show as text

Structure type: polymer chemical repeating unit
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_136044,IEDB_136105,IEDB_136906,IEDB_137472,IEDB_137485,IEDB_1394181,IEDB_1394182,IEDB_139420,IEDB_139421,IEDB_141794,IEDB_144983,IEDB_151528,IEDB_152206,IEDB_190606,IEDB_225177,IEDB_885823,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_44,SB_7,SB_72,SB_88

• Article ID: 3635
  Fukuda M, Egami F, Hammerling G, Luderitz O, Bagdian G, Staub AM "A reinvestigation of the anomeric configuration of mannose in the antigens of Salmonella groups B, D and E" - European Journal of Biochemistry 20(3) (1971) 438-441
  

  The anomeric configuration of mannose is a in the 0 antigens of Salmonella groups Band D, and b in group E, i.e. directly opposite to what was anticipated earlier from data obtained with mannosidase from rat epididymis. The present results were obtained with the aid of a-mannosidase from jack bean meal and of purified a- and b-mannosidases from a marine gastropod, which were allowed to act upon the disaccharides mannosyl-rhamnose isolated from partial hydrolysates of the respective antigens. The new findings, however, do not alter the validity of previous conclusions.

  antigen, chemistry, analysis, group, antigens, immunology, Salmonella, Salmonella typhimurium, chromatography, Mannose, configuration, reinvestigation, anomeric, anomeric configuration, Glycoside Hydrolases, D, Mollusca, Plant Extracts

  NCBI PubMed ID: 4931954
  Journal NLM ID: 0107600
  Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
  Institutions: Department of Biophysics and Biochemistry, Faculty of Science, Univwersity of Tokyo.
  Methods: biochemical methods
  
   
  
  Salmonella strasbourg D2
  CSDB ID 29901 (all data & tools)

Show legend Show as text

Structure type: polymer chemical repeating unit
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_130701,IEDB_136044,IEDB_136105,IEDB_137472,IEDB_1394181,IEDB_1394182,IEDB_141794,IEDB_144983,IEDB_152206,IEDB_190606,IEDB_225177,IEDB_885823,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_44,SB_67,SB_7,SB_72,SB_88

• Article ID: 3637
  Ryan JM, Conrad HE "Structural heterogeneity in the lipopolysaccharide of Salmonella newington" - Archives of Biochemistry and Biophysics 162(2) (1974) 530-535
  

  Salmonella newington lipopolysaccharide extracted from a cell paste grown up from a single smooth clone was fractionated by chromatography on DEAE-cellulose in the presence of 1% Triton X-100 into seven lipopolysaccharide fractions which differed in their degrees of polymerization of the repeating unit of the O-antigen side chain and in their substitution with ester phosphate. Several of the lipopolysaccharide fractions were hydrolyzed in 1% acetic acid at 100 °C to cleave the linkage between the polysaccharide and lipid A parts of the structure. The polysaccharide fractions from each of the purified lipopolysaccharides could be further fractionated on DEAE-cellulose columns to yield a number of peaks of polysaccharide having monosaccharide ratios quite distinct from those of the parent lipopolysaccharide. The results show a high degree of structural heterogeneity in the original lipopolysaccharide.

  Lipopolysaccharide, carbohydrates, lipopolysaccharides, structural, analysis, Salmonella, glucose, rhamnose, galactose, chromatography, Mannose, PDF, Glucosamine, heterogeneity, gel, Phosphates, DEAE-Cellulose, Salmonella newington, Surface-Active Agents

  NCBI PubMed ID: 4407306
  Journal NLM ID: 0372430
  Institutions: Department of Biochemistry, University of Illinois, Urbana, IL, USA
  Methods: sugar analysis
  
   
  
  Salmonella newington
  CSDB ID 23603 (all data & tools)

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Structure type: oligomer
Aglycon: lipid A
Compound class: core oligosaccharide with O-unit
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130658,IEDB_130659,IEDB_130693,IEDB_130701,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137777,IEDB_137778,IEDB_1394181,IEDB_1394182,IEDB_140529,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_144983,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_167069,IEDB_190606,IEDB_225177,IEDB_885823,IEDB_983930,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_44,SB_6,SB_67,SB_7,SB_72,SB_88

• Article ID: 3637
  Ryan JM, Conrad HE "Structural heterogeneity in the lipopolysaccharide of Salmonella newington" - Archives of Biochemistry and Biophysics 162(2) (1974) 530-535
  

  Salmonella newington lipopolysaccharide extracted from a cell paste grown up from a single smooth clone was fractionated by chromatography on DEAE-cellulose in the presence of 1% Triton X-100 into seven lipopolysaccharide fractions which differed in their degrees of polymerization of the repeating unit of the O-antigen side chain and in their substitution with ester phosphate. Several of the lipopolysaccharide fractions were hydrolyzed in 1% acetic acid at 100 °C to cleave the linkage between the polysaccharide and lipid A parts of the structure. The polysaccharide fractions from each of the purified lipopolysaccharides could be further fractionated on DEAE-cellulose columns to yield a number of peaks of polysaccharide having monosaccharide ratios quite distinct from those of the parent lipopolysaccharide. The results show a high degree of structural heterogeneity in the original lipopolysaccharide.

  Lipopolysaccharide, carbohydrates, lipopolysaccharides, structural, analysis, Salmonella, glucose, rhamnose, galactose, chromatography, Mannose, PDF, Glucosamine, heterogeneity, gel, Phosphates, DEAE-Cellulose, Salmonella newington, Surface-Active Agents

  NCBI PubMed ID: 4407306
  Journal NLM ID: 0372430
  Institutions: Department of Biochemistry, University of Illinois, Urbana, IL, USA
  Methods: sugar analysis
  
   
  
  Salmonella newington
  CSDB ID 23902 (all data & tools)

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Structure type: polymer chemical repeating unit ; n=20
Trivial name: lipoteichoic acid
Compound class: cell wall polysaccharide
Contained glycoepitopes: IEDB_130695,IEDB_136044,IEDB_136906,IEDB_137472,IEDB_141794,IEDB_151528,IEDB_1597446,IEDB_190606,SB_165,SB_166,SB_187,SB_195,SB_7,SB_88

• Article ID: 3802
  Webb AJ, Karatsa-Dodgson M, Grundling A "Two-enzyme systems for glycolipid and polyglycerolphosphate lipoteichoic acid synthesis in Listeria monocytogenes" - Molecular Microbiology 74(2) (2009) 299-314
  

  Lipoteichoic acid (LTA) is an important cell wall polymer in gram-positive bacteria and often consists a polyglycerolphosphate backbone chain that is linked to the membrane by a glycolipid. In Listeria monocytogenes this glycolipid is Gal-Glc-DAG or Gal-Ptd-6Glc-DAG. Using a bioinformatics approach, we have identified L. monocytogenes genes predicted to be involved in glycolipid (lmo2555 and lmo2554) and LTA backbone (lmo0644 and lmo0927) synthesis. LTA and glycolipid analysis of wild-type and mutant strains confirmed the function of Lmo2555 and Lmo2554 as glycosyltransferases required for the formation of Glc-DAG and Gal-Glc-DAG. Deletion of a third gene, lmo2553, located in the same operon resulted in the production of LTA with an altered structure. lmo0927 and lmo0644 encode proteins with high similarity to the staphylococcal LTA synthase LtaS, which is responsible for polyglycerolphosphate backbone synthesis. We show that both proteins are involved in LTA synthesis. Our data support a model whereby Lmo0644 acts as an LTA primase LtaP and transfers the initial glycerolphosphate onto the glycolipid anchor, and Lmo0927 functions as LTA synthase LtaS, which extends the glycerolphosphate backbone chain. Inactivation of LtaS leads to severe growth and cell division defects, underscoring the pivotal role of LTA in this gram-positive pathogen.

  lipopolysaccharides, structure, mass spectrometry, glycosyltransferase, glycolipid, lipoteichoic acid, Listeria monocytogenes

  NCBI PubMed ID: 19682249
  Journal NLM ID: 8712028
  Publisher: Blackwell Publishing
  Correspondence: a.grundling@imperial.ac.uk
  Institutions: Department of Microbiology, Imperial College London, London, UK
  Methods: SDS-PAGE, TLC, MALDI-MS, genetic methods, electron microscopy
  
   
  
  Listeria monocytogenes
  CSDB ID 23878 (all data & tools)