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_136906,IEDB_137472,IEDB_141794,IEDB_142488,IEDB_146664,IEDB_151528,IEDB_151770,IEDB_190606,IEDB_983931,SB_192,SB_7

• 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 RmJQ46
  CSDB ID 31514 (all data & tools)

Show legend Show as text

Structure type: fragment of a bigger structure
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130693,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_140529,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_983931,SB_192,SB_7

• Article ID: 339
  Nnalue NA, Khan GN, Mustafa N "Cross-reactivity between six Enterobacteriaceae complete lipopolysaccharide core chemotypes" - Journal of Medical Microbiology 48(5) (1999) 433-441
  

  To gain insight into the value of lipopolysaccharide (LPS) core determinants for cross-protective immunisation the serological relationships between six complete (LPS) core types from Enterobacteriaceae were investigated. Hyperimmune sera were raised in mice by repeated immunisation with heat-killed strains of Salmonella choleraesuis (Ra core type) or Escherichia coli (core types R1, R2, R3, R4 and K12) and characterised for reactivity with complete and incomplete core chemotypes by ELISA and immunoblotting. Three sera (anti-Ra, anti-R2 and anti-R3) reacted strongly with 3-5 different complete core types whereas the other three (anti-R1, anti-R4 and anti-K12) reacted strongly only with their homologous core types in these assays. Two approaches were used to examine further the structural bases for cross-reactivity between these cores. By the first approach the anti-complete-core sera were tested for cross-reactivity with truncated forms of the Salmonella species core (incomplete cores) derived from core-defective mutants. By the second approach, antisera raised against some core-defective mutants were tested for cross-reactivity with complete cores. The results of these investigations revealed that several pair-wise combinations of core types can be used as immunogens to elicit immune responses that recognise all six core types and that the major determinants which mediate cross-reactivity between complete cores are localised in the outer core region.

  Lipopolysaccharide, core, lipopolysaccharide core, chemotype, Chemotypes, cross-reactivity, crossreactivity, Enterobacteriaceae

  NCBI PubMed ID: 10229540
  Journal NLM ID: 0224131
  Publisher: Reading, England: Society for General Microbiology
  Institutions: Department of Medical Microbiology, Faculty of Medicine and Health Sciences, United Arab Emirates University, Al Ain, United Arab Emirates
  Methods: SDS-PAGE, ELISA, biological assays, serological methods, immunoblotting
  
   
  
  Salmonella choleraesuis SN57, Salmonella typhimurium TV119
  CSDB ID 7761 (all data & tools)

Show legend Show as text

Structure type: fragment of a bigger structure
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_131186,IEDB_135818,IEDB_136906,IEDB_137472,IEDB_141794,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_190606,IEDB_983931,SB_192,SB_7

• Article ID: 339
  Nnalue NA, Khan GN, Mustafa N "Cross-reactivity between six Enterobacteriaceae complete lipopolysaccharide core chemotypes" - Journal of Medical Microbiology 48(5) (1999) 433-441
  

  To gain insight into the value of lipopolysaccharide (LPS) core determinants for cross-protective immunisation the serological relationships between six complete (LPS) core types from Enterobacteriaceae were investigated. Hyperimmune sera were raised in mice by repeated immunisation with heat-killed strains of Salmonella choleraesuis (Ra core type) or Escherichia coli (core types R1, R2, R3, R4 and K12) and characterised for reactivity with complete and incomplete core chemotypes by ELISA and immunoblotting. Three sera (anti-Ra, anti-R2 and anti-R3) reacted strongly with 3-5 different complete core types whereas the other three (anti-R1, anti-R4 and anti-K12) reacted strongly only with their homologous core types in these assays. Two approaches were used to examine further the structural bases for cross-reactivity between these cores. By the first approach the anti-complete-core sera were tested for cross-reactivity with truncated forms of the Salmonella species core (incomplete cores) derived from core-defective mutants. By the second approach, antisera raised against some core-defective mutants were tested for cross-reactivity with complete cores. The results of these investigations revealed that several pair-wise combinations of core types can be used as immunogens to elicit immune responses that recognise all six core types and that the major determinants which mediate cross-reactivity between complete cores are localised in the outer core region.

  Lipopolysaccharide, core, lipopolysaccharide core, chemotype, Chemotypes, cross-reactivity, crossreactivity, Enterobacteriaceae

  NCBI PubMed ID: 10229540
  Journal NLM ID: 0224131
  Publisher: Reading, England: Society for General Microbiology
  Institutions: Department of Medical Microbiology, Faculty of Medicine and Health Sciences, United Arab Emirates University, Al Ain, United Arab Emirates
  Methods: SDS-PAGE, ELISA, biological assays, serological methods, immunoblotting
  
   
  
  Escherichia coli HF4704
  CSDB ID 31500 (all data & tools)

Show legend Show as text

Structure type: fragment of a bigger structure
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130693,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_140529,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_232584,IEDB_983931,SB_192,SB_7

• Article ID: 339
  Nnalue NA, Khan GN, Mustafa N "Cross-reactivity between six Enterobacteriaceae complete lipopolysaccharide core chemotypes" - Journal of Medical Microbiology 48(5) (1999) 433-441
  

  To gain insight into the value of lipopolysaccharide (LPS) core determinants for cross-protective immunisation the serological relationships between six complete (LPS) core types from Enterobacteriaceae were investigated. Hyperimmune sera were raised in mice by repeated immunisation with heat-killed strains of Salmonella choleraesuis (Ra core type) or Escherichia coli (core types R1, R2, R3, R4 and K12) and characterised for reactivity with complete and incomplete core chemotypes by ELISA and immunoblotting. Three sera (anti-Ra, anti-R2 and anti-R3) reacted strongly with 3-5 different complete core types whereas the other three (anti-R1, anti-R4 and anti-K12) reacted strongly only with their homologous core types in these assays. Two approaches were used to examine further the structural bases for cross-reactivity between these cores. By the first approach the anti-complete-core sera were tested for cross-reactivity with truncated forms of the Salmonella species core (incomplete cores) derived from core-defective mutants. By the second approach, antisera raised against some core-defective mutants were tested for cross-reactivity with complete cores. The results of these investigations revealed that several pair-wise combinations of core types can be used as immunogens to elicit immune responses that recognise all six core types and that the major determinants which mediate cross-reactivity between complete cores are localised in the outer core region.

  Lipopolysaccharide, core, lipopolysaccharide core, chemotype, Chemotypes, cross-reactivity, crossreactivity, Enterobacteriaceae

  NCBI PubMed ID: 10229540
  Journal NLM ID: 0224131
  Publisher: Reading, England: Society for General Microbiology
  Institutions: Department of Medical Microbiology, Faculty of Medicine and Health Sciences, United Arab Emirates University, Al Ain, United Arab Emirates
  Methods: SDS-PAGE, ELISA, biological assays, serological methods, immunoblotting
  
   
  
  Escherichia coli EH100
  CSDB ID 31501 (all data & tools)

Show legend Show as text

Structure type: fragment of a bigger structure
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_136906,IEDB_137340,IEDB_137472,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_232584,IEDB_983931,SB_192,SB_7

• Article ID: 339
  Nnalue NA, Khan GN, Mustafa N "Cross-reactivity between six Enterobacteriaceae complete lipopolysaccharide core chemotypes" - Journal of Medical Microbiology 48(5) (1999) 433-441
  

  To gain insight into the value of lipopolysaccharide (LPS) core determinants for cross-protective immunisation the serological relationships between six complete (LPS) core types from Enterobacteriaceae were investigated. Hyperimmune sera were raised in mice by repeated immunisation with heat-killed strains of Salmonella choleraesuis (Ra core type) or Escherichia coli (core types R1, R2, R3, R4 and K12) and characterised for reactivity with complete and incomplete core chemotypes by ELISA and immunoblotting. Three sera (anti-Ra, anti-R2 and anti-R3) reacted strongly with 3-5 different complete core types whereas the other three (anti-R1, anti-R4 and anti-K12) reacted strongly only with their homologous core types in these assays. Two approaches were used to examine further the structural bases for cross-reactivity between these cores. By the first approach the anti-complete-core sera were tested for cross-reactivity with truncated forms of the Salmonella species core (incomplete cores) derived from core-defective mutants. By the second approach, antisera raised against some core-defective mutants were tested for cross-reactivity with complete cores. The results of these investigations revealed that several pair-wise combinations of core types can be used as immunogens to elicit immune responses that recognise all six core types and that the major determinants which mediate cross-reactivity between complete cores are localised in the outer core region.

  Lipopolysaccharide, core, lipopolysaccharide core, chemotype, Chemotypes, cross-reactivity, crossreactivity, Enterobacteriaceae

  NCBI PubMed ID: 10229540
  Journal NLM ID: 0224131
  Publisher: Reading, England: Society for General Microbiology
  Institutions: Department of Medical Microbiology, Faculty of Medicine and Health Sciences, United Arab Emirates University, Al Ain, United Arab Emirates
  Methods: SDS-PAGE, ELISA, biological assays, serological methods, immunoblotting
  
   
  
  Escherichia coli F653
  CSDB ID 31502 (all data & tools)

Show legend Show as text

Structure type: fragment of a bigger structure
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_136906,IEDB_137472,IEDB_141794,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_190606,IEDB_232584,IEDB_983931,SB_192,SB_7

• Article ID: 339
  Nnalue NA, Khan GN, Mustafa N "Cross-reactivity between six Enterobacteriaceae complete lipopolysaccharide core chemotypes" - Journal of Medical Microbiology 48(5) (1999) 433-441
  

  To gain insight into the value of lipopolysaccharide (LPS) core determinants for cross-protective immunisation the serological relationships between six complete (LPS) core types from Enterobacteriaceae were investigated. Hyperimmune sera were raised in mice by repeated immunisation with heat-killed strains of Salmonella choleraesuis (Ra core type) or Escherichia coli (core types R1, R2, R3, R4 and K12) and characterised for reactivity with complete and incomplete core chemotypes by ELISA and immunoblotting. Three sera (anti-Ra, anti-R2 and anti-R3) reacted strongly with 3-5 different complete core types whereas the other three (anti-R1, anti-R4 and anti-K12) reacted strongly only with their homologous core types in these assays. Two approaches were used to examine further the structural bases for cross-reactivity between these cores. By the first approach the anti-complete-core sera were tested for cross-reactivity with truncated forms of the Salmonella species core (incomplete cores) derived from core-defective mutants. By the second approach, antisera raised against some core-defective mutants were tested for cross-reactivity with complete cores. The results of these investigations revealed that several pair-wise combinations of core types can be used as immunogens to elicit immune responses that recognise all six core types and that the major determinants which mediate cross-reactivity between complete cores are localised in the outer core region.

  Lipopolysaccharide, core, lipopolysaccharide core, chemotype, Chemotypes, cross-reactivity, crossreactivity, Enterobacteriaceae

  NCBI PubMed ID: 10229540
  Journal NLM ID: 0224131
  Publisher: Reading, England: Society for General Microbiology
  Institutions: Department of Medical Microbiology, Faculty of Medicine and Health Sciences, United Arab Emirates University, Al Ain, United Arab Emirates
  Methods: SDS-PAGE, ELISA, biological assays, serological methods, immunoblotting
  
   
  
  Escherichia coli F2513
  CSDB ID 31503 (all data & tools)

Show legend Show as text

Structure type: fragment of a bigger structure
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_135813,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_140529,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_232584,IEDB_983931,SB_192,SB_7

• Article ID: 339
  Nnalue NA, Khan GN, Mustafa N "Cross-reactivity between six Enterobacteriaceae complete lipopolysaccharide core chemotypes" - Journal of Medical Microbiology 48(5) (1999) 433-441
  

  To gain insight into the value of lipopolysaccharide (LPS) core determinants for cross-protective immunisation the serological relationships between six complete (LPS) core types from Enterobacteriaceae were investigated. Hyperimmune sera were raised in mice by repeated immunisation with heat-killed strains of Salmonella choleraesuis (Ra core type) or Escherichia coli (core types R1, R2, R3, R4 and K12) and characterised for reactivity with complete and incomplete core chemotypes by ELISA and immunoblotting. Three sera (anti-Ra, anti-R2 and anti-R3) reacted strongly with 3-5 different complete core types whereas the other three (anti-R1, anti-R4 and anti-K12) reacted strongly only with their homologous core types in these assays. Two approaches were used to examine further the structural bases for cross-reactivity between these cores. By the first approach the anti-complete-core sera were tested for cross-reactivity with truncated forms of the Salmonella species core (incomplete cores) derived from core-defective mutants. By the second approach, antisera raised against some core-defective mutants were tested for cross-reactivity with complete cores. The results of these investigations revealed that several pair-wise combinations of core types can be used as immunogens to elicit immune responses that recognise all six core types and that the major determinants which mediate cross-reactivity between complete cores are localised in the outer core region.

  Lipopolysaccharide, core, lipopolysaccharide core, chemotype, Chemotypes, cross-reactivity, crossreactivity, Enterobacteriaceae

  NCBI PubMed ID: 10229540
  Journal NLM ID: 0224131
  Publisher: Reading, England: Society for General Microbiology
  Institutions: Department of Medical Microbiology, Faculty of Medicine and Health Sciences, United Arab Emirates University, Al Ain, United Arab Emirates
  Methods: SDS-PAGE, ELISA, biological assays, serological methods, immunoblotting
  
   
  
  Escherichia coli W3110
  CSDB ID 31504 (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
Trivial name: core-lipid A carbohydrate backbone
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130650,IEDB_130659,IEDB_130670,IEDB_133751,IEDB_135394,IEDB_136906,IEDB_137472,IEDB_140088,IEDB_140529,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_150908,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_226811,IEDB_232584,IEDB_983931,SB_192,SB_7

• Article ID: 1037
  Müller-Loennies S, Brade L, MacKenzie CR, Di Padova FE, Brade H "Identification of a cross-reactive epitope widely present in lipopolysaccharide from enterobacteria and recognized by the cross-protective monoclonal antibody WN1 222-5" - Journal of Biological Chemistry 278(28) (2003) 25618-25627
  

  Septic shock due to infections with Gram-negative bacteria is a severe disease with a high mortality rate. We report the identification of the antigenic determinants of an epitope that is present in enterobacterial lipopolysaccharide (LPS) and recognized by a cross-reactive monoclonal antibody (mAb WN1 222-5) regarded as a potential means of treatment. Using whole LPS and a panel of neoglycoconjugates containing purified LPS oligosaccharides obtained from Escherichia coli core types R1, R2, R3, and R4, Salmonella enterica, and the mutant strain E. coli J-5, we showed that mAb WN1 222-5 binds to the distal part of the inner core region and recognizes the structural element R1-α-D-Glcp-(1→3)-[L-α-D-Hepp-(1→7)]-L-α-D-Hepp 4P-(1→3)-R2 (where R1 represents additional sugars of the outer core and R2 represents additional sugars of the inner core), which is common to LPS from all E. coli, Salmonella, and Shigella. WN1 222-5 binds poorly to molecules that lack the side chain heptose or lack phosphate at the branched heptose. Also molecules that are substituted with GlcpN at the side chain heptose are poorly bound. Thus, the side chain heptose and the 4-phosphate on the branched heptose are main determinants of the epitope. We have determined the binding kinetics and affinities (KD values) of the monovalent interaction of E. coli core oligosaccharides with WN1 222-5 by surface plasmon resonance and isothermal titration microcalorimetry. Affinity constants (KD values) determined by SPR were in the range of 3.6 x 10-5 to 3.2 x 10-8 m, with the highest affinity being observed for the core oligosaccharide from E. coli F576 (R2 core type) and the lowest KD values for those from E. coli J-5. Affinities of E. coli R1, R3, and R4 oligosaccharides were 5-10-fold lower, and values from the E. coli J-5 mutant were 29-fold lower than the R2 core oligosaccharide. Thus, the outer core sugars had a positive effect on binding

  Lipopolysaccharide, lipopolysaccharides, LPS, oligosaccharide, branched, common, core, heptose, chemistry, disease, metabolism, potential, strain, structural, Support, Non-U.S.Gov't, antigenic determinant, chain, molecule, Research, side chain, Escherichia, Escherichia coli, antibodies, antibody, epitope, monoclonal, monoclonal antibodies, monoclonal antibody, phosphate, Oligosaccharides, type, Carbohydrate Sequence, core oligosaccharide, high, infection, Molecular Sequence Data, epitopes, MAb, bacteria, mutant, Salmonella, enterobacterial, sugar, identification, core region, region, inner core, Magnetic Resonance Spectroscopy, medicine, resonance, Salmonella enterica, surface, enterobacteria, Shigella, interaction, Gram-negative bacteria, gram negative bacteria, Gram-negative, mutation, treatment, purified, sugars, antigenic, determinant, binding, bound, effect, Enterobacteriaceae, cross-reactive, heptoses, enzyme-linked immunosorbent assay, constant, neoglycoconjugate, affinity, calorimetry, cross-protective, Dose-Response Relationship, Immunologic, kinetics, mortality, plasmon, Protein Binding, septic, septic shock, shock, Surface Plasmon Resonance, Time Factors, titration

  NCBI PubMed ID: 12716894
  Publication DOI: 10.1074/jbc.M302904200
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: sml@fz-borstel.de
  Institutions: Research Center Borstel, Center for Medicine and Biosciences, Borstel, Germany, Institute for Biological Sciences, national research Council of Canada, Ottava, Ontario, K1A 0R6, Canada, Novartis Pharma AG, CH-4002 Base, Switzerland
  Methods: NMR, serological methods
  
   
  
  Escherichia coli J5
  CSDB ID 3826 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: core-lipid A carbohydrate backbone
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130650,IEDB_130659,IEDB_130670,IEDB_133751,IEDB_135394,IEDB_136906,IEDB_137472,IEDB_140088,IEDB_140529,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_150908,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_226811,IEDB_983931,SB_192,SB_7

• Article ID: 1037
  Müller-Loennies S, Brade L, MacKenzie CR, Di Padova FE, Brade H "Identification of a cross-reactive epitope widely present in lipopolysaccharide from enterobacteria and recognized by the cross-protective monoclonal antibody WN1 222-5" - Journal of Biological Chemistry 278(28) (2003) 25618-25627
  

  Septic shock due to infections with Gram-negative bacteria is a severe disease with a high mortality rate. We report the identification of the antigenic determinants of an epitope that is present in enterobacterial lipopolysaccharide (LPS) and recognized by a cross-reactive monoclonal antibody (mAb WN1 222-5) regarded as a potential means of treatment. Using whole LPS and a panel of neoglycoconjugates containing purified LPS oligosaccharides obtained from Escherichia coli core types R1, R2, R3, and R4, Salmonella enterica, and the mutant strain E. coli J-5, we showed that mAb WN1 222-5 binds to the distal part of the inner core region and recognizes the structural element R1-α-D-Glcp-(1→3)-[L-α-D-Hepp-(1→7)]-L-α-D-Hepp 4P-(1→3)-R2 (where R1 represents additional sugars of the outer core and R2 represents additional sugars of the inner core), which is common to LPS from all E. coli, Salmonella, and Shigella. WN1 222-5 binds poorly to molecules that lack the side chain heptose or lack phosphate at the branched heptose. Also molecules that are substituted with GlcpN at the side chain heptose are poorly bound. Thus, the side chain heptose and the 4-phosphate on the branched heptose are main determinants of the epitope. We have determined the binding kinetics and affinities (KD values) of the monovalent interaction of E. coli core oligosaccharides with WN1 222-5 by surface plasmon resonance and isothermal titration microcalorimetry. Affinity constants (KD values) determined by SPR were in the range of 3.6 x 10-5 to 3.2 x 10-8 m, with the highest affinity being observed for the core oligosaccharide from E. coli F576 (R2 core type) and the lowest KD values for those from E. coli J-5. Affinities of E. coli R1, R3, and R4 oligosaccharides were 5-10-fold lower, and values from the E. coli J-5 mutant were 29-fold lower than the R2 core oligosaccharide. Thus, the outer core sugars had a positive effect on binding

  Lipopolysaccharide, lipopolysaccharides, LPS, oligosaccharide, branched, common, core, heptose, chemistry, disease, metabolism, potential, strain, structural, Support, Non-U.S.Gov't, antigenic determinant, chain, molecule, Research, side chain, Escherichia, Escherichia coli, antibodies, antibody, epitope, monoclonal, monoclonal antibodies, monoclonal antibody, phosphate, Oligosaccharides, type, Carbohydrate Sequence, core oligosaccharide, high, infection, Molecular Sequence Data, epitopes, MAb, bacteria, mutant, Salmonella, enterobacterial, sugar, identification, core region, region, inner core, Magnetic Resonance Spectroscopy, medicine, resonance, Salmonella enterica, surface, enterobacteria, Shigella, interaction, Gram-negative bacteria, gram negative bacteria, Gram-negative, mutation, treatment, purified, sugars, antigenic, determinant, binding, bound, effect, Enterobacteriaceae, cross-reactive, heptoses, enzyme-linked immunosorbent assay, constant, neoglycoconjugate, affinity, calorimetry, cross-protective, Dose-Response Relationship, Immunologic, kinetics, mortality, plasmon, Protein Binding, septic, septic shock, shock, Surface Plasmon Resonance, Time Factors, titration

  NCBI PubMed ID: 12716894
  Publication DOI: 10.1074/jbc.M302904200
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: sml@fz-borstel.de
  Institutions: Research Center Borstel, Center for Medicine and Biosciences, Borstel, Germany, Institute for Biological Sciences, national research Council of Canada, Ottava, Ontario, K1A 0R6, Canada, Novartis Pharma AG, CH-4002 Base, Switzerland
  Methods: NMR, serological methods
  
   
  
  Escherichia coli J5
  CSDB ID 3827 (all data & tools)

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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)

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Structure type: oligomer
Trivial name: GPI-anchor
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130701,IEDB_131186,IEDB_134624,IEDB_135818,IEDB_136104,IEDB_136906,IEDB_137472,IEDB_140116,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_141829,IEDB_142346,IEDB_142347,IEDB_142348,IEDB_143632,IEDB_144983,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_176772,IEDB_190606,IEDB_474450,IEDB_983930,SB_136,SB_163,SB_191,SB_196,SB_198,SB_44,SB_67,SB_7,SB_72

• Article ID: 1736
  McConville MJ, Ferguson MAJ "The structure, biosynthesis and function of glycosylated phosphatidylinositols in the parasitic protozoa and higher eukaryotes" - Biochemical Journal 294 (1993) 305-324
  

  No abstract available

  NCBI PubMed ID: 8373346
  Publication DOI: 10.1042/bj2940305
  Journal NLM ID: 2984726R
  Publisher: London, UK : Published by Portland Press on behalf of the Biochemical Society
  Institutions: Department of Biochemistry, University of Dundee, U.K., Department of Biochemistry, University of Dundee, U.K
  
   
  
  Trypanosoma brucei
  CSDB ID 106315 (all data & tools)

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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)