Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Trivial name: lipooligosaccharide core L2
Compound class: LOS
Contained glycoepitopes: IEDB_130646,IEDB_130650,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_144998,IEDB_146100,IEDB_146664,IEDB_149144,IEDB_149174,IEDB_150933,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_418762,IEDB_418764,IEDB_418767,IEDB_418769,IEDB_419429,IEDB_419430,IEDB_423120,IEDB_983931,SB_115,SB_116,SB_131,SB_145,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_187,SB_192,SB_195,SB_30,SB_39,SB_6,SB_68,SB_7,SB_84,SB_88

• Article ID: 7
  Berrington AW, Tan YC, Srikhanta Y, Kuipers B, van der LP, Peak IR, Jennings MP "Phase variation in meningococcal lipooligosaccharide biosynthesis genes" - FEMS Immunology and Medical Microbiology 34(4) (2002) 267-275
  

  Neisseria meningitidis expresses a range of lipooligosaccharide (LOS) structures, comprising of at least 13 immunotypes (ITs). Meningococcal LOS is subject to phase variation of its terminal structures allowing switching between ITs, which is proposed to have functional significance in disease. The objectives of this study were to investigate the repertoire of structures that can be expressed in clinical isolates, and to examine the role of phase-variable expression of LOS genes during invasive disease. Southern blotting was used to detect the presence of LOS biosynthetic genes in two collections of meningococci, a global set of strains previously assigned to lineages of greater or lesser virulence, and a collection of local clinical isolates which included paired throat and blood isolates from individual patients. Where the phase-variable genes lgtA, lgtC or lgtG were identified, they were amplified by PCR and the homopolymeric tracts, responsible for their phase-variable expression, were sequenced. The results revealed great potential for variation between alternate LOS structures in the isolates studied, with most strains capable of expressing several alternative terminal structures. The structures predicted to be currently expressed by the genotype of the strains agreed well with conventional immunotyping. No correlation was observed between the structural repertoire and virulence of the isolate. Based on the potential for LOS phase variation in the clinical collection and observations with the paired patient isolates, our data suggest that phase variation of LOS structures is not required for translocation between distinct compartments in the host

  Lipopolysaccharide, biosynthesis, structure, Meningococcus, Phase variation, Lipooligosaccharide, Pathogenesis, Neisseria meningitidis, alternative, Bacterial Proteins, biosynthetic, blood, blotting, chemistry, clinical, correlation, disease, expression, functional, gene, Gene Expression Regulation, Bacterial, genetics, genotype, growth & development, host, human, immunotype, immunotyping, invasive, isolate, LOS, meningococcal, Meningococcal Infections, meningococci, metabolism, microbiology, Neisseria, pathogenicity, PCR, phase, phenotype, polymerase chain reaction, potential, role, Sequence Analysis, DNA, significance, strain, structural, Support, Non-U.S.Gov't, terminal, tract, translocation, variation, Variation (Genetics), virulence

  NCBI PubMed ID: 12443826
  Journal NLM ID: 9315554
  Publisher: Elsevier
  Correspondence: jennings@biosci.uq.edu.au
  Institutions: Department of Microbiology and Parasitology, University of Queensland, St. Lucia, Brisbane, Qld 4072, Australia, National Institute of Public Health and the Environment, Bilthoven, The Netherlands, School of Health Science, Gri?th University, Gold Coast Campus, Qld 4217, Australia
  Methods: PCR, DNA sequencing
  
   
  
  Neisseria meningitidis
  CSDB ID 1606 (all data & tools)
• Article ID: 277
  Kahler CM, Carlson RW, Rahman MM, Martin LE, Stephens DS "Two glycosyltransferase genes, lgtF and rfaK, constitute the lipooligosaccharide ice (inner core extension) biosynthesis operon of Neisseria meningitidis" - Journal of Bacteriology 178(23) (1996) 6677-6684
  

  We have characterized an operon required for inner-core biosynthesis of the lipooligosaccharide (LOS) of Neisseria meningitidis. Using Tn916 mutagenesis, we recently identified the α-1,2-N-acetylglucosamine (GlcNAc) transferase gene (rfaK), which when inactivated prevents the addition of GlcNAc and alpha chain to the meningococcal LOS inner core (C. M. Kahler, R. W. Carlson, M. M. Rahman, L. E. Martin, and D. S. Stephens, J. Bacteriol. 178:1265-1273, 1996). During the study of rfaK, a second open reading frame (lgtF) of 720 bp was found upstream of rfaK. An amino acid sequence homology search of the GenBank and EMBL databases revealed that the amino terminus of LgtF has significant homology with a family of β-glycosyltransferases involved in the biosynthesis of polysaccharides and O antigen of lipopolysaccharides. The chromosomal copy of lgtF was mutagenized with a nonpolar antibiotic resistance cassette to minimize potential polar effects on rfaK. Tricine sodium dodecyl sulfate-polyacrylamide gel electrophoresis and composition analysis of the LOS from the nonpolar lgtF mutant showed that this strain produced a truncated LOS structure which contained a LOS inner core of GlcNAc1Hep2KDO2lipid A but without the addition of lacto-N-neotetraose to HepI or glucose to HepII. These results and the amino acid homology with β-glycosyltransferases suggest that lgtF encodes the UDP-glucose:LOS-β-1,4-glucosyltransferase which attaches the first glucose residue to HepI of LOS. Reverse transcriptase PCR and primer extension analysis indicate that both lgtF and rfaK are cotranscribed as a polycistronic message from a promoter upstream of lgtF. This arrangement suggests that completion of the LOS inner core and the initiation of the alpha chain addition are tightly coregulated in N. meningitidis.

  biosynthesis, Lipooligosaccharide, Neisseria meningitidis, gene, inner core, glycosyltransferase, operon

  NCBI PubMed ID: 8955282
  Journal NLM ID: 2985120R
  Publisher: American Society for Microbiology
  Correspondence: dstep01@emory.edu
  Institutions: Departments of Medicine and Microbiology and Immunology, Emory University School of Medicine and Department of Veterans Affairs Medical Center, Atlanta, and The Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia
  Methods: genetic methods
  
   
  
  Neisseria meningitidis L2
  CSDB ID 7176 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_130646,IEDB_130650,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_149144,IEDB_149174,IEDB_150933,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_418762,IEDB_418764,IEDB_418767,IEDB_418769,IEDB_419429,IEDB_423120,IEDB_983931,SB_115,SB_116,SB_131,SB_145,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_187,SB_192,SB_195,SB_30,SB_39,SB_6,SB_68,SB_7,SB_84,SB_88

• Article ID: 7
  Berrington AW, Tan YC, Srikhanta Y, Kuipers B, van der LP, Peak IR, Jennings MP "Phase variation in meningococcal lipooligosaccharide biosynthesis genes" - FEMS Immunology and Medical Microbiology 34(4) (2002) 267-275
  

  Neisseria meningitidis expresses a range of lipooligosaccharide (LOS) structures, comprising of at least 13 immunotypes (ITs). Meningococcal LOS is subject to phase variation of its terminal structures allowing switching between ITs, which is proposed to have functional significance in disease. The objectives of this study were to investigate the repertoire of structures that can be expressed in clinical isolates, and to examine the role of phase-variable expression of LOS genes during invasive disease. Southern blotting was used to detect the presence of LOS biosynthetic genes in two collections of meningococci, a global set of strains previously assigned to lineages of greater or lesser virulence, and a collection of local clinical isolates which included paired throat and blood isolates from individual patients. Where the phase-variable genes lgtA, lgtC or lgtG were identified, they were amplified by PCR and the homopolymeric tracts, responsible for their phase-variable expression, were sequenced. The results revealed great potential for variation between alternate LOS structures in the isolates studied, with most strains capable of expressing several alternative terminal structures. The structures predicted to be currently expressed by the genotype of the strains agreed well with conventional immunotyping. No correlation was observed between the structural repertoire and virulence of the isolate. Based on the potential for LOS phase variation in the clinical collection and observations with the paired patient isolates, our data suggest that phase variation of LOS structures is not required for translocation between distinct compartments in the host

  Lipopolysaccharide, biosynthesis, structure, Meningococcus, Phase variation, Lipooligosaccharide, Pathogenesis, Neisseria meningitidis, alternative, Bacterial Proteins, biosynthetic, blood, blotting, chemistry, clinical, correlation, disease, expression, functional, gene, Gene Expression Regulation, Bacterial, genetics, genotype, growth & development, host, human, immunotype, immunotyping, invasive, isolate, LOS, meningococcal, Meningococcal Infections, meningococci, metabolism, microbiology, Neisseria, pathogenicity, PCR, phase, phenotype, polymerase chain reaction, potential, role, Sequence Analysis, DNA, significance, strain, structural, Support, Non-U.S.Gov't, terminal, tract, translocation, variation, Variation (Genetics), virulence

  NCBI PubMed ID: 12443826
  Journal NLM ID: 9315554
  Publisher: Elsevier
  Correspondence: jennings@biosci.uq.edu.au
  Institutions: Department of Microbiology and Parasitology, University of Queensland, St. Lucia, Brisbane, Qld 4072, Australia, National Institute of Public Health and the Environment, Bilthoven, The Netherlands, School of Health Science, Gri?th University, Gold Coast Campus, Qld 4217, Australia
  Methods: PCR, DNA sequencing
  
   
  
  Neisseria meningitidis
  CSDB ID 1708 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130646,IEDB_130650,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_149144,IEDB_149174,IEDB_150933,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_418761,IEDB_418762,IEDB_418763,IEDB_418764,IEDB_418765,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_423120,IEDB_983931,SB_115,SB_116,SB_131,SB_145,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_187,SB_192,SB_195,SB_30,SB_39,SB_6,SB_68,SB_7,SB_84,SB_88

• Article ID: 7
  Berrington AW, Tan YC, Srikhanta Y, Kuipers B, van der LP, Peak IR, Jennings MP "Phase variation in meningococcal lipooligosaccharide biosynthesis genes" - FEMS Immunology and Medical Microbiology 34(4) (2002) 267-275
  

  Neisseria meningitidis expresses a range of lipooligosaccharide (LOS) structures, comprising of at least 13 immunotypes (ITs). Meningococcal LOS is subject to phase variation of its terminal structures allowing switching between ITs, which is proposed to have functional significance in disease. The objectives of this study were to investigate the repertoire of structures that can be expressed in clinical isolates, and to examine the role of phase-variable expression of LOS genes during invasive disease. Southern blotting was used to detect the presence of LOS biosynthetic genes in two collections of meningococci, a global set of strains previously assigned to lineages of greater or lesser virulence, and a collection of local clinical isolates which included paired throat and blood isolates from individual patients. Where the phase-variable genes lgtA, lgtC or lgtG were identified, they were amplified by PCR and the homopolymeric tracts, responsible for their phase-variable expression, were sequenced. The results revealed great potential for variation between alternate LOS structures in the isolates studied, with most strains capable of expressing several alternative terminal structures. The structures predicted to be currently expressed by the genotype of the strains agreed well with conventional immunotyping. No correlation was observed between the structural repertoire and virulence of the isolate. Based on the potential for LOS phase variation in the clinical collection and observations with the paired patient isolates, our data suggest that phase variation of LOS structures is not required for translocation between distinct compartments in the host

  Lipopolysaccharide, biosynthesis, structure, Meningococcus, Phase variation, Lipooligosaccharide, Pathogenesis, Neisseria meningitidis, alternative, Bacterial Proteins, biosynthetic, blood, blotting, chemistry, clinical, correlation, disease, expression, functional, gene, Gene Expression Regulation, Bacterial, genetics, genotype, growth & development, host, human, immunotype, immunotyping, invasive, isolate, LOS, meningococcal, Meningococcal Infections, meningococci, metabolism, microbiology, Neisseria, pathogenicity, PCR, phase, phenotype, polymerase chain reaction, potential, role, Sequence Analysis, DNA, significance, strain, structural, Support, Non-U.S.Gov't, terminal, tract, translocation, variation, Variation (Genetics), virulence

  NCBI PubMed ID: 12443826
  Journal NLM ID: 9315554
  Publisher: Elsevier
  Correspondence: jennings@biosci.uq.edu.au
  Institutions: Department of Microbiology and Parasitology, University of Queensland, St. Lucia, Brisbane, Qld 4072, Australia, National Institute of Public Health and the Environment, Bilthoven, The Netherlands, School of Health Science, Gri?th University, Gold Coast Campus, Qld 4217, Australia
  Methods: PCR, DNA sequencing
  
   
  
  Neisseria meningitidis
  CSDB ID 1709 (all data & tools)

Show legend Show as text

Structure type: polymer chemical repeating unit ; n=5, 14, >14
Compound class: CPS
Contained glycoepitopes: IEDB_1083493,IEDB_1083495,IEDB_130646,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_1392542,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142344,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_143634,IEDB_146100,IEDB_146107,IEDB_146664,IEDB_149138,IEDB_149139,IEDB_149141,IEDB_149142,IEDB_149143,IEDB_149144,IEDB_149145,IEDB_149147,IEDB_149148,IEDB_149150,IEDB_149151,IEDB_149174,IEDB_150933,IEDB_151531,IEDB_161524,IEDB_190606,IEDB_423120,IEDB_983931,SB_115,SB_116,SB_131,SB_145,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_187,SB_192,SB_195,SB_30,SB_39,SB_6,SB_68,SB_7,SB_84,SB_88

• Article ID: 22
  Brisson J, Uhrinova S, Woods RJ, van der Zwan M, Jarrel HC, Paoletti LC, Kasper DL, Jennings HJ "NMR and molecular dynamics studies of the conformational epitope of the type III group B Streptococcus capsular polysaccharide and derivatives" - Biochemistry 36(11) (1997) 3278-3292
  

  The conformational epitope of the type III group B Streptococcus capsular polysaccharide (GBSP III) exhibits unique properties which can be ascribed to the presence of sialic acid in its structure and the requirement for an extended binding site. By means of NMR and molecular dynamics studies on GBSP III and its fragments, the extended epitope of GBSP III was further defined. The influence of sialic acid on the conformational properties of GBSP III was examined by performing conformational analysis on desialylated GBSP III, which is identical to the polysaccharide of Streptococcus pneumoniae type 14, and also on oxidized and reduced GBSP III. Conformational changes were gauged by 1H and 13C chemical shift analysis, NOE, 1D selective TOCSY-NOESY experiments, J(HH) and J(CH) variations, and NOE of OH resonances. Changes in mobility were examined by 13C T1 and T2 measurements. Unrestrained molecular dynamics simulations with explicit water using the AMBER force field and the GLYCAM parameter set were used to assess static and dynamic conformational models, simulate the observable NMR parameters and calculate helical parameters. GBSP III was found to be capable of forming extended helices. Hence, the length dependence of the conformational epitope could be explained by its location on extended helices within the random coil structure of GBSP III. The interaction of sialic acid with the backbone of the PS was also found to be important in defining the conformational epitope of GBSP III

  NMR, capsular, polysaccharide, Streptococcus, capsular polysaccharide, group, molecular, epitope, type, conformational, dynamics, group B Streptococcus, molecular dynamics, NMR spectroscopy, type III group B streptococcus

  NCBI PubMed ID: 9116006
  Publication DOI: 10.1021/bi961819l
  Journal NLM ID: 0370623
  Publisher: American Chemical Society
  Institutions: Institute for Biological Sciences, National Research Council of Canada, Ottawa, Canada K1A 0R6, and Channing Laboratory, HarVard Medical School, Boston, Massachusetts 02115
  Methods: 13C NMR, 1H NMR, NMR-2D, enzymatic hydrolysis
  
   
  
  Streptococcus pneumoniae B III
  CSDB ID 1658 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_130646,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136095,IEDB_136794,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142344,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_149139,IEDB_149142,IEDB_149174,IEDB_150933,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_423120,IEDB_983931,SB_115,SB_116,SB_131,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_187,SB_192,SB_195,SB_30,SB_39,SB_68,SB_7,SB_84,SB_88

• Article ID: 22
  Brisson J, Uhrinova S, Woods RJ, van der Zwan M, Jarrel HC, Paoletti LC, Kasper DL, Jennings HJ "NMR and molecular dynamics studies of the conformational epitope of the type III group B Streptococcus capsular polysaccharide and derivatives" - Biochemistry 36(11) (1997) 3278-3292
  

  The conformational epitope of the type III group B Streptococcus capsular polysaccharide (GBSP III) exhibits unique properties which can be ascribed to the presence of sialic acid in its structure and the requirement for an extended binding site. By means of NMR and molecular dynamics studies on GBSP III and its fragments, the extended epitope of GBSP III was further defined. The influence of sialic acid on the conformational properties of GBSP III was examined by performing conformational analysis on desialylated GBSP III, which is identical to the polysaccharide of Streptococcus pneumoniae type 14, and also on oxidized and reduced GBSP III. Conformational changes were gauged by 1H and 13C chemical shift analysis, NOE, 1D selective TOCSY-NOESY experiments, J(HH) and J(CH) variations, and NOE of OH resonances. Changes in mobility were examined by 13C T1 and T2 measurements. Unrestrained molecular dynamics simulations with explicit water using the AMBER force field and the GLYCAM parameter set were used to assess static and dynamic conformational models, simulate the observable NMR parameters and calculate helical parameters. GBSP III was found to be capable of forming extended helices. Hence, the length dependence of the conformational epitope could be explained by its location on extended helices within the random coil structure of GBSP III. The interaction of sialic acid with the backbone of the PS was also found to be important in defining the conformational epitope of GBSP III

  NMR, capsular, polysaccharide, Streptococcus, capsular polysaccharide, group, molecular, epitope, type, conformational, dynamics, group B Streptococcus, molecular dynamics, NMR spectroscopy, type III group B streptococcus

  NCBI PubMed ID: 9116006
  Publication DOI: 10.1021/bi961819l
  Journal NLM ID: 0370623
  Publisher: American Chemical Society
  Institutions: Institute for Biological Sciences, National Research Council of Canada, Ottawa, Canada K1A 0R6, and Channing Laboratory, HarVard Medical School, Boston, Massachusetts 02115
  Methods: 13C NMR, 1H NMR, NMR-2D, enzymatic hydrolysis
  
   
  
  Streptococcus pneumoniae B III
  CSDB ID 1798 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_1083493,IEDB_1083495,IEDB_130646,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136095,IEDB_136794,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142344,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_146100,IEDB_146107,IEDB_146664,IEDB_149138,IEDB_149139,IEDB_149141,IEDB_149142,IEDB_149143,IEDB_149144,IEDB_149145,IEDB_149147,IEDB_149148,IEDB_149174,IEDB_150933,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_423120,IEDB_983931,SB_115,SB_116,SB_131,SB_145,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_187,SB_192,SB_195,SB_30,SB_39,SB_6,SB_68,SB_7,SB_84,SB_88

• Article ID: 22
  Brisson J, Uhrinova S, Woods RJ, van der Zwan M, Jarrel HC, Paoletti LC, Kasper DL, Jennings HJ "NMR and molecular dynamics studies of the conformational epitope of the type III group B Streptococcus capsular polysaccharide and derivatives" - Biochemistry 36(11) (1997) 3278-3292
  

  The conformational epitope of the type III group B Streptococcus capsular polysaccharide (GBSP III) exhibits unique properties which can be ascribed to the presence of sialic acid in its structure and the requirement for an extended binding site. By means of NMR and molecular dynamics studies on GBSP III and its fragments, the extended epitope of GBSP III was further defined. The influence of sialic acid on the conformational properties of GBSP III was examined by performing conformational analysis on desialylated GBSP III, which is identical to the polysaccharide of Streptococcus pneumoniae type 14, and also on oxidized and reduced GBSP III. Conformational changes were gauged by 1H and 13C chemical shift analysis, NOE, 1D selective TOCSY-NOESY experiments, J(HH) and J(CH) variations, and NOE of OH resonances. Changes in mobility were examined by 13C T1 and T2 measurements. Unrestrained molecular dynamics simulations with explicit water using the AMBER force field and the GLYCAM parameter set were used to assess static and dynamic conformational models, simulate the observable NMR parameters and calculate helical parameters. GBSP III was found to be capable of forming extended helices. Hence, the length dependence of the conformational epitope could be explained by its location on extended helices within the random coil structure of GBSP III. The interaction of sialic acid with the backbone of the PS was also found to be important in defining the conformational epitope of GBSP III

  NMR, capsular, polysaccharide, Streptococcus, capsular polysaccharide, group, molecular, epitope, type, conformational, dynamics, group B Streptococcus, molecular dynamics, NMR spectroscopy, type III group B streptococcus

  NCBI PubMed ID: 9116006
  Publication DOI: 10.1021/bi961819l
  Journal NLM ID: 0370623
  Publisher: American Chemical Society
  Institutions: Institute for Biological Sciences, National Research Council of Canada, Ottawa, Canada K1A 0R6, and Channing Laboratory, HarVard Medical School, Boston, Massachusetts 02115
  Methods: 13C NMR, 1H NMR, NMR-2D, enzymatic hydrolysis
  
   
  
  Streptococcus pneumoniae B III
  CSDB ID 1800 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_1083495,IEDB_130646,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136095,IEDB_136794,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142344,IEDB_142487,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_149138,IEDB_149139,IEDB_149142,IEDB_149143,IEDB_149147,IEDB_149174,IEDB_150933,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_423120,IEDB_983931,SB_115,SB_116,SB_131,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_187,SB_192,SB_195,SB_30,SB_39,SB_6,SB_68,SB_7,SB_84,SB_88

• Article ID: 22
  Brisson J, Uhrinova S, Woods RJ, van der Zwan M, Jarrel HC, Paoletti LC, Kasper DL, Jennings HJ "NMR and molecular dynamics studies of the conformational epitope of the type III group B Streptococcus capsular polysaccharide and derivatives" - Biochemistry 36(11) (1997) 3278-3292
  

  The conformational epitope of the type III group B Streptococcus capsular polysaccharide (GBSP III) exhibits unique properties which can be ascribed to the presence of sialic acid in its structure and the requirement for an extended binding site. By means of NMR and molecular dynamics studies on GBSP III and its fragments, the extended epitope of GBSP III was further defined. The influence of sialic acid on the conformational properties of GBSP III was examined by performing conformational analysis on desialylated GBSP III, which is identical to the polysaccharide of Streptococcus pneumoniae type 14, and also on oxidized and reduced GBSP III. Conformational changes were gauged by 1H and 13C chemical shift analysis, NOE, 1D selective TOCSY-NOESY experiments, J(HH) and J(CH) variations, and NOE of OH resonances. Changes in mobility were examined by 13C T1 and T2 measurements. Unrestrained molecular dynamics simulations with explicit water using the AMBER force field and the GLYCAM parameter set were used to assess static and dynamic conformational models, simulate the observable NMR parameters and calculate helical parameters. GBSP III was found to be capable of forming extended helices. Hence, the length dependence of the conformational epitope could be explained by its location on extended helices within the random coil structure of GBSP III. The interaction of sialic acid with the backbone of the PS was also found to be important in defining the conformational epitope of GBSP III

  NMR, capsular, polysaccharide, Streptococcus, capsular polysaccharide, group, molecular, epitope, type, conformational, dynamics, group B Streptococcus, molecular dynamics, NMR spectroscopy, type III group B streptococcus

  NCBI PubMed ID: 9116006
  Publication DOI: 10.1021/bi961819l
  Journal NLM ID: 0370623
  Publisher: American Chemical Society
  Institutions: Institute for Biological Sciences, National Research Council of Canada, Ottawa, Canada K1A 0R6, and Channing Laboratory, HarVard Medical School, Boston, Massachusetts 02115
  Methods: 13C NMR, 1H NMR, NMR-2D, enzymatic hydrolysis
  
   
  
  Streptococcus pneumoniae B III
  CSDB ID 1801 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_1083495,IEDB_130646,IEDB_135813,IEDB_136044,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_149138,IEDB_149143,IEDB_149174,IEDB_150933,IEDB_151531,IEDB_190606,IEDB_423120,IEDB_983931,SB_115,SB_116,SB_131,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_192,SB_195,SB_30,SB_39,SB_6,SB_68,SB_7,SB_84,SB_88

• Article ID: 22
  Brisson J, Uhrinova S, Woods RJ, van der Zwan M, Jarrel HC, Paoletti LC, Kasper DL, Jennings HJ "NMR and molecular dynamics studies of the conformational epitope of the type III group B Streptococcus capsular polysaccharide and derivatives" - Biochemistry 36(11) (1997) 3278-3292
  

  The conformational epitope of the type III group B Streptococcus capsular polysaccharide (GBSP III) exhibits unique properties which can be ascribed to the presence of sialic acid in its structure and the requirement for an extended binding site. By means of NMR and molecular dynamics studies on GBSP III and its fragments, the extended epitope of GBSP III was further defined. The influence of sialic acid on the conformational properties of GBSP III was examined by performing conformational analysis on desialylated GBSP III, which is identical to the polysaccharide of Streptococcus pneumoniae type 14, and also on oxidized and reduced GBSP III. Conformational changes were gauged by 1H and 13C chemical shift analysis, NOE, 1D selective TOCSY-NOESY experiments, J(HH) and J(CH) variations, and NOE of OH resonances. Changes in mobility were examined by 13C T1 and T2 measurements. Unrestrained molecular dynamics simulations with explicit water using the AMBER force field and the GLYCAM parameter set were used to assess static and dynamic conformational models, simulate the observable NMR parameters and calculate helical parameters. GBSP III was found to be capable of forming extended helices. Hence, the length dependence of the conformational epitope could be explained by its location on extended helices within the random coil structure of GBSP III. The interaction of sialic acid with the backbone of the PS was also found to be important in defining the conformational epitope of GBSP III

  NMR, capsular, polysaccharide, Streptococcus, capsular polysaccharide, group, molecular, epitope, type, conformational, dynamics, group B Streptococcus, molecular dynamics, NMR spectroscopy, type III group B streptococcus

  NCBI PubMed ID: 9116006
  Publication DOI: 10.1021/bi961819l
  Journal NLM ID: 0370623
  Publisher: American Chemical Society
  Institutions: Institute for Biological Sciences, National Research Council of Canada, Ottawa, Canada K1A 0R6, and Channing Laboratory, HarVard Medical School, Boston, Massachusetts 02115
  Methods: 13C NMR, 1H NMR, NMR-2D, enzymatic hydrolysis
  
   
  
  Streptococcus pneumoniae B III
  CSDB ID 1803 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_1083495,IEDB_130646,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142344,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_144998,IEDB_146100,IEDB_146664,IEDB_149138,IEDB_149139,IEDB_149141,IEDB_149142,IEDB_149143,IEDB_149144,IEDB_149145,IEDB_149147,IEDB_149174,IEDB_150933,IEDB_151531,IEDB_190606,IEDB_423120,IEDB_983931,SB_115,SB_116,SB_131,SB_145,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_187,SB_192,SB_195,SB_30,SB_39,SB_6,SB_68,SB_7,SB_84,SB_88

• Article ID: 40
  Demchenko A, Boons GJ "A highly convergent synthesis of a hexasaccharide derived from the oligosaccharide of group B type III Streptococcus" - Tetrahedron Letters 38(9) (1997) 1629-1632
  

  We have developed a novel glycosylation strategy which enabled a highly convergent assembly of a hexasaccharide derived from group B type I11 Streptococcus

  synthesis, oligosaccharide, hexasaccharide, Streptococcus, group, type

  Journal NLM ID: 2984819R
  Publisher: Elsevier
  Institutions: School of Chemistry, The University of Birmingham, Edgbaston, Birmingham B15 2TT
  
   
  
  Streptococcus sp. B III
  CSDB ID 2005 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: poly[N-(acryloyloxy)succinimide]
Contained glycoepitopes: IEDB_1083495,IEDB_130646,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142344,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_149138,IEDB_149139,IEDB_149141,IEDB_149142,IEDB_149143,IEDB_149144,IEDB_149145,IEDB_149147,IEDB_149174,IEDB_150933,IEDB_151531,IEDB_190606,IEDB_423120,IEDB_983931,SB_115,SB_116,SB_131,SB_145,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_187,SB_192,SB_195,SB_30,SB_39,SB_6,SB_68,SB_7,SB_84,SB_88

• Article ID: 41
  Demchenko AV, Boons GJ "A highly convergent synthesis of a complex oligosaccharide derived from group B type III Streptococcus" - Journal of Organic Chemistry 66(8) (2001) 2547-2554
  

  An efficient synthesis of a heptasaccharide derived from group B type III Streptococcus carrying an artificial spacer (1) is described. Rapid assembly of a protected heptasaccharide (16a) is accomplished from readily available building blocks 2-5 without a single protecting group manipulation between glycosylation steps. The synthetic strategy may be applied to the assembly of other branched complex oligosaccharides. The deprotected heptasaccharide 1 was coupled to a poly[N-(acryloyloxy)succinimide, and the resulting material will be used for the development of an ELISA assay to detect antibodies against GBS, type III in pregnant women

  synthesis, oligosaccharide, Streptococcus, group, type, complex

  NCBI PubMed ID: 11304169
  Journal NLM ID: 2985193R
  Publisher: Columbus, OH: American Chemical Society
  Institutions: Complex Carbohydrate Research Center, University of Georgia, 220 Riverbend Road, Athens, GA 30602, USA
  
   
  
  Streptococcus sp. B III
  CSDB ID 2006 (all data & tools)

Show legend Show as text

Structure type: polymer chemical repeating unit ; n=100-300
Compound class: CPS
Contained glycoepitopes: IEDB_1083493,IEDB_1083495,IEDB_130646,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_1392542,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142344,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_143634,IEDB_146100,IEDB_146107,IEDB_146664,IEDB_149138,IEDB_149139,IEDB_149141,IEDB_149142,IEDB_149143,IEDB_149144,IEDB_149145,IEDB_149147,IEDB_149148,IEDB_149150,IEDB_149151,IEDB_149174,IEDB_150933,IEDB_151531,IEDB_161524,IEDB_190606,IEDB_423120,IEDB_983931,SB_115,SB_116,SB_131,SB_145,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_187,SB_192,SB_195,SB_30,SB_39,SB_6,SB_68,SB_7,SB_84,SB_88

• Article ID: 43
  Deng LY, Kasper DL, Krick TP, Wessels MR "Characterization of the linkage between the type III capsular polysaccharide and the bacterial cell wall of group B Streptococcus" - Journal of Biological Chemistry 275(11) (2000) 7497-7504
  

  The capsular polysaccharide of group B Streptococcus is a key virulence factor and an important target for protective immune responses. Until now, the nature of the attachment between the capsular polysaccharide and the bacterial cell has been poorly defined. We isolated insoluble cell wall fragments from lysates of type III group B Streptococcus and showed that the complexes contained both capsular polysaccharide and group B carbohydrate covalently bound to peptidoglycan. Treatment with the endo-N-acetylmuramidase mutanolysin released soluble complexes of capsular polysaccharide linked to group B carbohydrate by peptidoglycan fragments. Capsular polysaccharide could be enzymatically cleaved from group B carbohydrate by treatment of the soluble complexes with β-N-acetylglucosaminidase, which catalyzes hydrolysis of the β-D-GlcNAc(1→4)β-D-MurNAc subunit produced by mutanolysin digestion of peptidoglycan. Evidence from gas chromatography/mass spectrometry and (31)P NMR analysis of the separated polysaccharides supports a model of the group B Streptococcus cell surface in which the group B carbohydrate and the capsular polysaccharide are independently linked to the glycan backbone of cell wall peptidoglycan; group B carbohydrate is linked to N-acetylmuramic acid, and capsular polysaccharide is linked via a phosphodiester bond and an oligosaccharide linker to N-acetylglucosamine

  polysaccharide, Streptococcus, capsular polysaccharide, type, group B Streptococcus, cell wall, linkage

  NCBI PubMed ID: 10713053
  Publication DOI: 10.1074/jbc.275.11.7497
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: mwessels@channing.harvard.edu
  Institutions: Channing Laboratory, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115, USA
  Methods: enzymatic degradation
  
   
  
  Streptococcus sp. B III
  CSDB ID 2008 (all data & tools)
• Article ID: 6200
  Au MB, Haserick JR, Chen Y, Gibson FC, Deng LL "Structural Identification of Lipid-α: A Glycosyl Lipid Involved in Oligo- And Polysaccharides Metabolism in Streptococcus agalactiae (Group B Streptococcus)" - Current Microbiology 80(1) (2023) 16
  

  Streptococcus agalactiae (group B Streptococcus, GBS) is a gram-positive bacterium that is an asymptomatic colonizer commonly found in the gastrointestinal and genitourinary tract of healthy adults. GBS is also the most common cause of life-threatening bacterial infections in newborns and is emerging as a pathogen in immunocompromised and diabetic adults. The GBS cell wall and covalently linked capsular polysaccharides (CPS) are vital to the protection of the bacterial cell and act as virulence factors. GBS-CPS have been successfully used to produce conjugate vaccines for all currently identified GBS serotypes. However, the mechanisms of biosynthesis and assembly of CPS and the other cell wall components remain poorly defined due to their complex surface structures. In this biosynthetic study of the GBS cell wall-CPS complex, glycolipids with varying lengths of glycosyl-chains were discovered. Among those, one of the smallest glycolipids (named GBS Lipid-α) was structurally characterized. Lipid-α is involved in GBS saccharide metabolism and presumably acts as a glycosyl acceptor to elongate the glycosyl chain. GBS Lipid-α was determined to be a 3-monosaccharide 1,2 acyl glycerol with a molecular mass in the range of m/z = 724-808. GBS Lipid-α is highly heterogenic with various acyl groups and glycosyl moieties. This knowledge will pave the way for future studies to elucidate the entire metabolic pathway and genes involved. The Lipid-α pathway may also exist in other bacterial species and has the potential to be a biomarker for future drug development.

  lipid A, group B Streptococcus, Streptococcus agalactiae, capsular polysaccharides (CPS)

  NCBI PubMed ID: 36459236
  Publication DOI: 10.1007/s00284-022-03117-8
  Journal NLM ID: 7808448
  Publisher: Springer International
  Correspondence: lynndeng@bu.edu
  Institutions: Department of Medicine, Boston University School of Medicine, Boston, MA, USA, Glyde Bio, Inc., Cambridge, MA, USA, Teva Pharmaceuticals, Weston, FL, USA, Department of Oral Biology, College of Dentistry, University of Florida, Gainesville, FL, USA, Channing Laboratory, Harvard Medical School, Brigham and Women's Hospital, Boston, MA, USA
  Methods: methylation, GC-MS, sugar analysis, TLC, ESI-MS, MS/MS, MALDI-TOF MS, radiolabeling, HPIC
  
   
  
  Streptococcus agalactiae B III
  CSDB ID 8431 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_130646,IEDB_130650,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_137779,IEDB_138949,IEDB_139428,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_149174,IEDB_150933,IEDB_151531,IEDB_190606,IEDB_2189046,IEDB_2189047,IEDB_423120,IEDB_983931,SB_115,SB_116,SB_131,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_187,SB_192,SB_195,SB_30,SB_39,SB_68,SB_7,SB_84,SB_88

• Article ID: 75
  Filiatrault MJ, Gibson BW, Schilling B, Sun SH, Munson RS, Campagnari AA "Construction and characterization of Haemophilus ducreyi lipooligosaccharide (LOS) mutants defective in expression of heptosyltransferase III and b1,4-glucosyltransferase: Identification of LOS glycoforms containing lactosamine repeats" - Infection and Immunity 68(6) (2000) 3352-3361
  

  To begin to understand the role of the lipooligosaccharide (LOS) molecule in chancroid infections, we constructed mutants defective in expression of glycosyltransferase genes. Pyocin lysis and immunoscreening was used to identify a LOS mutant of Haemophilus ducreyi 35000. This mutant, HD35000R, produced a LOS molecule that lacked the monoclonal antibody 3F11 epitope and migrated with an increased mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Structural studies indicated that the principal LOS glycoform contains lipid A, Kdo, and two of the three core heptose residues. HD35000R was transformed with a plasmid library of H. ducreyi 35000 DNA, and a clone producing the wild-type LOS was identified. Sequence analysis of the plasmid insert revealed one open reading frame (ORF) that encodes a protein with homology to the WaaQ (heptosyltransferase III) of Escherichia coli. A second ORF had homology to the LgtF (glucosyltransferase) of Neisseria meningitidis. Individual isogenic mutants lacking expression of the putative H. ducreyi heptosyltransferase III, the putative glucosyltransferase, and both glycosyltransferases were constructed and characterized. Each mutant was complemented with the representative wild-type genes in trans to restore expression of parental LOS and confirm the function of each enzyme. Matrix-assisted laser desorption ionization mass spectrometry and SDS-PAGE analysis identified several unique LOS glycoforms containing di-, tri-, and poly-N-acetyllactosamine repeats added to the terminal region of the main LOS branch synthesized by the heptosyltransferase III mutant. These novel H. ducreyi mutants provide important tools for studying the regulation of LOS assembly and biosynthesis

  Haemophilus, Haemophilus ducreyi, Lipooligosaccharide, expression, LOS, characterization, identification, mutant, mutants, construction, heptosyltransferase, lactosamine

  NCBI PubMed ID: 10816485
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Correspondence: AAC@acsu.buffalo.edu
  Institutions: Department of Microbiology, Department of Medicine, Division of Infectious Diseases, and Center for Microbial Pathogenesis, University at Buffalo, Buffalo, New York 14214, Department of Pharmaceutical Chemistry, University of California, San Francisco, CA, USA3, and Children's Research Institute4 and Department of Molecular Virology, Immunology, and Medical Genetics,5 Ohio State University, Columbus, Ohio 43205-2696
  
   
  
  Haemophilus ducreyi 35000WT
  CSDB ID 2067 (all data & tools)
• Article ID: 398
  Tullius MV, Phillips NJ, Scheffler NK, Samuels NM, Munson JR, Hansen EJ, Stevens-Riley M, Campagnari AA, Gibson BW "The lbgAB gene cluster of Haemophilus ducreyi encodes a b-1,4-galactosyltransferase and an a-1,6-DD-heptosyltransferase involved in lipooligosaccharide biosynthesis" - Infection and Immunity 70(6) (2002) 2853-2861
  

  All Haemophilus ducreyi strains examined contain a lipooligosaccharide (LOS) consisting of a single but variable branch oligosaccharide that emanates off the first heptose (Hep-I) of a conserved Hep(3)-phosphorylated 3-deoxy-D-manno-octulosonic acid-lipid A core. In a previous report, identification of tandem genes, lbgA and lbgB, that are involved in LOS biosynthesis was described (Stevens et al., Infect. Immun. 65:651-660, 1997). In a separate study, the same gene cluster was identified and the lbgB (losB) gene was found to be required for transfer of the second sugar, D-glycero-D-manno-heptose (DD-Hep), of the major branch structure (Gibson et al., J. Bacteriol. 179:5062-5071, 1997). In this study, we identified the function of the neighboring upstream gene, lbgA, and found that it is necessary for addition of the third sugar in the dominant oligosaccharide branch, a galactose-linked β1→4, to the DD-Hep. LOS from an lbgA mutant and an lbgAB double mutant were isolated and were characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, carbohydrate analysis, mass spectrometry, and nuclear magnetic resonance spectroscopy. The results showed that the mutant strains synthesize truncated LOS glycoforms that terminate after addition of the first glucose (lbgAB) or the disaccharide DDHep α1→6 Glcβ1 (lbgA) that is attached to the heptose core. Both mutants show a significant reduction in the ability to adhere to human keratinocytes. Although minor differences were observed after two-dimensional gel electrophoresis of total proteins from the wild-type and mutant strains, the expression levels of the vast majority of proteins were unchanged, suggesting that the differences in adherence and invasion are due to differences in LOS. These studies add to the mounting evidence for a role of full-length LOS structures in the pathophysiology of H. ducreyi infection.

  Haemophilus, lipopolysaccharides, Haemophilus ducreyi, Molecular Sequence Data, gene cluster, glycosyltransferases, Magnetic Resonance Spectroscopy, Bacterial Adhesion, Keratinocytes

  NCBI PubMed ID: 12010972
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Correspondence: bgibson@buckinstitute.org
  Institutions: Department of Pharmaceutical Chemistry, University of California, San Francisco, CA, USA, Children's Research Institute and The Ohio State University, Columbus, Ohio 43205-26962, Southwestern Medical Center, University of Texas, Dallas, Texas 75235-90483, State University of New York, Buffalo, New York 142144, and Buck Institute for Age Research, Novato, California 949455
  Methods: NMR, MS, composition analysis, genetic methods, linkage analysis
  
   
  
  Haemophilus ducreyi 35000
  CSDB ID 8388 (all data & tools)
• Article ID: 1175
  Schilling B, Gibson BW, Filiatrault M, Campagnari AA "Characterization of lipooligosaccharides from Haemophilus ducreyi containing polylactosamine repeats" - Journal of the American Society for Mass Spectrometry 13(6) (2002) 724-734
  

  Haemophilus ducreyi, a gram-negative human mucosal pathogen, is one of the principal causes of genital ulcer disease. The lipooligosaccharides (LOS) of these bacteria are considered to be a major virulence factor and have been implicated in the adherence and invasion of H. ducreyi to several human cell types. An isogenic heptosyltransferase-III knockout strain (waaQ) was recently constructed from H. ducreyi 35000 wild-type strain and immunochemical and molecular weight data of the isolated LOS suggested the presence of poly-N-acetyllactosamine (LacNAc) (Filiatrault et al., Infect. Immun. 2000, 68, 3352-3361). In this present study, the structures of these novel LOS-glycoforms were characterized by matrix-assisted laser desorption/ionization (MALDI) and electrospray ionization (ESI) mass spectrometry in combination with exoglycosidase digestion. Detailed structural information was obtained for the oligosaccharide (OS) portions of these LOS showing between one to five linear LacNAc repeats on the non-reducing terminus of the main oligosaccharide branch. When grown on solid media, the organism produced LacNAc repeats that were further modified by the addition of sialic acid. Enzymatic digestion with β-galactosidase, β-N- acetylhexosaminidase, and neuraminidase type VI-A yielded truncated glycoforms consistent with a polyLacNAc structure capped at various end points with sialic acid. ESI-MS/MS mass spectrometry on a quadrupole time-of-flight instrument was particularly effective in obtaining detailed structural information on the least abundant, high-mass glycoforms. Although LOS containing terminal di-LacNAc have been reported, this is the first time to our knowledge that a linear polyLacNAc structure has been characterized in bacteria

  Lipopolysaccharide, Haemophilus, lipopolysaccharides, oligosaccharide, structure, Haemophilus ducreyi, Lipooligosaccharide, blotting, chemistry, disease, human, LOS, strain, structural, Support, terminal, virulence, characterization, cell, molecular, Research, solid, adherence, acid, type, factor, wild type, bacteria, electrospray, hydrolysis, spectrometry, sugar, lactosamine, mass spectrometry, enzymatic, modified, ionization, sialic acid, MALDI, immunochemical, lipooligosaccharides, Gram-negative, pathogen, sugars, nonreducing, time, Western, amino, linear, culture, isogenic, virulence factor, U.S.Gov't, molecular weight, Matrix-Assisted Laser Desorption-Ionization, glycoside, amino sugar, terminus, United States, electrophoresis, Mass, Electrospray Ionization, medium, electrospray-ionization, P.H.S., LacNAc, amino sugars, Culture Media, desorption/ionization, Polyacrylamide Gel, genital, Glycoside Hydrolases, hydrolase, invasion, laser desorption/ionization, matrix-assisted, matrix-assisted laser, mucosal, neuraminidase, ulcer

  NCBI PubMed ID: 12056572
  Journal NLM ID: 9010412
  Publisher: Elsevier
  Correspondence: bgidson@Buckistitute.org
  Institutions: Buck Institute for Age Research, Novato, California 94945, USA
  Methods: NMR
  
   
  
  Haemophilus ducreyi 3500
  CSDB ID 4616 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130646,IEDB_130650,IEDB_130659,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_144998,IEDB_146100,IEDB_146664,IEDB_149144,IEDB_149174,IEDB_150933,IEDB_151531,IEDB_175430,IEDB_190606,IEDB_2189047,IEDB_226300,IEDB_418761,IEDB_418762,IEDB_418763,IEDB_418764,IEDB_418765,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_419430,IEDB_423120,IEDB_983931,SB_115,SB_116,SB_131,SB_145,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_187,SB_192,SB_195,SB_30,SB_39,SB_6,SB_68,SB_7,SB_84,SB_88

• Article ID: 121
  Tsai CM, Kao G, Zhu P "Influence of the length of the lipooligosaccharide a chain on its sialylation in Neisseria meningitidis" - Infection and Immunity 70(1) (2002) 407-411
  

  The sialylation of lipooligosaccharide (LOS) in Neisseria meningitidis plays a role in the resistance of the organism to killing by normal human serum. The length of the alpha chain extending out from the heptose I [Hep (I)] moiety of LOS influenced sialylation of N. meningitidis LOS in vitro and in vivo. The alpha chain required a terminal Gal and a trisaccharide or longer oligosaccharide to serve as an acceptor for sialylation. The disaccharide lactose (Galβ1-4Glc) in the alpha chain of immunotype L8 LOS could not function as an acceptor for the sialyltransferase, probably due to steric hindrance imposed by the neighboring Hep (II) with phosphorylethanolamine and another group attached.

  Lipooligosaccharide, Neisseria meningitidis, sialyltransferase, structure-activity relationship, Substrate Specificity

  NCBI PubMed ID: 11748209
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Correspondence: tsai@cber.fda.gov
  Institutions: Division of Bacterial, Parasitic, and Allergenic Products, Center for Biologics, Food and Drug Administration, Bethesda, MD, USA
  Methods: SDS-PAGE
  
   
  
  Neisseria meningitidis M986-NCV
  CSDB ID 5234 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130646,IEDB_130650,IEDB_130659,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_144998,IEDB_146100,IEDB_146664,IEDB_149144,IEDB_149174,IEDB_150933,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_226300,IEDB_418762,IEDB_418764,IEDB_418767,IEDB_418769,IEDB_419429,IEDB_419430,IEDB_423120,IEDB_983931,SB_115,SB_116,SB_131,SB_145,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_187,SB_192,SB_195,SB_30,SB_39,SB_6,SB_68,SB_7,SB_84,SB_88

• Article ID: 120
  Tsai C, Chen WH, Balakonis PA "Characterization of terminal NeuNAca2-3Galb1-4GlcNAc sequence in lipooligosaccharide of Neisseria meningitidis" - Glycobiology 8(4) (1998) 359-365
  

  Group B and C Neisseria meningitidis are the major cause of meningococcal disease in the United States and in Europe. N . meningitidis lipooligosaccharide (LOS), a major surface antigen, can be divided into 12 immunotypes of which L1 through L8 were found among Group B and C organisms. Groups B and C but not Group A may sialylate their LOSs with N-acetylneuraminic acid (NeuNAc) at the nonreducing end because they synthesize CMP-NeuNAc. Using sialic acid-galactose binding lectins as probes in an ELISA format, six of the eight LOS immunotypes (L2, L3, L4, L5, L7, and L8) in Groups B and C bound specifically to Maackia amurensis leukoagglutinin (MAL), which recognizes NeuNAcα2-3Galβ1-4GlcNAc/Glc sequence, but not to Sambucus nigra agglutinin, which binds NeuNAcα2-6Gal sequence. The combination of SDS-PAGE and MAL-blot analyses revealed that these six LOSs contained only the NeuNAcα2-3Galβ1-4GlcNAc trisaccharide sequence in their 4.1 kDa LOS components, which have a common terminal lacto-N-neotetraose (LNnT, Galβ1-4GlcNAcβ1-3Galβ1-4Glc) structure when nonsialylated as shown by previous studies. The LOS-lectin binding was abolished when the LOSs were treated with Newcastle disease viral neuraminidase which cleaves α2→3 linked sialic acid. Methylation analysis of a representative LOS (L2) confirmed that NeuNAc is 2→3 linked to Gal. Thus, these LOSs structurally mimic certain glycolipids, i.e., paragloboside (LNnT-ceramide) and sialylparagloboside and some glycoproteins in having LNnT and N-acetyllactosamine sequences, respectively, with or without α2→3 linked NeuNAc. The molecular mimicry of the LOSs may play a role in the pathogenesis of N.meningitidis by assisting the organism to evade host immune defenses in man.

  LPS, structure, core, Lipooligosaccharide, Neisseria meningitidis, Neisseria, terminal, characterization, neuraminic acid, lactosamine, sequence

  NCBI PubMed ID: 9499383
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Institutions: Division of Bacterial Products, Center for Biologics Evaluation and Research, FDA, Bethesda, MD, USA.
  Methods: methylation, ELISA
  
   
  
  Neisseria meningitidis
  CSDB ID 5394 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130646,IEDB_130650,IEDB_130659,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_149144,IEDB_149174,IEDB_150933,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_226300,IEDB_418762,IEDB_418764,IEDB_418767,IEDB_418769,IEDB_419429,IEDB_423120,IEDB_983931,SB_115,SB_116,SB_131,SB_145,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_187,SB_192,SB_195,SB_30,SB_39,SB_6,SB_68,SB_7,SB_84,SB_88

• Article ID: 120
  Tsai C, Chen WH, Balakonis PA "Characterization of terminal NeuNAca2-3Galb1-4GlcNAc sequence in lipooligosaccharide of Neisseria meningitidis" - Glycobiology 8(4) (1998) 359-365
  

  Group B and C Neisseria meningitidis are the major cause of meningococcal disease in the United States and in Europe. N . meningitidis lipooligosaccharide (LOS), a major surface antigen, can be divided into 12 immunotypes of which L1 through L8 were found among Group B and C organisms. Groups B and C but not Group A may sialylate their LOSs with N-acetylneuraminic acid (NeuNAc) at the nonreducing end because they synthesize CMP-NeuNAc. Using sialic acid-galactose binding lectins as probes in an ELISA format, six of the eight LOS immunotypes (L2, L3, L4, L5, L7, and L8) in Groups B and C bound specifically to Maackia amurensis leukoagglutinin (MAL), which recognizes NeuNAcα2-3Galβ1-4GlcNAc/Glc sequence, but not to Sambucus nigra agglutinin, which binds NeuNAcα2-6Gal sequence. The combination of SDS-PAGE and MAL-blot analyses revealed that these six LOSs contained only the NeuNAcα2-3Galβ1-4GlcNAc trisaccharide sequence in their 4.1 kDa LOS components, which have a common terminal lacto-N-neotetraose (LNnT, Galβ1-4GlcNAcβ1-3Galβ1-4Glc) structure when nonsialylated as shown by previous studies. The LOS-lectin binding was abolished when the LOSs were treated with Newcastle disease viral neuraminidase which cleaves α2→3 linked sialic acid. Methylation analysis of a representative LOS (L2) confirmed that NeuNAc is 2→3 linked to Gal. Thus, these LOSs structurally mimic certain glycolipids, i.e., paragloboside (LNnT-ceramide) and sialylparagloboside and some glycoproteins in having LNnT and N-acetyllactosamine sequences, respectively, with or without α2→3 linked NeuNAc. The molecular mimicry of the LOSs may play a role in the pathogenesis of N.meningitidis by assisting the organism to evade host immune defenses in man.

  LPS, structure, core, Lipooligosaccharide, Neisseria meningitidis, Neisseria, terminal, characterization, neuraminic acid, lactosamine, sequence

  NCBI PubMed ID: 9499383
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Institutions: Division of Bacterial Products, Center for Biologics Evaluation and Research, FDA, Bethesda, MD, USA.
  Methods: methylation, ELISA
  
   
  
  Neisseria meningitidis
  CSDB ID 5395 (all data & tools)