Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Trivial name: lipooligosaccharide core L2
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130650,IEDB_130659,IEDB_136044,IEDB_136906,IEDB_137472,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_145003,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_226300,IEDB_418767,IEDB_418769,IEDB_419429,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_6,SB_7,SB_88

• Article ID: 432
  Zhu P, Klutch MJ, Bash MC, Tsang RS, Ng LK, Tsai CM "Genetic diversity of three lgt loci for biosynthesis of lipooligosaccharide (LOS) in Neisseria species" - Microbiology 148(6) (2002) 1833-1844
  

  Lipooligosaccharide (LOS) is a major virulence factor of the pathogenic NEISSERIA: Nine lgt genes at three chromosomal loci (lgt-1, 2, 3) encoding the glycosyltransferases responsible for the biosynthesis of LOS oligosaccharide chains were examined in 26 Neisseria meningitidis, 51 Neisseria gonorrhoeae and 18 commensal Neisseria strains. DNA hybridization, PCR and nucleotide sequence data were compared to previously reported lgt genes. Analysis of the genetic organization of the lgt loci revealed that in N. meningitidis, the lgt-1 and lgt-3 loci were hypervariable genomic regions, whereas the lgt-2 locus was conserved. In N. gonorrhoeae, no variability in the composition or organization of the three lgt loci was observed. lgt genes were detected only in some commensal Neisseria species. The genetic organization of the lgt-1 locus was classified into eight types and the lgt-3 locus was classified into four types. Two types of arrangement at lgt-1 (II and IV) and one type of arrangement at lgt-3 (IV) were novel genetic organizations reported in this study. Based on the three lgt loci, 10 LOS genotypes of N. meningitidis were distinguished. Phylogenetic analysis revealed a gene cluster, lgtH, which separated from the homologous genes lgtB and lgtE. The lgtH and lgtE genes were mutually exclusive and were located at the same position in lgt-1. The data demonstrated that pathogenic and commensal Neisseria share a common lgt gene pool and horizontal gene transfer appears to contribute to the genetic diversity of the lgt loci in Neisseria

  biosynthesis, oligosaccharide structure, Neisseria meningitidis, Neisseria, gene cluster, glycosyltransferases, Gonorrhoeae, Neisseria gonorrhoeae, genetic diversity, lipooligosaccharide (LOS), phylogenetic analysis, virulence factor

  NCBI PubMed ID: 12055303
  Journal NLM ID: 0376646
  Publisher: Washington, DC: Kluwer Academic/Plenum Publishers
  Correspondence: zhu@cber.fda.gov
  Institutions: Division of Bacterial, Parasitic and Allergenic Products and Division of Viral Products, Center for Biologics Evaluation and Research, FDA, 8800 Rockville Pike, Bethesda, MD, USA
  Methods: PCR, DNA sequencing, DNA techniques, genetic methods, RT-PCR
  
   
  
  Neisseria meningitidis 35E
  CSDB ID 8725 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Trivial name: lipooligosaccharide core L5
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130650,IEDB_130659,IEDB_136044,IEDB_136906,IEDB_137472,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_145003,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_226300,IEDB_418767,IEDB_418769,IEDB_419429,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_6,SB_7,SB_88

• Article ID: 432
  Zhu P, Klutch MJ, Bash MC, Tsang RS, Ng LK, Tsai CM "Genetic diversity of three lgt loci for biosynthesis of lipooligosaccharide (LOS) in Neisseria species" - Microbiology 148(6) (2002) 1833-1844
  

  Lipooligosaccharide (LOS) is a major virulence factor of the pathogenic NEISSERIA: Nine lgt genes at three chromosomal loci (lgt-1, 2, 3) encoding the glycosyltransferases responsible for the biosynthesis of LOS oligosaccharide chains were examined in 26 Neisseria meningitidis, 51 Neisseria gonorrhoeae and 18 commensal Neisseria strains. DNA hybridization, PCR and nucleotide sequence data were compared to previously reported lgt genes. Analysis of the genetic organization of the lgt loci revealed that in N. meningitidis, the lgt-1 and lgt-3 loci were hypervariable genomic regions, whereas the lgt-2 locus was conserved. In N. gonorrhoeae, no variability in the composition or organization of the three lgt loci was observed. lgt genes were detected only in some commensal Neisseria species. The genetic organization of the lgt-1 locus was classified into eight types and the lgt-3 locus was classified into four types. Two types of arrangement at lgt-1 (II and IV) and one type of arrangement at lgt-3 (IV) were novel genetic organizations reported in this study. Based on the three lgt loci, 10 LOS genotypes of N. meningitidis were distinguished. Phylogenetic analysis revealed a gene cluster, lgtH, which separated from the homologous genes lgtB and lgtE. The lgtH and lgtE genes were mutually exclusive and were located at the same position in lgt-1. The data demonstrated that pathogenic and commensal Neisseria share a common lgt gene pool and horizontal gene transfer appears to contribute to the genetic diversity of the lgt loci in Neisseria

  biosynthesis, oligosaccharide structure, Neisseria meningitidis, Neisseria, gene cluster, glycosyltransferases, Gonorrhoeae, Neisseria gonorrhoeae, genetic diversity, lipooligosaccharide (LOS), phylogenetic analysis, virulence factor

  NCBI PubMed ID: 12055303
  Journal NLM ID: 0376646
  Publisher: Washington, DC: Kluwer Academic/Plenum Publishers
  Correspondence: zhu@cber.fda.gov
  Institutions: Division of Bacterial, Parasitic and Allergenic Products and Division of Viral Products, Center for Biologics Evaluation and Research, FDA, 8800 Rockville Pike, Bethesda, MD, USA
  Methods: PCR, DNA sequencing, DNA techniques, genetic methods, RT-PCR
  
   
  
  Neisseria meningitidis M981
  CSDB ID 8728 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_136044,IEDB_136906,IEDB_137472,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_145003,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_418765,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_6,SB_7,SB_88

• Article ID: 659
  Griffiss JM, Brandt BL, Saunders NB, Zollinger W "Structural relationships and sialylation among meningococcal L1, L8, and L3,7 lipooligosaccharide serotypes" - Journal of Biological Chemistry 275(13) (2000) 9716-9724
  

  Eighteen of 34 endemic meningococcal case strains were of the L8 lipooligosaccharide (LOS) type; four of these were both L3 and L7 (L3,7), and seven were L1. L1 structures arose by alternative terminal Gal substitutions of lactosyl diheptoside L8 structures, as determined by electrospray ionization and other mass spectrometric techniques, and enzymatic and chemical degradations (Structures L1 and L1a). [see text for structure] The more abundant molecule, designated L1, had a trihexose globosyl alpha chain; the less abundant one, designated L1a, had a β-lactosyl alpha chain and a parallel α-lactosaminyl gamma chain. A P(k) globoside (Gal α1→4 Gal β1→4 Glc-R) monoclonal antibody bound 9/10 L1 strains, but a P(1) globoside (Gal α1→4 Gal β1→4 GlcNAc-R) mAb bound none of them. α-Galactosidase caused loss of both L1 structures and creation of L8 structures; β-galactosidase caused loss of the L8 determinant. The L1/P(k) glycose was partially sialylated. Some LOS also had unsubstituted basal β-GlcNAc additions. These structural relationships explain co-expression of L8, L1, and L3,7 serotypes.

  Lipooligosaccharide, meningococcal, structural, serotype, Serotypes, relationship, sialylation

  NCBI PubMed ID: 10734124
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: crapaud@vacom.ucsf.edu
  Institutions: Centre for Immunochemistry and Department of Laboratory Medicine, University of California, San Francisco, California 94121, Department of Bacterial Diseases, Walter Reed Army Institute of Research, Washington, D. C. 20307
  Methods: dephosphorylation, ESI-MS, MS/MS, enzymatic degradation, LSI-MS
  
   
  
  Neisseria meningitidis L1
  CSDB ID 577 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130646,IEDB_130650,IEDB_130670,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391962,IEDB_140088,IEDB_140108,IEDB_140122,IEDB_140529,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142488,IEDB_143794,IEDB_144998,IEDB_145003,IEDB_146664,IEDB_150899,IEDB_151528,IEDB_151531,IEDB_167070,IEDB_190606,IEDB_2189047,IEDB_226811,IEDB_232584,IEDB_885811,IEDB_983931,SB_137,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_29,SB_30,SB_7,SB_88

• Article ID: 1108
  Phillips NJ, Miller TJ, Engstrom JJ, Melaugh W, McLaughlin R, Apicella MA, Gibson BW "Characterization of chimeric lipopolysaccharides from Escherichia coli strain JM109 transformed with lipooligosaccharide synthesis genes (lsg) from Haemophilus influenzae" - Journal of Biological Chemistry 275(7) (2000) 4747-4758
  

  Previously, we reported the expression of chimeric lipopolysaccharides (LPS) in Escherichia coli strain JM109 (a K-12 strain) transformed with plasmids containing Haemophilus influenzae lipooligosaccharide synthesis genes (lsg) (Abu Kwaik, Y., McLaughlin, R. E., Apicella, M. A., and Spinola, S. M. (1991) Mol. Microbiol. 5, 2475-2480). In this current study, we have analyzed the O-deacylated LPS and free oligosaccharides from three transformants (designated pGEMLOS-4, pGEMLOS-5, and pGEMLOS-7) by matrix-assisted laser desorption ionization, electrospray ionization, and tandem mass spectrometry techniques, along with composition and linkage analyses. These data show that the chimeric LPS consist of the complete E. coli LPS core structure glycosylated on the 7-position of the non-reducing terminal branch heptose with oligosaccharides from H. influenzae. In pGEMLOS-7, the disaccharide Gal 1→3 GlcNAc1→ is added, and in pGEMLOS-5, the structure is extended to Gal 1→4 GlcNAc 1→3 Gal 1→3 GlcNAc1→. PGEMLOS-5 LPS reacts positively with monoclonal antibody 3F11, an antibody that recognizes the terminal disaccharide of lacto-N-neotetraose. In pGEMLOS-4 LPS, the 3F11 epitope is apparently blocked by glycosylation on the 6-position of the terminal Gal with either Gal or GlcNAc. The biosynthesis of these chimeric LPS was found to be dependent on a functional wecA (formerly rfe) gene in E. coli. By using this carbohydrate expression system, we have been able to examine the functions of the lsg genes independent of the effects of other endogenous Haemophilus genes and expressed proteins.

  Lipopolysaccharide, synthesis, Haemophilus, Haemophilus influenzae, lipopolysaccharides, Lipooligosaccharide, gene, strain, characterization, Escherichia, Escherichia coli

  NCBI PubMed ID: 10671507
  Publication DOI: 10.1074/jbc.275.7.4747
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: gibson@socrates.cgl.ucsf.edu
  Institutions: Department of Pharmaceutical Chemistry, University of California, San Francisco, CA, USA, Department of Microbiology, University of Iowa, Iowa City, Iowa 52242, Department of Microbiology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104
  Methods: ESI-MS, MALDI-MS, MS/MS, composition analysis, linkage analysis
  
   
  
  Escherichia coli pGEMLOS-4
  CSDB ID 4175 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130646,IEDB_130650,IEDB_130670,IEDB_130697,IEDB_134624,IEDB_135813,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391962,IEDB_140088,IEDB_140108,IEDB_140122,IEDB_140529,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142488,IEDB_143794,IEDB_144998,IEDB_145003,IEDB_146664,IEDB_150899,IEDB_151528,IEDB_151531,IEDB_153201,IEDB_156493,IEDB_167070,IEDB_190606,IEDB_2189047,IEDB_226811,IEDB_232584,IEDB_742248,IEDB_983931,SB_137,SB_163,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_29,SB_30,SB_7,SB_88

• Article ID: 1108
  Phillips NJ, Miller TJ, Engstrom JJ, Melaugh W, McLaughlin R, Apicella MA, Gibson BW "Characterization of chimeric lipopolysaccharides from Escherichia coli strain JM109 transformed with lipooligosaccharide synthesis genes (lsg) from Haemophilus influenzae" - Journal of Biological Chemistry 275(7) (2000) 4747-4758
  

  Previously, we reported the expression of chimeric lipopolysaccharides (LPS) in Escherichia coli strain JM109 (a K-12 strain) transformed with plasmids containing Haemophilus influenzae lipooligosaccharide synthesis genes (lsg) (Abu Kwaik, Y., McLaughlin, R. E., Apicella, M. A., and Spinola, S. M. (1991) Mol. Microbiol. 5, 2475-2480). In this current study, we have analyzed the O-deacylated LPS and free oligosaccharides from three transformants (designated pGEMLOS-4, pGEMLOS-5, and pGEMLOS-7) by matrix-assisted laser desorption ionization, electrospray ionization, and tandem mass spectrometry techniques, along with composition and linkage analyses. These data show that the chimeric LPS consist of the complete E. coli LPS core structure glycosylated on the 7-position of the non-reducing terminal branch heptose with oligosaccharides from H. influenzae. In pGEMLOS-7, the disaccharide Gal 1→3 GlcNAc1→ is added, and in pGEMLOS-5, the structure is extended to Gal 1→4 GlcNAc 1→3 Gal 1→3 GlcNAc1→. PGEMLOS-5 LPS reacts positively with monoclonal antibody 3F11, an antibody that recognizes the terminal disaccharide of lacto-N-neotetraose. In pGEMLOS-4 LPS, the 3F11 epitope is apparently blocked by glycosylation on the 6-position of the terminal Gal with either Gal or GlcNAc. The biosynthesis of these chimeric LPS was found to be dependent on a functional wecA (formerly rfe) gene in E. coli. By using this carbohydrate expression system, we have been able to examine the functions of the lsg genes independent of the effects of other endogenous Haemophilus genes and expressed proteins.

  Lipopolysaccharide, synthesis, Haemophilus, Haemophilus influenzae, lipopolysaccharides, Lipooligosaccharide, gene, strain, characterization, Escherichia, Escherichia coli

  NCBI PubMed ID: 10671507
  Publication DOI: 10.1074/jbc.275.7.4747
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: gibson@socrates.cgl.ucsf.edu
  Institutions: Department of Pharmaceutical Chemistry, University of California, San Francisco, CA, USA, Department of Microbiology, University of Iowa, Iowa City, Iowa 52242, Department of Microbiology, University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma 73104
  Methods: ESI-MS, MALDI-MS, MS/MS, composition analysis, linkage analysis
  
   
  
  Escherichia coli pGEMLOS-4
  CSDB ID 4176 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130646,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136906,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_145003,IEDB_146664,IEDB_149144,IEDB_151528,IEDB_151531,IEDB_167070,IEDB_190606,IEDB_2189047,IEDB_419428,IEDB_419429,IEDB_983931,SB_145,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_6,SB_7,SB_88

• Article ID: 1132
  Ram S, Cox AD, Wright JC, Vogel U, Getzlaff S, Boden R, Li J, Plested JS, Meri S, Gulati S, Stein DC, Richards JC, Moxon ER, Rice PA "Neisserial lipooligosaccharide is a target for complement component C4b: Inner core phosphoethanolamine residues define C4b linkage specificity" - Journal of Biological Chemistry 278(51) (2003) 50853-50862
  

  We identified Neisseria meningitidis lipooligosaccharide (LOS) as an acceptor for complement component C4b (C4b). Phosphoethanolamine (PEA) residues on the second heptose (HepII) residue in the LOS core structure formed amide linkages with C4b. PEA on the 6-position of HepII (6-PEA) was more efficient than 3-PEA in binding C4b. Strains bearing 6-PEA bound more C4b than strains with 3-PEA and were more susceptible to complement-mediated killing in serum bactericidal assays. Deleting 3-PEA from a strain that expressed both 3- and 6-PEA simultaneously on HepII did not decrease C4b binding. Glycose chain extension of the first heptose residue (HepI) influenced the nature of the C4b-LOS linkage. Predominantly ester C4b-LOS bonds were seen when lacto-N-neotetraose formed the terminus of the glycose chain extension of HepI with 3-PEA on HepII in the LOS core. Related LOS species with more truncated chain extensions from HepI bound C4b via amide linkages to 3-PEA on HepII. However, 6-PEA in the LOS core bound C4b even when the glycose chain from HepI bore lacto-N-neotetraose at the terminus. The C4A isoform exclusively formed amide linkages, while C4B bound meningococci preferentially via ester linkages. These data may serve to explain the preponderance of 3-PEA bearing meningococci among clinical isolates because 6-PEA enhances C4b binding that may facilitate clearance of 6-PEA-bearing strains resulting from enhanced serum killing by the classical pathway of complement

  structure, core, heptose, Lipooligosaccharide, Neisseria meningitidis, clinical, disease, isolate, LOS, meningococci, Neisseria, strain, chain, enhanced, infectious disease, specificity, linkage, inner core, medicine, phosphoethanolamine, Infectious, component, binding, lacto-N-neotetraose, acceptor, pathway, serum, bound, bactericidal, serum killing, species, killing, assay, decrease, terminus, amide, target, classical, clearance, complement, ester, pea

  NCBI PubMed ID: 14525973
  Publication DOI: 10.1074/jbc.M308364200
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: sram@bu.edu
  Institutions: Institute for Biological Sciences, National Research Council, Ottawa, Ontario K1A 0R6, Canada, Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, Maryland 20742, Section of Infectious Diseases, Evans Biomedical Research Center, Boston University Medical Center, Boston, Massachusetts 02118, Molecular Infectious Diseases Group, Oxford University Department of Pediatrics, John Radcliffe Hospital, Oxford OX3 9DU, United Kingdom, nstitute for Hygiene and Microbiology, University of Wuerzburg, 97080 Wuerzburg, Germany, Department of Bacteriology and Immunology, Haartman Institute, University of Helsinki, Helsinki, Finland-00014
  Methods: 1H NMR, ESI-MS, Western blotting
  
   
  
  Neisseria meningitidis MC51, Neisseria meningitidis 2120
  CSDB ID 4422 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130646,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136906,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_145003,IEDB_146664,IEDB_149144,IEDB_151528,IEDB_151531,IEDB_167070,IEDB_190606,IEDB_2189047,IEDB_419429,IEDB_419431,IEDB_983931,SB_145,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_6,SB_7,SB_88

• Article ID: 1132
  Ram S, Cox AD, Wright JC, Vogel U, Getzlaff S, Boden R, Li J, Plested JS, Meri S, Gulati S, Stein DC, Richards JC, Moxon ER, Rice PA "Neisserial lipooligosaccharide is a target for complement component C4b: Inner core phosphoethanolamine residues define C4b linkage specificity" - Journal of Biological Chemistry 278(51) (2003) 50853-50862
  

  We identified Neisseria meningitidis lipooligosaccharide (LOS) as an acceptor for complement component C4b (C4b). Phosphoethanolamine (PEA) residues on the second heptose (HepII) residue in the LOS core structure formed amide linkages with C4b. PEA on the 6-position of HepII (6-PEA) was more efficient than 3-PEA in binding C4b. Strains bearing 6-PEA bound more C4b than strains with 3-PEA and were more susceptible to complement-mediated killing in serum bactericidal assays. Deleting 3-PEA from a strain that expressed both 3- and 6-PEA simultaneously on HepII did not decrease C4b binding. Glycose chain extension of the first heptose residue (HepI) influenced the nature of the C4b-LOS linkage. Predominantly ester C4b-LOS bonds were seen when lacto-N-neotetraose formed the terminus of the glycose chain extension of HepI with 3-PEA on HepII in the LOS core. Related LOS species with more truncated chain extensions from HepI bound C4b via amide linkages to 3-PEA on HepII. However, 6-PEA in the LOS core bound C4b even when the glycose chain from HepI bore lacto-N-neotetraose at the terminus. The C4A isoform exclusively formed amide linkages, while C4B bound meningococci preferentially via ester linkages. These data may serve to explain the preponderance of 3-PEA bearing meningococci among clinical isolates because 6-PEA enhances C4b binding that may facilitate clearance of 6-PEA-bearing strains resulting from enhanced serum killing by the classical pathway of complement

  structure, core, heptose, Lipooligosaccharide, Neisseria meningitidis, clinical, disease, isolate, LOS, meningococci, Neisseria, strain, chain, enhanced, infectious disease, specificity, linkage, inner core, medicine, phosphoethanolamine, Infectious, component, binding, lacto-N-neotetraose, acceptor, pathway, serum, bound, bactericidal, serum killing, species, killing, assay, decrease, terminus, amide, target, classical, clearance, complement, ester, pea

  NCBI PubMed ID: 14525973
  Publication DOI: 10.1074/jbc.M308364200
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: sram@bu.edu
  Institutions: Institute for Biological Sciences, National Research Council, Ottawa, Ontario K1A 0R6, Canada, Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, Maryland 20742, Section of Infectious Diseases, Evans Biomedical Research Center, Boston University Medical Center, Boston, Massachusetts 02118, Molecular Infectious Diseases Group, Oxford University Department of Pediatrics, John Radcliffe Hospital, Oxford OX3 9DU, United Kingdom, nstitute for Hygiene and Microbiology, University of Wuerzburg, 97080 Wuerzburg, Germany, Department of Bacteriology and Immunology, Haartman Institute, University of Helsinki, Helsinki, Finland-00014
  Methods: 1H NMR, ESI-MS, Western blotting
  
   
  
  Neisseria meningitidis 89I
  CSDB ID 4424 (all data & tools)

Show legend Show as text

Structure type: polymer chemical repeating unit
Compound class: EPS
Contained glycoepitopes: IEDB_136044,IEDB_136906,IEDB_137472,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_145003,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_153543,IEDB_190606,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_6,SB_7,SB_88

• Article ID: 1287
  Yamamoto Y, Nunome T, Yamauchi R, Kato K, Sone Y "Structure of an exocellular polysaccharide of Lactobacillus helveticus TN-4, a spontaneous mutant strain of Lactobacillus helveticus TY1-2" - Carbohydrate Research 275(2) (1995) 319-332
  

  Lactobacillus helveticus strain TN-4, a spontaneous mutant strain of Lactobacillus helveticus TY1-2, produced an exocellular polysaccharide from reconstituted skim milk. On the basis of the results of methylation analysis, enzymatic digestion, mild Smith degradation, mild acid hydrolysis, acetolysis, and 1D and 2D 1H NMR spectroscopy, it was concluded that the polysaccharide has a D-galactofuranose containing hexasaccharide repeating unit with the following structure: [formula see text]

  NMR, structure, strain, polysaccharide, exocellular polysaccharide, mutant, Lactobacillus helveticus, lactic acid, milk, Exocellular polysaccharide; Lactobacillus helveticus TN-4; Lactobacillus helveticus TYI-2, Lactobacillus helveticus TN-4, Lactobacillus helveticus TYI-2

  NCBI PubMed ID: 8529226
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: United Graduate School of Agricultural Science, Gifu University, Gifu 501-11, Japan, Takeda Food Products, Ltd., 3 - 20 Imoji, Itami, Hyougo 664, Japan, Faculty of Human Life Science, Osaka City University, Sugimoto-cho, Sumiyoshi-ku, Osaka 558, Japan
  Methods: NMR-2D, methylation, NMR, mild acid hydrolysis, Smith degradation, acetolysis, b-galactosidase digestion
  
   
  
  Lactobacillus helveticus TY1-2
  CSDB ID 6006 (all data & tools)
• Article ID: 3106
  Yamamoto Y, Murosaki S, Yamauchi R, Kato K, Sone Y "Structural study on an exocellular polysaccharide produced by Lactobacillus helveticus TY1-2" - Carbohydrate Research 261 (1994) 67-78
  

  Lactobacillus helveticus TY1-2 produced an exocellular polysaccharide when it was cultured in reconstituted skim milk. This polysaccharide is a high molecular weight heteropolymer of D-glucopyranosyl, D-galactopyranosyl, and 2-acetamido-2-deoxy-D-glucopyranosyl residues in the molar ratio 3.0:2.8:0.9. The primary structure of the polysaccharide was shown by glycose analysis, methylation analysis, Smith degradation, and NMR spectroscopy to be composed of branched heptasaccharide repeating units having the following structure: [formula: see text]

  NCBI PubMed ID: 8087810
  Publication DOI: 10.1016/0008-6215(94)80006-5
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: United Graduate School of Agricultural Science, Gifu University, Japan
  
   
  
  Lactobacillus helveticus TY1-2
  CSDB ID 118066 (all data & tools)
• Article ID: 5791
  Knirel YA, Van Calsteren M "Bacterial exopolysaccharides" - Book: Comprehensive Glycoscience: From Chemistry to Systems Biology. Reference Module in Chemistry, Molecular Sciences and Chemical Engineering (2021) 1-75
  

  Bacterial extracellular polysaccharides are known as a cell-bound capsule, a sheath, or a slime, which is excreted into the environment. They play an important role in virulence of medical bacteria and plant-to-symbiont interaction and are used for serotyping of bacteria and production of vaccines. Some exopolysaccharides have commercial applications in industry, and claims of health benefits have been documented for an increasing number of them. Exopolysaccharides have diverse composition and structure, and some contain sugar and non-sugar components that are found in bacterial carbohydrates only. The present article provides an updated collection of the data on exopolysaccharides of various classes of gram-negative and gram-positive bacteria reported until the end of 2019. When known, biosynthesis pathways of exopolysaccharides are treated in a summary manner. References are made to structure and biosynthesis relatedness between exopolysaccharides of different bacterial taxa as well as between bacterial polysaccharides and mammalian glycosaminoglycans.

  polysaccharide structure, Gram-negative bacteria, capsule, Biofilm, polysaccharide biosynthesis, gram-positive bacteria, Monosaccharide composition, Bacterial exopolysaccharide, non-sugar component

  Publication DOI: 10.1016/B978-0-12-819475-1.00005-5
  Publisher: Elsevier
  Correspondence: marie-rose.vancalsteren@canada.ca; yknirel@gmail.com
  Editors: Barchi J, Kamerling H
  Institutions: N. D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, Saint-Hyacinthe Research and Development Centre, Agriculture and Agri-Food Canada, Saint-Hyacinthe, QC, Canada
  
   
  
  Lactobacillus helveticus TY1-2
  CSDB ID 25049 (all data & tools)
• Article ID: 5880
  De Vuyst L, De Vin F "Exopolysaccharides from Lactic Acid Bacteria" - Book: Comprehensive Glycoscience: From Chemistry to Systems Biology. Reference Module in Chemistry, Molecular Sciences and Chemical Engineering (2007) 477-519
  

  carbohydrates, polysaccharides, Lactic acid bacteria, exopolysaccharides, glycolipids, glycoproteins, Glycomics

  Publication DOI: 10.1016/B978-044451967-2/00129-X
  Publisher: Elsevier
  Correspondence: ldvuyst@vub.ac.be
  Editors: Barchi J, Kamerling H
  Institutions: Department of Applied Biological Sciences and Engineering, Research Group of Industrial Microbiology and Food Biotechnology, Vrije Universiteit Brussel, Brussels, Belgium
  
   
  
  Lactobacillus helveticus TY1-2
  CSDB ID 25146 (all data & tools)

Show legend Show as text

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

• Article ID: 2969
  Gmeiner J "The ribitol-phosphate-containing lipopolysaccharide from Proteus mirabilis, strain D52. Investigations of O-specific chains" - European Journal of Biochemistry 74 (1977) 171-180
  

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

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

Show legend Show as text

Structure type: polymer chemical repeating unit
Compound class: EPS
Contained glycoepitopes: IEDB_135813,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_145003,IEDB_146664,IEDB_149139,IEDB_151528,IEDB_151531,IEDB_153543,IEDB_167070,IEDB_190606,IEDB_983931,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_6,SB_7,SB_88

• Article ID: 3405
  Gorska S, Grycko P, Rybka J, Gamian A "Exopolysaccharides of lactic acid bacteria: structure and biosynthesis" - Postȩpy Higieny i Medycyny Doświadczalnej [Polish] 61 (2007) 805-818
  

  The group of lactic acid bacteria (LABs) includes four genera: Lactobacillus, Leuconostoc, Pediococcus, and Streptococcus. The most characteristic feature of this group of microorganisms is the production of lactic acid as a main product of carbohydrate metabolism. LABs are responsible for the fermentation of alimentary products and they also produce a variety of agents, among them exopolysaccharides (EPSs), which inhibit the growth of pathogenic bacteria. In this article on the different types of EPSs produced by LABs, data concerning their structure and biosynthesis are presented

  biosynthesis, structure, Streptococcus, Lactic acid bacteria, exopolysaccharides, Lactococcus, Lactobacillus, Leuconostoc

  NCBI PubMed ID: 18097339
  Journal NLM ID: 0421052
  Publisher: Warszawa: Panstwowy Zaklad Wydawnictw Lekarskich
  Institutions: Laboratorium Mikrobiologii Lekarskiej, Instytut Immunologii i Terapii Doswiadczalnej PAN im. L. Hirszfelda we Wroclawiu
  
   
  
  Lactobacillus helveticus TY 1-2
  CSDB ID 21992 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: 2-aminoethyl-(N-methyl)-hydroxylamine
Trivial name: LPS-typhimurium-conjugate-Sp2
Compound class: LPS
Contained glycoepitopes: IEDB_127517,IEDB_130650,IEDB_130670,IEDB_130693,IEDB_130701,IEDB_135509,IEDB_135513,IEDB_135514,IEDB_135611,IEDB_136093,IEDB_136105,IEDB_136775,IEDB_136906,IEDB_137472,IEDB_137486,IEDB_140088,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144983,IEDB_144998,IEDB_145003,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_190606,IEDB_2189047,IEDB_225177,IEDB_226811,IEDB_885823,IEDB_983930,IEDB_983931,SB_192,SB_44,SB_67,SB_7,SB_72

• Article ID: 3440
  Blixt O, Hoffmann J, Svenson S, Norberg T "Pathogen specific carbohydrate antigen microarrays: a chip for detection of Salmonella O-antigen specific antibodies" - Glycoconjugate Journal 25(1) (2008) 27-36
  

  A Salmonella O-antigen microarray was developed by covalent coupling of oligosaccharide antigens specific for serogroups Salmonella enterica sv. Paratyphi (group A), Typhimurium (group B) and Enteritidis (group D). Antibodies were correctly detected in sera from patients with culture verified salmonellosis. High serogroup-specificity was seen with the disaccharide antigens. With the larger antigens, containing the backbone sequence Manα1-2Rhaα1-2Gal (MRG), common backbone-specific antibodies (O-antigen 12) were also detected. This is 'proof of principle' that pathogen-specific carbohydrate antigen microarrays constitute a novel technology for rapid and specific serological diagnosis in either individual patients or larger sero-epidemiological and vaccine studies.

  oligosaccharide, polysaccharide, antibody, vaccine, salmonellosis, glycanarray

  NCBI PubMed ID: 17558551
  Publication DOI: 10.1007/s10719-007-9045-0
  Journal NLM ID: 8603310
  Publisher: Kluwer Academic Publishers
  Correspondence: olablixt@scripps.edu
  Institutions: Department of Molecular Biology, Glycan Array Synthesis Core D, Consortium for Functional Glycomics. The Scripps Research Institute, CB 248A 10550 N. Torrey Pines Road, La Jolla, CA, 92037, USA
  Methods: serological methods
  
   
  
  Salmonella typhimurium O4, Salmonella typhimurium O12
  CSDB ID 22841 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130646,IEDB_130650,IEDB_130654,IEDB_130655,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_140088,IEDB_140108,IEDB_140122,IEDB_141500,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_142489,IEDB_144556,IEDB_144562,IEDB_144998,IEDB_145003,IEDB_145669,IEDB_146664,IEDB_147455,IEDB_149557,IEDB_150092,IEDB_150939,IEDB_151528,IEDB_151531,IEDB_152214,IEDB_158550,IEDB_167070,IEDB_174333,IEDB_190606,IEDB_2151203,IEDB_2189046,IEDB_2189047,IEDB_461720,IEDB_952752,IEDB_983931,SB_157,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_7,SB_86,SB_88

• Article ID: 3520
  Moran AP "Relevance of fucosylation and Lewis antigen expression in the bacterial gastroduodenal pathogen Helicobacter pylori" - Carbohydrate Research 343(12) (2008) 1952-1965
  

  Helicobacter pylori is a prevalent bacterial, gastroduodenal pathogen of humans that can express Lewis (Le) and related antigens in the O-chains of its surface lipopolysaccharide. The O-chains of H. pylori are commonly composed of internal Le(x) units with terminal Le(x) or Le(y) units or, in some strains, with additional units of Le(a), Le(b), Le(c), sialyl-Le(x) and H-1 antigens, as well as blood groups A and B, thereby producing a mosaicism of antigenic units expressed. The genetic determination of the Le antigen biosynthetic pathways in H. pylori has been studied, and despite striking functional similarity, low sequence homology occurs between the bacterial and mammalian α(1,3/4)- and α(1,2)-fucosyltransferases. Factors affecting Le antigen expression in H. pylori, that can influence the biological impact of this molecular mimicry, include regulation of fucosyltransferase genes through slipped-strand mispairing, the activity and expression levels of the functional enzymes, the preferences of the expressed enzyme for distinctive acceptor molecules and the availability of activated sugar intermediates. Le mimicry was initially implicated in immune evasion and gastric adaptation by the bacterium, but more recent studies show a role in gastric colonization and bacterial adhesion with galectin-3 identified as the gastric receptor for polymeric Le(x) on the bacterium. From the host defence aspect, innate immune recognition of H. pylori by surfactant protein D is influenced by the extent of LPS fucosylation. Furthermore, Le antigen expression affects both the inflammatory response and T-cell polarization that develops after infection. Although controversial, evidence suggests that long-term H. pylori infection can induce autoreactive anti-Le antibodies cross-reacting with the gastric mucosa, in part leading to the development of gastric atrophy. Thus, Le antigen expression and fucosylation in H. pylori have multiple biological effects on pathogenesis and disease outcome.

  molecular mimicry, Helicobacter pylori, Fucosyltransferases, bacterial pathogenesis, Lewis antigens, fucosylation

  NCBI PubMed ID: 18279843
  Publication DOI: 10.1016/j.carres.2007.12.012
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: anthony.moran@nuigalway.ie
  Institutions: Department of Microbiology, School of Natural Sciences, National University of Ireland, Galway, Ireland, Institute for Glycomics, Gold Coast Campus, Griffith University, Queensland 4222, Australia
  Methods: NMR, sugar analysis, MS, genetic methods
  
   
  
  Helicobacter pylori NCTC 11637
  CSDB ID 23178 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130646,IEDB_130650,IEDB_130670,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391962,IEDB_140088,IEDB_140108,IEDB_140122,IEDB_140529,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142488,IEDB_143794,IEDB_144998,IEDB_145003,IEDB_146664,IEDB_150899,IEDB_151528,IEDB_151531,IEDB_167070,IEDB_190606,IEDB_2189047,IEDB_226811,IEDB_232584,IEDB_983931,SB_137,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_29,SB_30,SB_7,SB_88

• Article ID: 3866
  Johansen EB, Szoka FC, Zaleski A, Apicella MA, Gibson BW "Utilizing the O-antigen Lipopolysaccharide Biosynthesis Pathway in Escherichia coli to Interrogate the Substrate Specificities of Exogenous Glycosyltransferase Genes in a Combinatorial Approach" - Glycobiology 20(6) (2010) 763-774
  

  In previous work, our laboratory generated novel chimeric lipopolysaccharides (LPS) in Escherichia coli transformed with a plasmid containing exogenous lipooligosaccharide synthesis genes (lsg) from Haemophilus influenzae. Analysis of these novel oligosaccharide-LPS chimeras allowed characterization of the carbohydrate structures generated by several putative glycosyltransferase genes within the lsg locus. Here, we adapted this strategy to construct a modular approach to study the synthetic properties of individual glycosyltransferases expressed alone and in combinations. To this end, a set of expression vectors containing one to four putative glycosyltransferase genes from the lsg locus, lsgC-F, were transformed into E. coli K12 (XL-1) which is defective in LPS O-antigen biosynthesis. This strategy relied on the inclusion of the H. influenzae gene product lsgG in every plasmid construct, which partially rescues the E. coli LPS biosynthesis defect by priming UDP-undecaprenyl in the WecA-dependent O-antigen synthetic pathway with N-acetyl-glucosamine (GlcNAc). This GlcNAc-undecaprenyl then served as an acceptor substrate for further carbohydrate extension by transformed glycosyltransferases. The resultant LPS-linked chimeric glycans were isolated from their E. coli constructs and characterized by mass spectrometry, methylation analysis and ELISA. These structural data allowed the specificity of various glycosyltransferases to be unambiguously assigned to individual genes. LsgF was found to transfer a galactose (Gal) to terminal GlcNAc. LsgE was found to transfer GlcNAc to Gal-GlcNAc, and both LsgF and LsgD were found to transfer Gal to GlcNAc-Gal-GlcNAc, but with differing linkage specificities. This method can be generalized and readily adapted to study the substrate specificity of other putative or uncharacterized glycosyltransferases.

  Escherichia coli, mass spectrometry, glycosyltransferase, assay, E. coli, chimera

  NCBI PubMed ID: 20208062
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Correspondence: bgibson@buckinstitute.org
  Institutions: Department of Pharmaceutical Chemistry and Pharmaceutical Sciences, University of California, San Francisco, CA, USA
  Methods: HF solvolysis, de-O-acylation, SDS-PAGE, ELISA, MALDI-TOF MS, genetic methods
  
   
  
  Escherichia coli K12 (pGEM)
  CSDB ID 25295 (all data & tools)

Show legend Show as text

Structure type: polymer chemical repeating unit
Contained glycoepitopes: IEDB_136044,IEDB_136906,IEDB_137472,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_145003,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_153543,IEDB_190606,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_6,SB_7,SB_88

• Article ID: 5880
  De Vuyst L, De Vin F "Exopolysaccharides from Lactic Acid Bacteria" - Book: Comprehensive Glycoscience: From Chemistry to Systems Biology. Reference Module in Chemistry, Molecular Sciences and Chemical Engineering (2007) 477-519
  

  carbohydrates, polysaccharides, Lactic acid bacteria, exopolysaccharides, glycolipids, glycoproteins, Glycomics

  Publication DOI: 10.1016/B978-044451967-2/00129-X
  Publisher: Elsevier
  Correspondence: ldvuyst@vub.ac.be
  Editors: Barchi J, Kamerling H
  Institutions: Department of Applied Biological Sciences and Engineering, Research Group of Industrial Microbiology and Food Biotechnology, Vrije Universiteit Brussel, Brussels, Belgium
  
   
  
  Lactobacillus helveticus TY1-2
  CSDB ID 25146 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure
Trivial name: ceramide phosphoinositol glycan core (CPI-GC)
Compound class: LPG
Contained glycoepitopes: IEDB_135813,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_141794,IEDB_141807,IEDB_145003,IEDB_151528,IEDB_151531,IEDB_167070,IEDB_190606,SB_173,SB_7

• Article ID: 5942
  Heiss C, Wang Z, Azadi P, Fichrova RN, Singh BN "Novel structural features of the immunocompetent ceramide phospho-inositol glycan core from Trichomonas vaginalis" - Carbohydrate Research 419 (2016) 51-59
  

  The ceramide phosphoinositol glycan core (CPI-GC) of the lipophosphoglycan of Trichomonas vaginalis is a major virulent factor of this common genitourinary parasite. While its carbohydrate composition has been reported before, its structure has remained largely unknown. We isolated the glycan portions of CPI-GC by nitrous acid deamination and hydrofluoric acid treatment and investigated their structures by methylation analysis and 1- and 2-D NMR. We found that the α-anomer of galactose is a major constituent of CPI-GC. The β-anomer was found exclusively at the non-reducing end of CPI-GC side chains. Furthermore the data showed that the rhamnan backbone is more complex than previously thought and that the inositol residue at the reducing end is linked to a 4-linked α-glucuronic acid (GlcA) residue. This appears to be the most striking and novel feature of this GPI-anchor type molecule.

  NMR, glycoconjugates, Phospho-inositol glycan core, Trichomonas vaginalis

  NCBI PubMed ID: 26671321
  Publication DOI: 10.1016/j.carres.2015.11.001
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: singhb@upstate.edu; cheiss@uga.edu
  Institutions: Complex Carbohydrate Research Center, The University of Georgia, 315 Riverbend Road, Athens, GA 30602, USA, Department of Obstetrics, Gynecology and Reproductive Biology, Brigham and Women's Hospital, Harvard Medical School, 221 Longwood Avenue, Boston, MA 02115, USA, Department of Biochemistry and Molecular Biology, SUNY Upstate Medical University, 750 E Adams St, Syracuse, NY 13210, USA
  Methods: 13C NMR, 1H NMR, NMR-2D, methylation, GC-MS, HF treatment, nitrous deamination, enzymatic treatment, HPAE-PAD HPLC
  
   
  
  Trichomonas vaginalis UR1
  CSDB ID 4543 (all data & tools)