Show legend Show as text

Structure type: oligomer
Trivial name: Lewisa, Lewis a
Contained glycoepitopes: IEDB_130653,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_1391962,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_149556,IEDB_150899,IEDB_151531,IEDB_152214,IEDB_174333,IEDB_190606,IEDB_423096,IEDB_461723,SB_137,SB_155,SB_165,SB_166,SB_187,SB_195,SB_29,SB_7,SB_86,SB_88

• Article ID: 16
  Blixt O, Van Die I, Norberg T, van den Eijnden DH "High-level expression of the Neisseria meningitidis lgtA gene in Escherichia coli and characterization of the encoded N-acetylglucosaminyltransferase as a useful catalyst in the synthesis of GlcNAcb1→3Gal and GalNAcb1-3Gal linkages" - Glycobiology 9(10) (1999) 1061-1071
  

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

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

  NCBI PubMed ID: 10521543
  Publication DOI: 10.1093/glycob/9.10.1061
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Institutions: Department of Chemistry, Swedish University of Agricultural Sciences, Uppsala, Sweden, Department of Medical Chemistry, Vrije Universiteit, Van der Boechorstraat 7, 1081 BT Amsterdam, The Netherlands
  Methods: 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, enzyme-assisted synthesis, DNA techniques, glycosyltransferase assays, kinetics assays
  
   
  
  Escherichia coli
  CSDB ID 1740 (all data & tools)
• Article ID: 230
  Feizi T "Progress in deciphering the information content of the 'glycome' - a crescendo in the closing years of the millennium" - Glycoconjugate Journal 17(7-9) (2000) 553-565
  

  The closing years of the second millennium have been uplifting for carbohydrate biology. Optimism that oligosaccharide sequences are bearers of crucial biological information has been borne out by the constellation of efforts of carbohydrate chemists, biochemists, immunochemists, and cell- and molecular biologists. The direct involvement of specific oligosaccharide sequences in protein targeting and folding, and in mechanisms of infection, inflammation and immunity is now unquestioned. With the emergence of families of proteins with carbohydrate-binding activities, assignments of information content for defined oligosaccharide sequences will become more common, but the pinpointing and elucidation of the bioactive domains on oligosaccharides will continue to pose challenges even to the most experienced carbohydrate biologists. The neoglycolipid technology incorporates some of the key requirements for this challenge: namely the resolution of complex glycan mixtures, and ligand binding coupled with sequence determination by mass spectrometry.

  monoclonal antibodies, mass spectrometry, blood group antigen, carbohydrate ligands, differentiation antigens, embryonic development, galectins, inflammation, leukocyte adhesion, neoglycolipids, oligosaccharide ligands, oligosaccharid probes, selectins

  NCBI PubMed ID: 11421348
  Journal NLM ID: 8603310
  Publisher: Kluwer Academic Publishers
  Correspondence: t.feizi@ic.ac.uk
  Institutions: The Glycosciences Laboratory, Imperial College School of Medicine, Harrow, United Kingdom
  
   
  
  (bacteria)
  CSDB ID 6941 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: 3'-sialyl-LeA
Contained glycoepitopes: IEDB_130653,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_1391962,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142353,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_146100,IEDB_149174,IEDB_149556,IEDB_150899,IEDB_150933,IEDB_151531,IEDB_152214,IEDB_153235,IEDB_174333,IEDB_190606,IEDB_241110,IEDB_423096,IEDB_461723,SB_116,SB_127,SB_137,SB_155,SB_165,SB_166,SB_170,SB_171,SB_172,SB_186,SB_187,SB_195,SB_29,SB_39,SB_68,SB_7,SB_84,SB_86,SB_88

• Article ID: 230
  Feizi T "Progress in deciphering the information content of the 'glycome' - a crescendo in the closing years of the millennium" - Glycoconjugate Journal 17(7-9) (2000) 553-565
  

  The closing years of the second millennium have been uplifting for carbohydrate biology. Optimism that oligosaccharide sequences are bearers of crucial biological information has been borne out by the constellation of efforts of carbohydrate chemists, biochemists, immunochemists, and cell- and molecular biologists. The direct involvement of specific oligosaccharide sequences in protein targeting and folding, and in mechanisms of infection, inflammation and immunity is now unquestioned. With the emergence of families of proteins with carbohydrate-binding activities, assignments of information content for defined oligosaccharide sequences will become more common, but the pinpointing and elucidation of the bioactive domains on oligosaccharides will continue to pose challenges even to the most experienced carbohydrate biologists. The neoglycolipid technology incorporates some of the key requirements for this challenge: namely the resolution of complex glycan mixtures, and ligand binding coupled with sequence determination by mass spectrometry.

  monoclonal antibodies, mass spectrometry, blood group antigen, carbohydrate ligands, differentiation antigens, embryonic development, galectins, inflammation, leukocyte adhesion, neoglycolipids, oligosaccharide ligands, oligosaccharid probes, selectins

  NCBI PubMed ID: 11421348
  Journal NLM ID: 8603310
  Publisher: Kluwer Academic Publishers
  Correspondence: t.feizi@ic.ac.uk
  Institutions: The Glycosciences Laboratory, Imperial College School of Medicine, Harrow, United Kingdom
  
   
  
  (bacteria)
  CSDB ID 6943 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: 3'-sulfo-LeA
Contained glycoepitopes: IEDB_130653,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_1391962,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_149556,IEDB_150899,IEDB_151531,IEDB_152214,IEDB_174333,IEDB_190606,IEDB_241114,IEDB_423096,IEDB_461723,SB_118,SB_137,SB_155,SB_165,SB_166,SB_187,SB_195,SB_29,SB_7,SB_86,SB_88

• Article ID: 230
  Feizi T "Progress in deciphering the information content of the 'glycome' - a crescendo in the closing years of the millennium" - Glycoconjugate Journal 17(7-9) (2000) 553-565
  

  The closing years of the second millennium have been uplifting for carbohydrate biology. Optimism that oligosaccharide sequences are bearers of crucial biological information has been borne out by the constellation of efforts of carbohydrate chemists, biochemists, immunochemists, and cell- and molecular biologists. The direct involvement of specific oligosaccharide sequences in protein targeting and folding, and in mechanisms of infection, inflammation and immunity is now unquestioned. With the emergence of families of proteins with carbohydrate-binding activities, assignments of information content for defined oligosaccharide sequences will become more common, but the pinpointing and elucidation of the bioactive domains on oligosaccharides will continue to pose challenges even to the most experienced carbohydrate biologists. The neoglycolipid technology incorporates some of the key requirements for this challenge: namely the resolution of complex glycan mixtures, and ligand binding coupled with sequence determination by mass spectrometry.

  monoclonal antibodies, mass spectrometry, blood group antigen, carbohydrate ligands, differentiation antigens, embryonic development, galectins, inflammation, leukocyte adhesion, neoglycolipids, oligosaccharide ligands, oligosaccharid probes, selectins

  NCBI PubMed ID: 11421348
  Journal NLM ID: 8603310
  Publisher: Kluwer Academic Publishers
  Correspondence: t.feizi@ic.ac.uk
  Institutions: The Glycosciences Laboratory, Imperial College School of Medicine, Harrow, United Kingdom
  
   
  
  (bacteria)
  CSDB ID 6945 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: core
Trivial name: Lewis A
Contained glycoepitopes: IEDB_130653,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_1391962,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_149556,IEDB_150899,IEDB_151531,IEDB_152214,IEDB_174333,IEDB_190606,IEDB_423096,IEDB_461723,SB_137,SB_155,SB_165,SB_166,SB_187,SB_195,SB_29,SB_7,SB_86,SB_88

• Article ID: 329
  Monteiro MA, Chan KHN, Rasko DA, Taylor DE, Zheng PY, Appelmelk BJ, Wirth HP, Yang MQ, Blaser MJ, Hynes SO, Moran AP, Perry MB "Simultaneous expression of type 1 and type 2 Lewis blood group antigens by Helicobacter pylori lipopolysaccharides" - Journal of Biological Chemistry 273(19) (1998) 11533-11543
  

  Previous structural investigations performed on the lipopolysaccharides (LPSs) from the human gastric pathogen Helicobacter pylori have revealed that these cell surface glycan molecules express type 2 partially fucosylated, glucosylated, or galactosylated N-acetyllactosamine O antigen chains (O-chains) of various lengths, which may or may not be terminated at the nonreducing end by Lewis X (Lex) and/or Ley blood group epitopes in mimicry of human cell surface glycoconjugates and glycolipids. Subsequently, serological experiments with commercially available Lewis-specific monoclonal antibodies also have recognized the presence of Lex and Ley blood group antigens in H. pylori but, in addition, have indicated the presence of type 1 chain Lea, Leb, and Led (H-type 1) blood group epitopes in some H. pylori strains. To confirm their presence, structural studies and additional serological experiments were undertaken on H. pylori strains suspected of carrying type 1 chain epitopes. These investigations revealed that the O-chain region of H. pylori strain UA948 carried both Lea (type 1) and Lex (type 2) blood group determinants. The O-chain from H. pylori UA955 LPS expressed the terminal Lewis disaccharide (type 1 chain) and Lex and Ley antigens (type 2). The O-chain of H. pylori J223 LPS carried the type 1 chain precursor Lec, the H-1 epitope (Led, type 1 chain) and an elongated nonfucosylated type 2 N-acetyllactosamine chain (i antigen). Thus, O-chains from H. pylori LPSs can also express fucosylated type 1 sequences, and the LPS from a single H. pylori strain may carry O-chains with type 1 and 2 Lewis blood groups simultaneously. That monoclonal antibodies putatively specific for the Leb determinant can detect glycan substructures (Le disaccharide, Lec, and Led) of Leb indicates their nonspecificity. The expression of both type 1 and 2 Lewis antigens by H. pylori LPSs mimics the cell surface glycomolecules present in both the gastric superficial (which expresses mainly type 1 determinants) and the superficial and glandular epithelium regions (both of which express predominantly type 2 determinants). Therefore, each H. pylori strain may have a different niche within the gastric mucosa, and each individual LPS blood group antigen may have a dissimilar role in H. pylori adaptation.

  antigen, lipopolysaccharides, expression, type, Helicobacter pylori, Helicobacter, Lewis, blood group antigens

  NCBI PubMed ID: 9565568
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: Mario.Monteiro@nrc.ca
  Institutions: Department of Microbiology, National University of Ireland, Galway, Ireland, Canadian Bacterial Diseases Network, b Institute for Biological Sciences, National Research Council, Ottawa, K1A 0R6 Ontario, Canada, Department of Medical Microbiology and Immunology, University of Alberta, Edmonton, T6G 2H7 Alberta, Canada, Department of Medical Microbiology, Vrije Universiteit Amsterdam, Amsterdam, The Netherlands, Division of Gastroenterology, Zurich University Scool of Medicine, Zurich, Switzerland, Department of Medicine, Vanderbilt University and Veterans Affairs Medical Center, Nashville, Tennessee
  Methods: 1H NMR, FAB-MS, ELISA, GLC, immunoblotting
  
   
  
  Helicobacter pylori UA948
  CSDB ID 7819 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: LPS
Trivial name: Lewis a
Contained glycoepitopes: IEDB_130653,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_1391962,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_149556,IEDB_150899,IEDB_151531,IEDB_152214,IEDB_174333,IEDB_190606,IEDB_423096,IEDB_461723,SB_137,SB_155,SB_165,SB_166,SB_187,SB_195,SB_29,SB_7,SB_86,SB_88

• Article ID: 603
  Appelmelk BJ, Martino MC, Veenhof E, Monteiro MA, Maaskant JJ, Negrini R, Lindh F, Perry MB, del Guidice G, Vandenbroucke-Grauls CMJE "Phase variation in H type 1 and Lewis a epitopes of Helicobacter pylori lipopolysaccharide" - Infection and Immunity 68(10) (2000) 5928-5932
  

  Helicobacter pylori NCTC11637 lipopolysaccharide (LPS) expresses the human blood group antigens Lewis x (Lex), Ley, and H type I. In this report, we demonstrate that the H type I epitope displays high-frequency phase variation. One variant expressed Lex and Ley and no H type I as determined by serology; this switch was reversible. Insertional mutagenesis in NCTC11637 of JHP563 (a poly(C) tract containing an open reading frame homologous to glycosyltransferases) yielded a transformant with a serotype similar to the phase variant. Structural analysis of the NCTC11637 LPS confirmed the loss of the H type I epitope. Sequencing of JHP563 in strains NCTC11637, an H type I-negative variant, and an H type I-positive switchback variant showed a C14 (gene on), C13 (gene off), and C14 tract, respectively. Inactivation of strain G27, which expresses Lex, Ley, H type I, and Lea, yielded a transformant that expressed Lex and Ley. We conclude that JHP563 encodes a b3-galactosyltransferase involved in the biosynthesis of H type I and Lea and that phase variation in H type I is due to C-tract changes in this gene. A second H type I-negative variant (variant 3a) expressed Lex and Lea and had lost both H type I and Ley expression. Inactivation of HP093-HP094 resulted in a transformant expressing Lex and lacking Ley and H type I. Structural analysis of a mutant LPS confirmed the serological data. We conclude that the HP093-HP094 a2-fucosyltransferase (a2-Fuct) gene product is involved in the biosynthesis of both Ley and Lex. Finally, we inactivated HP0379 in strain 3a. The transformant had lost both Lex and Lea expression, which demonstrates that the HP0379 gene product is both an a3- and an a4-FucT. Our data provide understanding at the molecular level of how H. pylori is able to diversify in the host, a requirement likely essential for successful colonization and transmission.

  Lipopolysaccharide, Phase variation, gene, phase, tract, variation, epitope, type, epitopes, Helicobacter pylori, Helicobacter, change, Lewis, fucosyltransferase, Lewis a

  NCBI PubMed ID: 10992504
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Correspondence: BJ.Appelmelk.mm@med.vu.nl
  Institutions: Department of Medical Microbiology, Vrije Universiteit, Medical School, 1081 BT Amsterdam, The Netherlands, IRIS Research Center, Chiron SpA, Siena, Laboratory Unit, City Hospital, Brescia, Italy, National Research Council, Ottawa, Canada, Isosep, Tullinge, Sweden
  Methods: PCR, DNA sequencing, FAB-MS, ELISA, MAb studies, insertional mutagenesis
  
   
  
  Helicobacter pylori
  CSDB ID 286 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: LPS
Trivial name: Lewis b
Contained glycoepitopes: IEDB_130652,IEDB_130653,IEDB_131182,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137354,IEDB_137472,IEDB_1391962,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_149554,IEDB_149556,IEDB_150899,IEDB_150948,IEDB_151531,IEDB_152214,IEDB_153553,IEDB_174333,IEDB_190606,IEDB_423096,IEDB_461709,IEDB_461719,IEDB_461723,IEDB_461724,SB_100,SB_137,SB_146,SB_154,SB_155,SB_165,SB_166,SB_187,SB_195,SB_29,SB_7,SB_86,SB_88

• Article ID: 603
  Appelmelk BJ, Martino MC, Veenhof E, Monteiro MA, Maaskant JJ, Negrini R, Lindh F, Perry MB, del Guidice G, Vandenbroucke-Grauls CMJE "Phase variation in H type 1 and Lewis a epitopes of Helicobacter pylori lipopolysaccharide" - Infection and Immunity 68(10) (2000) 5928-5932
  

  Helicobacter pylori NCTC11637 lipopolysaccharide (LPS) expresses the human blood group antigens Lewis x (Lex), Ley, and H type I. In this report, we demonstrate that the H type I epitope displays high-frequency phase variation. One variant expressed Lex and Ley and no H type I as determined by serology; this switch was reversible. Insertional mutagenesis in NCTC11637 of JHP563 (a poly(C) tract containing an open reading frame homologous to glycosyltransferases) yielded a transformant with a serotype similar to the phase variant. Structural analysis of the NCTC11637 LPS confirmed the loss of the H type I epitope. Sequencing of JHP563 in strains NCTC11637, an H type I-negative variant, and an H type I-positive switchback variant showed a C14 (gene on), C13 (gene off), and C14 tract, respectively. Inactivation of strain G27, which expresses Lex, Ley, H type I, and Lea, yielded a transformant that expressed Lex and Ley. We conclude that JHP563 encodes a b3-galactosyltransferase involved in the biosynthesis of H type I and Lea and that phase variation in H type I is due to C-tract changes in this gene. A second H type I-negative variant (variant 3a) expressed Lex and Lea and had lost both H type I and Ley expression. Inactivation of HP093-HP094 resulted in a transformant expressing Lex and lacking Ley and H type I. Structural analysis of a mutant LPS confirmed the serological data. We conclude that the HP093-HP094 a2-fucosyltransferase (a2-Fuct) gene product is involved in the biosynthesis of both Ley and Lex. Finally, we inactivated HP0379 in strain 3a. The transformant had lost both Lex and Lea expression, which demonstrates that the HP0379 gene product is both an a3- and an a4-FucT. Our data provide understanding at the molecular level of how H. pylori is able to diversify in the host, a requirement likely essential for successful colonization and transmission.

  Lipopolysaccharide, Phase variation, gene, phase, tract, variation, epitope, type, epitopes, Helicobacter pylori, Helicobacter, change, Lewis, fucosyltransferase, Lewis a

  NCBI PubMed ID: 10992504
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Correspondence: BJ.Appelmelk.mm@med.vu.nl
  Institutions: Department of Medical Microbiology, Vrije Universiteit, Medical School, 1081 BT Amsterdam, The Netherlands, IRIS Research Center, Chiron SpA, Siena, Laboratory Unit, City Hospital, Brescia, Italy, National Research Council, Ottawa, Canada, Isosep, Tullinge, Sweden
  Methods: PCR, DNA sequencing, FAB-MS, ELISA, MAb studies, insertional mutagenesis
  
   
  
  Helicobacter pylori
  CSDB ID 287 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Trivial name: type 1 Lewis A determinant
Contained glycoepitopes: IEDB_130650,IEDB_130653,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_1391962,IEDB_140088,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142488,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_144998,IEDB_146664,IEDB_149556,IEDB_150899,IEDB_151531,IEDB_152214,IEDB_174333,IEDB_190606,IEDB_2189046,IEDB_2189047,IEDB_423096,IEDB_461723,IEDB_983931,SB_137,SB_155,SB_165,SB_166,SB_187,SB_192,SB_195,SB_29,SB_7,SB_86,SB_88

• Article ID: 1005
  Monteiro MA, Zheng P, Ho B, Yokota S, Amano K, Pan Z, Berg DE, Chan KH, MacLean LL, Perry MB "Expression of histo-blood group antigens by lipopolysaccharides of Helicobacter pylori strains from Asian hosts: the propensity to express type 1 blood-group antigens" - Glycobiology 10(7) (2000) 701-713
  

  Past studies have shown that the cell surface lipopolysaccharides (LPSs) of the ubiquitous human gastric pathogen Helicobacter pylori (a type 1 carcinogen) isolated from people residing in Europe and North America express predominantly type 2 Lewis x (Le(x)) and Le(y) epitopes and, infrequently, type 1 Le(a), Le(b), and Le(d) antigens. This production of Lewis blood-group structures by H. pylori LPSs, similar to those found in the surfaces of human gastric cells, allows the bacterium to mimic its human niche. In this study, LPSs of H.pylori strains extracted from patients living in China, Japan, and Singapore were chemically and serologically analyzed. When compared with Western H.pylori LPSs, these Asian strains showed a stronger tendency to produce type 1 blood groups. Of particular interest, and novel observations in H.pylori, the O-chain regions of strains F-58C and R-58A carried type 1 Le(a) without the presence of type 2 Le(x), strains R-7A and H607 were shown to have the capability of producing the type 1 blood group A antigen, and strains CA2, H507, and H428 expressed simultaneously the difucosyl isomeric antigens, type 1 Le(b) and type 2 Le(y). The apparent proclivity for the production of type 1 histo-blood group antigens in Asian H.pylori LPSs, as compared with Western strains, may be an adaptive evolutionary effect in that differences in the gastric cell surfaces of the respective hosts might be significantly dissimilar to select for the formation of different LPS structures on the resident H.pylori strain.

  lipopolysaccharides, structural determination, Helicobacter pylori, histo-blood groups

  NCBI PubMed ID: 10910974
  Publication DOI: 10.1093/glycob/10.7.701
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Institutions: Institute for Biological Sciences, National Research Council, Ottawa, Canada, Department of Microbiology, National University of Singapore, Singapore, Central Research Laboratory, Akita University School of Medicine, Akita, Japan, Departments of Molecular Microbiology and Genetics, Washington University School of Medicine, St. Louis, MO 63130, USA
  Methods: FAB-MS, NMR
  
   
  
  Helicobacter pylori F-58C, Helicobacter pylori R-58A, Helicobacter pylori F-15A, Helicobacter pylori CA4, Helicobacter pylori CA5, Helicobacter pylori GU2
  CSDB ID 3478 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Trivial name: type 1 difucosyl A blood-group determinant
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130648,IEDB_130650,IEDB_130652,IEDB_130653,IEDB_131182,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_136095,IEDB_137340,IEDB_137354,IEDB_137472,IEDB_137473,IEDB_1391961,IEDB_1391962,IEDB_140088,IEDB_140124,IEDB_141584,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142488,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_144998,IEDB_146664,IEDB_149554,IEDB_149556,IEDB_149568,IEDB_150899,IEDB_150948,IEDB_151531,IEDB_152213,IEDB_152214,IEDB_152218,IEDB_153205,IEDB_153223,IEDB_153536,IEDB_153553,IEDB_153554,IEDB_157005,IEDB_174039,IEDB_174333,IEDB_190606,IEDB_2189046,IEDB_2189047,IEDB_423096,IEDB_461709,IEDB_461712,IEDB_461719,IEDB_461723,IEDB_461724,IEDB_885822,IEDB_983931,SB_100,SB_102,SB_137,SB_146,SB_149,SB_154,SB_155,SB_165,SB_166,SB_187,SB_192,SB_195,SB_29,SB_7,SB_86,SB_88

• Article ID: 1005
  Monteiro MA, Zheng P, Ho B, Yokota S, Amano K, Pan Z, Berg DE, Chan KH, MacLean LL, Perry MB "Expression of histo-blood group antigens by lipopolysaccharides of Helicobacter pylori strains from Asian hosts: the propensity to express type 1 blood-group antigens" - Glycobiology 10(7) (2000) 701-713
  

  Past studies have shown that the cell surface lipopolysaccharides (LPSs) of the ubiquitous human gastric pathogen Helicobacter pylori (a type 1 carcinogen) isolated from people residing in Europe and North America express predominantly type 2 Lewis x (Le(x)) and Le(y) epitopes and, infrequently, type 1 Le(a), Le(b), and Le(d) antigens. This production of Lewis blood-group structures by H. pylori LPSs, similar to those found in the surfaces of human gastric cells, allows the bacterium to mimic its human niche. In this study, LPSs of H.pylori strains extracted from patients living in China, Japan, and Singapore were chemically and serologically analyzed. When compared with Western H.pylori LPSs, these Asian strains showed a stronger tendency to produce type 1 blood groups. Of particular interest, and novel observations in H.pylori, the O-chain regions of strains F-58C and R-58A carried type 1 Le(a) without the presence of type 2 Le(x), strains R-7A and H607 were shown to have the capability of producing the type 1 blood group A antigen, and strains CA2, H507, and H428 expressed simultaneously the difucosyl isomeric antigens, type 1 Le(b) and type 2 Le(y). The apparent proclivity for the production of type 1 histo-blood group antigens in Asian H.pylori LPSs, as compared with Western strains, may be an adaptive evolutionary effect in that differences in the gastric cell surfaces of the respective hosts might be significantly dissimilar to select for the formation of different LPS structures on the resident H.pylori strain.

  lipopolysaccharides, structural determination, Helicobacter pylori, histo-blood groups

  NCBI PubMed ID: 10910974
  Publication DOI: 10.1093/glycob/10.7.701
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Institutions: Institute for Biological Sciences, National Research Council, Ottawa, Canada, Department of Microbiology, National University of Singapore, Singapore, Central Research Laboratory, Akita University School of Medicine, Akita, Japan, Departments of Molecular Microbiology and Genetics, Washington University School of Medicine, St. Louis, MO 63130, USA
  Methods: FAB-MS, NMR
  
   
  
  Helicobacter pylori R-7A
  CSDB ID 3546 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Trivial name: type 1 Lewis B determinant
Contained glycoepitopes: IEDB_130650,IEDB_130652,IEDB_130653,IEDB_131182,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137354,IEDB_137472,IEDB_1391962,IEDB_140088,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142488,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_144998,IEDB_146664,IEDB_149554,IEDB_149556,IEDB_150899,IEDB_150948,IEDB_151531,IEDB_152214,IEDB_153553,IEDB_174333,IEDB_190606,IEDB_2189046,IEDB_2189047,IEDB_423096,IEDB_461709,IEDB_461719,IEDB_461723,IEDB_461724,IEDB_983931,SB_100,SB_137,SB_146,SB_154,SB_155,SB_165,SB_166,SB_187,SB_192,SB_195,SB_29,SB_7,SB_86,SB_88

• Article ID: 1005
  Monteiro MA, Zheng P, Ho B, Yokota S, Amano K, Pan Z, Berg DE, Chan KH, MacLean LL, Perry MB "Expression of histo-blood group antigens by lipopolysaccharides of Helicobacter pylori strains from Asian hosts: the propensity to express type 1 blood-group antigens" - Glycobiology 10(7) (2000) 701-713
  

  Past studies have shown that the cell surface lipopolysaccharides (LPSs) of the ubiquitous human gastric pathogen Helicobacter pylori (a type 1 carcinogen) isolated from people residing in Europe and North America express predominantly type 2 Lewis x (Le(x)) and Le(y) epitopes and, infrequently, type 1 Le(a), Le(b), and Le(d) antigens. This production of Lewis blood-group structures by H. pylori LPSs, similar to those found in the surfaces of human gastric cells, allows the bacterium to mimic its human niche. In this study, LPSs of H.pylori strains extracted from patients living in China, Japan, and Singapore were chemically and serologically analyzed. When compared with Western H.pylori LPSs, these Asian strains showed a stronger tendency to produce type 1 blood groups. Of particular interest, and novel observations in H.pylori, the O-chain regions of strains F-58C and R-58A carried type 1 Le(a) without the presence of type 2 Le(x), strains R-7A and H607 were shown to have the capability of producing the type 1 blood group A antigen, and strains CA2, H507, and H428 expressed simultaneously the difucosyl isomeric antigens, type 1 Le(b) and type 2 Le(y). The apparent proclivity for the production of type 1 histo-blood group antigens in Asian H.pylori LPSs, as compared with Western strains, may be an adaptive evolutionary effect in that differences in the gastric cell surfaces of the respective hosts might be significantly dissimilar to select for the formation of different LPS structures on the resident H.pylori strain.

  lipopolysaccharides, structural determination, Helicobacter pylori, histo-blood groups

  NCBI PubMed ID: 10910974
  Publication DOI: 10.1093/glycob/10.7.701
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Institutions: Institute for Biological Sciences, National Research Council, Ottawa, Canada, Department of Microbiology, National University of Singapore, Singapore, Central Research Laboratory, Akita University School of Medicine, Akita, Japan, Departments of Molecular Microbiology and Genetics, Washington University School of Medicine, St. Louis, MO 63130, USA
  Methods: FAB-MS, NMR
  
   
  
  Helicobacter pylori CA2, Helicobacter pylori H428, Helicobacter pylori H507
  CSDB ID 3550 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Trivial name: type 1 Lewis A determinant
Contained glycoepitopes: IEDB_130650,IEDB_130653,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_1391962,IEDB_140088,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142488,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_144998,IEDB_146664,IEDB_149556,IEDB_150899,IEDB_151531,IEDB_152214,IEDB_158538,IEDB_174333,IEDB_190606,IEDB_2189046,IEDB_2189047,IEDB_423096,IEDB_461723,IEDB_983931,SB_137,SB_155,SB_165,SB_166,SB_187,SB_192,SB_195,SB_29,SB_7,SB_86,SB_88

• Article ID: 1005
  Monteiro MA, Zheng P, Ho B, Yokota S, Amano K, Pan Z, Berg DE, Chan KH, MacLean LL, Perry MB "Expression of histo-blood group antigens by lipopolysaccharides of Helicobacter pylori strains from Asian hosts: the propensity to express type 1 blood-group antigens" - Glycobiology 10(7) (2000) 701-713
  

  Past studies have shown that the cell surface lipopolysaccharides (LPSs) of the ubiquitous human gastric pathogen Helicobacter pylori (a type 1 carcinogen) isolated from people residing in Europe and North America express predominantly type 2 Lewis x (Le(x)) and Le(y) epitopes and, infrequently, type 1 Le(a), Le(b), and Le(d) antigens. This production of Lewis blood-group structures by H. pylori LPSs, similar to those found in the surfaces of human gastric cells, allows the bacterium to mimic its human niche. In this study, LPSs of H.pylori strains extracted from patients living in China, Japan, and Singapore were chemically and serologically analyzed. When compared with Western H.pylori LPSs, these Asian strains showed a stronger tendency to produce type 1 blood groups. Of particular interest, and novel observations in H.pylori, the O-chain regions of strains F-58C and R-58A carried type 1 Le(a) without the presence of type 2 Le(x), strains R-7A and H607 were shown to have the capability of producing the type 1 blood group A antigen, and strains CA2, H507, and H428 expressed simultaneously the difucosyl isomeric antigens, type 1 Le(b) and type 2 Le(y). The apparent proclivity for the production of type 1 histo-blood group antigens in Asian H.pylori LPSs, as compared with Western strains, may be an adaptive evolutionary effect in that differences in the gastric cell surfaces of the respective hosts might be significantly dissimilar to select for the formation of different LPS structures on the resident H.pylori strain.

  lipopolysaccharides, structural determination, Helicobacter pylori, histo-blood groups

  NCBI PubMed ID: 10910974
  Publication DOI: 10.1093/glycob/10.7.701
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Institutions: Institute for Biological Sciences, National Research Council, Ottawa, Canada, Department of Microbiology, National University of Singapore, Singapore, Central Research Laboratory, Akita University School of Medicine, Akita, Japan, Departments of Molecular Microbiology and Genetics, Washington University School of Medicine, St. Louis, MO 63130, USA
  Methods: FAB-MS, NMR
  
   
  
  Helicobacter pylori CA6
  CSDB ID 3555 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: acetylphenylenediamine-HSA
Trivial name: Lewis a antigen determinant
Compound class: neoglycoconjugate
Contained glycoepitopes: IEDB_117715,IEDB_130653,IEDB_135511,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_1391962,IEDB_1391966,IEDB_141499,IEDB_141794,IEDB_141807,IEDB_142076,IEDB_142078,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_144998,IEDB_146664,IEDB_149556,IEDB_150899,IEDB_151531,IEDB_152214,IEDB_157001,IEDB_174333,IEDB_190606,IEDB_226432,IEDB_423096,IEDB_461723,IEDB_983931,SB_137,SB_145,SB_155,SB_156,SB_160,SB_161,SB_165,SB_166,SB_173,SB_174,SB_187,SB_192,SB_195,SB_29,SB_6,SB_7,SB_86,SB_88

• Article ID: 1358
  Appelmelk BJ, Simoons-Smit I, Negrini R, Moran AP, Aspinall GO, Forte JG, de Vries T, Quan H, Verboom T, Maaskant JJ, Ghiara P, Kuipers EJ, Bloemena E, Tadema TM, Townsend RR, Tyagarajan K, Crothers JM, Monteiro MA, Savio A, De Graaf J "Potential role of molecular mimicry between Helicobacter pylori lipopolysaccharide and host Lewis blood group antigens in autoimmunity" - Infection and Immunity 64 (1996) 2031-2040
  

  Helicobacter pylori is involved in gastritis, gastric and duodenal ulcers, gastric adenocarcinoma, and mucosa-associated lymphoid tissue lymphoma. Earlier studies already suggested a role for autoimmune phenomena in H. pylori-linked disease. We now report that lipopolysaccharides (LPS) of H. pylori express Lewis y, Lewis x, and H type I blood group structures similar to those commonly occurring in gastric mucosa. Immunization of mice and rabbits with H. pylori cells or purified LPS induced an anti-Lewis x or y or anti-H type I response, yielding antibodies that bound human and murine gastric glandular tissue, granulocytes, adenocarcinoma, and mucosa-associated lymphoid tissue lymphoma cells. Experimental oral infections in mice or natural infection in humans yielded anti-Lewis antibodies also. The beta chain of gastric (H+,K+)-ATPase, the parietal cell proton pump involved in acid secretion, contained Lewis y epitopes; gastric mucin contained Lewis x and y antigenic determinants. Growth in mice of a hybridoma that secretes H. pylori-induced anti-Lewis y monoclonal antibodies resulted in histopathological evidence of gastritis, which indicates a direct pathogenic role for anti-Lewis antibodies. In conclusion, our observations demonstrate that molecular mimicry between H. pylori LPS and the host, based on Lewis antigens, and provide understanding of an autoimmune mechanism for H. pylori-associated type B gastritis.

  Lipopolysaccharide, antigen, LPS, potential, molecular mimicry, Helicobacter pylori, S-type LPS, Lewis x, blood group antigens

  NCBI PubMed ID: 8675304
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Correspondence: BJ.Appelmelk.mm@med.vu.nl
  Institutions: Department of Medical Microbiology, Vrije Universiteit, Medical School, Amsterdam, The Netherlands
  
   
  
  Helicobacter pylori
  CSDB ID 6363 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: acetylphenylenediamine-HSA
Trivial name: Lewis b antigen determinant
Compound class: neoglycoconjugate
Contained glycoepitopes: IEDB_117715,IEDB_130652,IEDB_130653,IEDB_131182,IEDB_135511,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137354,IEDB_137472,IEDB_1391962,IEDB_1391966,IEDB_141499,IEDB_141794,IEDB_141807,IEDB_142076,IEDB_142078,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_142489,IEDB_143248,IEDB_143249,IEDB_143794,IEDB_144562,IEDB_144998,IEDB_146664,IEDB_149554,IEDB_149556,IEDB_150899,IEDB_150948,IEDB_151531,IEDB_152214,IEDB_153553,IEDB_157001,IEDB_174333,IEDB_190606,IEDB_226432,IEDB_423095,IEDB_423096,IEDB_461709,IEDB_461719,IEDB_461723,IEDB_461724,IEDB_983931,SB_100,SB_137,SB_145,SB_146,SB_150,SB_153,SB_154,SB_155,SB_156,SB_160,SB_161,SB_165,SB_166,SB_173,SB_174,SB_187,SB_192,SB_195,SB_29,SB_6,SB_7,SB_86,SB_88

• Article ID: 1358
  Appelmelk BJ, Simoons-Smit I, Negrini R, Moran AP, Aspinall GO, Forte JG, de Vries T, Quan H, Verboom T, Maaskant JJ, Ghiara P, Kuipers EJ, Bloemena E, Tadema TM, Townsend RR, Tyagarajan K, Crothers JM, Monteiro MA, Savio A, De Graaf J "Potential role of molecular mimicry between Helicobacter pylori lipopolysaccharide and host Lewis blood group antigens in autoimmunity" - Infection and Immunity 64 (1996) 2031-2040
  

  Helicobacter pylori is involved in gastritis, gastric and duodenal ulcers, gastric adenocarcinoma, and mucosa-associated lymphoid tissue lymphoma. Earlier studies already suggested a role for autoimmune phenomena in H. pylori-linked disease. We now report that lipopolysaccharides (LPS) of H. pylori express Lewis y, Lewis x, and H type I blood group structures similar to those commonly occurring in gastric mucosa. Immunization of mice and rabbits with H. pylori cells or purified LPS induced an anti-Lewis x or y or anti-H type I response, yielding antibodies that bound human and murine gastric glandular tissue, granulocytes, adenocarcinoma, and mucosa-associated lymphoid tissue lymphoma cells. Experimental oral infections in mice or natural infection in humans yielded anti-Lewis antibodies also. The beta chain of gastric (H+,K+)-ATPase, the parietal cell proton pump involved in acid secretion, contained Lewis y epitopes; gastric mucin contained Lewis x and y antigenic determinants. Growth in mice of a hybridoma that secretes H. pylori-induced anti-Lewis y monoclonal antibodies resulted in histopathological evidence of gastritis, which indicates a direct pathogenic role for anti-Lewis antibodies. In conclusion, our observations demonstrate that molecular mimicry between H. pylori LPS and the host, based on Lewis antigens, and provide understanding of an autoimmune mechanism for H. pylori-associated type B gastritis.

  Lipopolysaccharide, antigen, LPS, potential, molecular mimicry, Helicobacter pylori, S-type LPS, Lewis x, blood group antigens

  NCBI PubMed ID: 8675304
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Correspondence: BJ.Appelmelk.mm@med.vu.nl
  Institutions: Department of Medical Microbiology, Vrije Universiteit, Medical School, Amsterdam, The Netherlands
  
   
  
  Helicobacter pylori
  CSDB ID 6364 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: LPS
Contained glycoepitopes: IEDB_115136,IEDB_130650,IEDB_130659,IEDB_131182,IEDB_136044,IEDB_136045,IEDB_137472,IEDB_140630,IEDB_141794,IEDB_141806,IEDB_141807,IEDB_142488,IEDB_142489,IEDB_144562,IEDB_144998,IEDB_146664,IEDB_149554,IEDB_149556,IEDB_150899,IEDB_150948,IEDB_151531,IEDB_152214,IEDB_153553,IEDB_174333,IEDB_190606,IEDB_423153,IEDB_461719,IEDB_983931,SB_100,SB_137,SB_146,SB_154,SB_155,SB_165,SB_166,SB_187,SB_192,SB_195,SB_29,SB_7,SB_86,SB_88

• Article ID: 3471
  Gargiulo V, Garozzo D, Lanzetta R, Molinaro A, Sturiale L, De Castro C, Parrilli M "Rhizobium rubi(T): A Gram-Negative Phytopathogenic Bacterium Expressing the Lewis B Epitope on the Outer Core of its Lipooligosaccharide Fraction" - Chembiochem: a European Journal of Chemical Biology 9(11) (2008) 1830-1835
  

  The structure of the core oligosaccharide from the phytopathogenic bacterium Rhizobium rubi was deduced by combining information from complementary chemical approaches (alkaline and acid hydrolysis), similar to the 'overlap peptide' strategy. This structure is new and it contains two main oligosaccharide backbones that differ in the substitution degree of the external Kdo unit. The relevant feature shared by both oligosaccharides is the presence of a tetrasaccharide motif that is similar to the blood group Lewis B antigen (Le(B)). This epitope differs from Le(B) in the glycosidic configuration of the glucosamine unit (alpha and not beta) and in the occurrence of acetyls substituents at O3 and/or O4 of the galactose moiety. Other notable structural features are the location of the Dha residue, the presence of a α-glucose unit that is linked to the inner Kdo unit, the high number of acid sugars and the highly branched core structure

  structure, Lipooligosaccharide, epitope, core oligosaccharide, Phytopathogenic bacteria, Lewis B antigen, Rhizobium rubi

  NCBI PubMed ID: 18574826
  Publication DOI: 10.1002/cbic.200800191
  Journal NLM ID: 100937360
  Publisher: Weinheim, Germany: Wiley Interscience
  Correspondence: decastro@unina.it
  Institutions: Department of Organic Chemistry and Biochemistry, University of Napoli 'Federico II', Via Cintia 4, 80126 Napoli (Italy), Fax: (+39) 81674393
  Methods: 13C NMR, 1H NMR, NMR-2D, methylation, GC-MS, 31P NMR, acid hydrolysis, alkaline degradation, MALDI-MS, composition analysis
  
   
  
  Rhizobium rubi T
  CSDB ID 22649 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: LPS
Contained glycoepitopes: IEDB_115136,IEDB_130650,IEDB_130659,IEDB_131182,IEDB_136044,IEDB_136045,IEDB_137472,IEDB_140630,IEDB_141794,IEDB_141806,IEDB_141807,IEDB_142488,IEDB_142489,IEDB_144562,IEDB_144998,IEDB_146664,IEDB_149554,IEDB_149556,IEDB_150899,IEDB_150948,IEDB_151531,IEDB_152214,IEDB_153553,IEDB_174333,IEDB_190606,IEDB_423153,IEDB_461719,IEDB_983931,SB_100,SB_137,SB_146,SB_154,SB_155,SB_165,SB_166,SB_187,SB_192,SB_195,SB_29,SB_7,SB_86,SB_88

• Article ID: 3471
  Gargiulo V, Garozzo D, Lanzetta R, Molinaro A, Sturiale L, De Castro C, Parrilli M "Rhizobium rubi(T): A Gram-Negative Phytopathogenic Bacterium Expressing the Lewis B Epitope on the Outer Core of its Lipooligosaccharide Fraction" - Chembiochem: a European Journal of Chemical Biology 9(11) (2008) 1830-1835
  

  The structure of the core oligosaccharide from the phytopathogenic bacterium Rhizobium rubi was deduced by combining information from complementary chemical approaches (alkaline and acid hydrolysis), similar to the 'overlap peptide' strategy. This structure is new and it contains two main oligosaccharide backbones that differ in the substitution degree of the external Kdo unit. The relevant feature shared by both oligosaccharides is the presence of a tetrasaccharide motif that is similar to the blood group Lewis B antigen (Le(B)). This epitope differs from Le(B) in the glycosidic configuration of the glucosamine unit (alpha and not beta) and in the occurrence of acetyls substituents at O3 and/or O4 of the galactose moiety. Other notable structural features are the location of the Dha residue, the presence of a α-glucose unit that is linked to the inner Kdo unit, the high number of acid sugars and the highly branched core structure

  structure, Lipooligosaccharide, epitope, core oligosaccharide, Phytopathogenic bacteria, Lewis B antigen, Rhizobium rubi

  NCBI PubMed ID: 18574826
  Publication DOI: 10.1002/cbic.200800191
  Journal NLM ID: 100937360
  Publisher: Weinheim, Germany: Wiley Interscience
  Correspondence: decastro@unina.it
  Institutions: Department of Organic Chemistry and Biochemistry, University of Napoli 'Federico II', Via Cintia 4, 80126 Napoli (Italy), Fax: (+39) 81674393
  Methods: 13C NMR, 1H NMR, NMR-2D, methylation, GC-MS, 31P NMR, acid hydrolysis, alkaline degradation, MALDI-MS, composition analysis
  
   
  
  Rhizobium rubi T
  CSDB ID 22951 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_115136,IEDB_130650,IEDB_131182,IEDB_136044,IEDB_136045,IEDB_137472,IEDB_140630,IEDB_141794,IEDB_141806,IEDB_141807,IEDB_142488,IEDB_142489,IEDB_144562,IEDB_144998,IEDB_146664,IEDB_149554,IEDB_149556,IEDB_150899,IEDB_150948,IEDB_151531,IEDB_152214,IEDB_153553,IEDB_174333,IEDB_190606,IEDB_423153,IEDB_461719,IEDB_983931,SB_100,SB_137,SB_146,SB_154,SB_155,SB_165,SB_166,SB_187,SB_192,SB_195,SB_29,SB_7,SB_86,SB_88

• Article ID: 3471
  Gargiulo V, Garozzo D, Lanzetta R, Molinaro A, Sturiale L, De Castro C, Parrilli M "Rhizobium rubi(T): A Gram-Negative Phytopathogenic Bacterium Expressing the Lewis B Epitope on the Outer Core of its Lipooligosaccharide Fraction" - Chembiochem: a European Journal of Chemical Biology 9(11) (2008) 1830-1835
  

  The structure of the core oligosaccharide from the phytopathogenic bacterium Rhizobium rubi was deduced by combining information from complementary chemical approaches (alkaline and acid hydrolysis), similar to the 'overlap peptide' strategy. This structure is new and it contains two main oligosaccharide backbones that differ in the substitution degree of the external Kdo unit. The relevant feature shared by both oligosaccharides is the presence of a tetrasaccharide motif that is similar to the blood group Lewis B antigen (Le(B)). This epitope differs from Le(B) in the glycosidic configuration of the glucosamine unit (alpha and not beta) and in the occurrence of acetyls substituents at O3 and/or O4 of the galactose moiety. Other notable structural features are the location of the Dha residue, the presence of a α-glucose unit that is linked to the inner Kdo unit, the high number of acid sugars and the highly branched core structure

  structure, Lipooligosaccharide, epitope, core oligosaccharide, Phytopathogenic bacteria, Lewis B antigen, Rhizobium rubi

  NCBI PubMed ID: 18574826
  Publication DOI: 10.1002/cbic.200800191
  Journal NLM ID: 100937360
  Publisher: Weinheim, Germany: Wiley Interscience
  Correspondence: decastro@unina.it
  Institutions: Department of Organic Chemistry and Biochemistry, University of Napoli 'Federico II', Via Cintia 4, 80126 Napoli (Italy), Fax: (+39) 81674393
  Methods: 13C NMR, 1H NMR, NMR-2D, methylation, GC-MS, 31P NMR, acid hydrolysis, alkaline degradation, MALDI-MS, composition analysis
  
   
  
  Rhizobium rubi T
  CSDB ID 22954 (all data & tools)