Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_130646,IEDB_130654,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145669,IEDB_149557,IEDB_150092,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_174333,IEDB_190606,IEDB_423128,IEDB_461720,IEDB_983930,SB_157,SB_165,SB_166,SB_187,SB_195,SB_30,SB_44,SB_67,SB_7,SB_72,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 1730 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_130646,IEDB_130650,IEDB_130654,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_140088,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_142489,IEDB_144562,IEDB_144998,IEDB_145669,IEDB_146664,IEDB_149557,IEDB_150092,IEDB_151531,IEDB_152214,IEDB_174333,IEDB_190606,IEDB_2189046,IEDB_2189047,IEDB_461720,IEDB_983931,SB_157,SB_165,SB_166,SB_187,SB_192,SB_195,SB_30,SB_7,SB_86,SB_88

• Article ID: 53
  Edwards NJ, Monteiro MA, Walsh EJ, Moran AP, Roberts IS, High NJ "Lewis X structures in the O antigen side-chain promote adhesion of Helicobacter pylori to the gastric epithelium" - Molecular Microbiology 35(6) (2000) 1530-1539
  

  Helicobacter pylori NCTC11637 expresses a lipopolysaccharide (LPS) that comprises an O antigen side-chain with structural homology to the human blood group antigen Lewis X (Le(x)). The role of this molecule in adhesion of H. pylori to gastric epithelial cells was investigated. Mutants expressing truncated LPS structures were generated through insertional mutagenesis of rfbM and galE; genes encode GDP mannose pyrophosphorylase and galactose epimerase respectively. Compositional and structural analysis revealed that the galE mutant expressed a rough LPS that lacked an O antigen side-chain. In contrast, an O antigen side-chain was still synthesized by the rfbM mutant, but it lacked fucose and no longer reacted with anti-Le(x) monoclonal antibodies (Mabs). The ability of these mutants to bind to paraffin-embedded sections from the antrum region of a human stomach was assessed. Adhesion of the wild type was characterized by tropic binding to the apical surface of mucosal epithelial cells and cells lining gastric pits. In contrast, both the rfbM and galE mutants failed to demonstrate tropic binding and adhered to the tissue surface in a haphazard manner. These results indicate that LPS and, more specifically, Le(x) structures in the O antigen side-chain play an important role in targeting H. pylori to specific cell lineages within the gastric mucosa. The role of Le(x) in this interaction was confirmed by the tropic binding of synthetic Le(x), conjugated to latex beads, to gastric tissue. The observed pattern of adhesion was indistinguishable from that of wild-type H. pylori

  NCBI PubMed ID: 10760152
  Journal NLM ID: 8712028
  Publisher: Blackwell Publishing
  Correspondence: Nicky.High@man.ac
  Institutions: School of Biological Sciences, The University of Manchester, Manchester, UK, Institute for Biological Sciences, National Research Council, Ottawa, ON, Canada, Institute of Pathology, University of Erlangen-Nuremberg, Erlangen, Germany, Department of Microbiology, National University of Ireland Galway, Galway, Ireland
  
   
  
  Helicobacter pylori NCTC 11637
  CSDB ID 2031 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_130650,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_140088,IEDB_141807,IEDB_142488,IEDB_142489,IEDB_144562,IEDB_144998,IEDB_145669,IEDB_146664,IEDB_150092,IEDB_151531,IEDB_152214,IEDB_158538,IEDB_174333,IEDB_2189046,IEDB_2189047,IEDB_983931,SB_192,SB_86

• Article ID: 53
  Edwards NJ, Monteiro MA, Walsh EJ, Moran AP, Roberts IS, High NJ "Lewis X structures in the O antigen side-chain promote adhesion of Helicobacter pylori to the gastric epithelium" - Molecular Microbiology 35(6) (2000) 1530-1539
  

  Helicobacter pylori NCTC11637 expresses a lipopolysaccharide (LPS) that comprises an O antigen side-chain with structural homology to the human blood group antigen Lewis X (Le(x)). The role of this molecule in adhesion of H. pylori to gastric epithelial cells was investigated. Mutants expressing truncated LPS structures were generated through insertional mutagenesis of rfbM and galE; genes encode GDP mannose pyrophosphorylase and galactose epimerase respectively. Compositional and structural analysis revealed that the galE mutant expressed a rough LPS that lacked an O antigen side-chain. In contrast, an O antigen side-chain was still synthesized by the rfbM mutant, but it lacked fucose and no longer reacted with anti-Le(x) monoclonal antibodies (Mabs). The ability of these mutants to bind to paraffin-embedded sections from the antrum region of a human stomach was assessed. Adhesion of the wild type was characterized by tropic binding to the apical surface of mucosal epithelial cells and cells lining gastric pits. In contrast, both the rfbM and galE mutants failed to demonstrate tropic binding and adhered to the tissue surface in a haphazard manner. These results indicate that LPS and, more specifically, Le(x) structures in the O antigen side-chain play an important role in targeting H. pylori to specific cell lineages within the gastric mucosa. The role of Le(x) in this interaction was confirmed by the tropic binding of synthetic Le(x), conjugated to latex beads, to gastric tissue. The observed pattern of adhesion was indistinguishable from that of wild-type H. pylori

  NCBI PubMed ID: 10760152
  Journal NLM ID: 8712028
  Publisher: Blackwell Publishing
  Correspondence: Nicky.High@man.ac
  Institutions: School of Biological Sciences, The University of Manchester, Manchester, UK, Institute for Biological Sciences, National Research Council, Ottawa, ON, Canada, Institute of Pathology, University of Erlangen-Nuremberg, Erlangen, Germany, Department of Microbiology, National University of Ireland Galway, Galway, Ireland
  
   
  
  Helicobacter pylori galE mutant
  CSDB ID 2122 (all data & tools)

Show legend Show as text

Structure type: polymer chemical repeating unit
Compound class: O-polysaccharide
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145669,IEDB_150092,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_174333,IEDB_983930,SB_44,SB_67,SB_72,SB_86

• Article ID: 199
  Vinogradov EV, Pantophlet R, Brade H, Holst O "Structural and serological characterisation of the O-antigenic polysaccharide of the lipopolysaccharide from Acinetobacter strain 96 (DNA group 11)" - Journal of Endotoxin Research 7(2) (2001) 113-118
  

  A polysaccharide containing D-Manp, L-Fucp (6-deoxygalactopyranose, fucose) and D-GlcpNAc was isolated by mild acid hydrolysis, followed by gel-permeation chromatography, from the lipopolysaccharide derived from Acinetobacter strain 96 (DNA group 11). The structure of the O-antigen was determined by compositional analysis and NMR spectroscopy of the polysaccharide as: [carbohydrate structure see text] A monoclonal antibody obtained after immunization of mice with heat-killed bacteria of Acinetobacter strain 96 was shown to bind to the O-antigen and did not cross-react with any Acinetobacter O-antigen of known structure.

  Lipopolysaccharide, NMR, antigen, structure, blotting, chemistry, Bacterial, human, DNA, strain, structural, polysaccharide, O-antigen, analysis, O antigen, group, O-antigenic, O-antigenic polysaccharide, acid, Acinetobacter, antibodies, antibody, epitope, monoclonal, monoclonal antibodies, monoclonal antibody, animal, antigens, Carbohydrate Sequence, immunization, immunology, mice, Inbred BALB C, Molecular Sequence Data, epitopes, NMR spectroscopy, Cross Reactions, O antigens, O-antigens, bacteria, hydrolysis, serological, biological, Magnetic Resonance Spectroscopy, spectroscopy, gel permeation chromatography, Western, Carbohydrate Conformation, chromatography, classification, fucose, serotyping

  NCBI PubMed ID: 11521091
  Journal NLM ID: 9433350
  Publisher: Maney Publishing
  Correspondence: oholst@fzborstel.de
  Institutions: Institute for Biological Sciences, NRCC, Ottawa, Ontario, Canada, The Scripps Research Institute, Department of Immunology, La Jolla, California, USA, Divisions of Medical and Biochemical Microbiology, Analytical Biochemistry, Research Center Borstel, Borstel, Germany
  Methods: NMR-2D, NMR, composition analysis
  
   
  
  Acinetobacter sp. 96 (DNA group 11)
  CSDB ID 5530 (all data & tools)
• Article ID: 4328
  Knirel YA "Structure of O-antigens" - Book: Bacterial lipopolysaccharides: Structure, chemical synthesis, biogenesis and interaction with host cells (2011) Chapter 3, 41-115
  

  The lipopolysaccharide (LPS) is the major constituent of the outer leaflet of the outer membrane of Gram-negative bacteria. Its lipid A moiety is embedded in the membrane and serves as an anchor for the rest of the LPS molecule. The outermost repetitive glycan region of the LPS is linked to the lipid A through a core oligosaccharide (OS), and is designated as the O-specific polysaccharide (O-polysaccharide, OPS) or O-antigen. The O-antigen is the most variable portion of the LPS and provides serological specificity, which is used for bacterial serotyping. The OPS also provides protection to the microorganisms from host defenses such as complement mediated killing and phagocytosis, and is involved in interactions of bacteria with plants and bacteriophages. Studies of the OPSs ranging from the elucidation of their chemical structures and conformations to their biological and physico-chemical properties help improving classification schemes of Gram-negative bacteria. Furthermore, these studies contributed to a better understanding of the mechanisms of pathogenesis of infectious diseases, as well as provided information to develop novel vaccines and diagnostic reagents.

  Lipopolysaccharide, synthesis, lipopolysaccharides, structure, Bacterial, host, O-antigen, O antigen, cell, O antigens, O-antigens, chemical, interaction, cells, PDF, chemical synthesis, biogenesis

  Publication DOI: 10.1007/978-3-7091-0733-1_3
  Publisher: Springer
  Correspondence: knirel@ioc.ac.ru
  Editors: Knirel YA, Valvano MA
  Institutions: Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia
  
   
  
  Acinetobacter sp. 96
  CSDB ID 27765 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: Lewis X, Lewis x antigen
Compound class: LOS
Contained glycoepitopes: IEDB_130646,IEDB_130654,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_145669,IEDB_149557,IEDB_150092,IEDB_151531,IEDB_152214,IEDB_174333,IEDB_190606,IEDB_461720,SB_157,SB_165,SB_166,SB_187,SB_195,SB_30,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 6940 (all data & tools)
• Article ID: 237
  Ge Z, Nora WC, Palcic MM, Taylor DE "Cloning and heterologous expression of an a-1,3-fucosyltransferase gene from the gastric pathogen Helicobacter pylori" - Journal of Biological Chemistry 272(34) (1997) 21357-21363
  

  Helicobacter pylori is an important human pathogen which causes both gastric and duodenal ulcers and is also associated with gastric cancer and lymphoma. This microorganism has been shown to express cell surface glycoconjugates including Lewis X and Lewis Y. These bacterial oligosaccharides are structurally similar to tumor-associated carbohydrate antigens found in mammals. In this study, we report the cloning of a novel a1,3-fucosyltranferase gene (HpfucT) involved in the biosynthesis of LeX within H. pylori. The deduced amino acid sequence of HpfucT consists of 478 residues with the calculated molecular mass of 56,194 daltons, which is approximately 100 amino acids longer than known mammalian a1,3/1,4 fucosyltransferases. The 52-kDa protein encoded by HpfucT was expressed in Escherichia coli CSRDE3 cells and gave rise to a1,3-fucosyltransferase activity but neither a1,4-fucosyltransferase nor a1,2-fucosyltransferase activity as characterized by radiochemical assays and cappilary zone electrophoresis. Truncation of the C-terminal 100 amino acids if HpfucT abolished the enzyme activity. An approximately 72-amino acids region of HpFucT exhibits significant sequence identity (40-45%) with the highly conserved C-terminal catalytic domain among known mammalian and chicken a1,3-fucosyltranserase. In addition, several structural features unique to HpfucT, including 10 direct repeats of seven amino acids and the lack of the transmembrane segment typical for known eukaryotic a1,3-fucosyltransferases, were revealed. Notably, the repeat region contains a leucine zipper motif previously demonstrated to be responsible for dimerization of various basic region-leucine zipper proteins, suggesting that the HpfucT protein could form dimers.

  lipopolysaccharides, expression, gene, cloning, bacteria, biological, sequencing, Helicobacter pylori, pathogen, gastric, genome, Helicobacter, heterologous

  NCBI PubMed ID: 9261149
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: diane.taylor@ualberta.ca
  Institutions: Departement of Medical Microbiology and Immunology, Department of Chemistry, Departement of Biological Sciences, University of Alberta, Edmonton, AB, Canada
  
   
  
  Helicobacter pylori
  CSDB ID 6919 (all data & tools)
• Article ID: 3186
  Nilsson C, Skoglund A, Moran AP, Annuk H, Engstrand L, Normark S "An enzymatic ruler modulates Lewis antigen glycosylation of Helicobacter pylori LPS during persistent infection" - Proceedings of the National Academy of Sciences of the USA 103(8) (2006) 2863-2868
  

  Helicobacter pylori persistently colonizes about half the human population and contributes to the development of peptic ulcer disease and gastric cancer. This organism has evolved means to structurally alter its surface characteristics to evade innate and adaptive immune responses. H. pylori produces LPS O-antigen units that can be posttranslationally fucosylated to generate Lewis antigens, structures also found on human epithelial cells. We demonstrate an extensive diversity of Lewis x and Lewis y expression in LPS O-antigen units, occurring over time and in different regions of the human stomach. Lewis expression patterns were correlated with the on/off status of the three fucosyltransferases (FucT), FutA, FutB, and FutC, which are regulated via slipped-strand mispairing in intragenic polyC tract regions of the corresponding genes. The α1,3-FucT, FutA and FutB, each contain a C-terminal heptad repeat region, consisting of a variable number of DD/NLRV/INY tandem repeats. Variations in the number of heptad repeats correlated to the sizes of O-antigen polymers to become decorated by fucose residues. Our data support a molecular ruler mechanism for how H. pylori varies its LPS fucosylation pattern, where one heptad repeat in the enzyme corresponds to one N-acetyl-β-lactosamine unit in the O-antigen polysaccharide.

  Phase variation, chronic, human stomach

  NCBI PubMed ID: 16477004
  Publication DOI: 10.1073/pnas.0511119103
  Journal NLM ID: 7505876
  Publisher: National Academy of Sciences
  Correspondence: christina.nilsson@mtc.ki.se
  Institutions: Department of Microbiology, National University of Ireland, Galway, Ireland, Microbiology and Tumor Biology Center, Karolinska Institutet, 171 77 Stockholm, Sweden, Department of Bacteriology, Swedish Institute for Infectious Disease Control, 171 82 Solna, Sweden
  Methods: serological methods, genetic methods
  
   
  
  Helicobacter pylori
  CSDB ID 20204 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: 3'-sialyl-LeX
Contained glycoepitopes: IEDB_130646,IEDB_130654,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_140108,IEDB_140122,IEDB_141586,IEDB_141794,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_145669,IEDB_146100,IEDB_149174,IEDB_149557,IEDB_150092,IEDB_150933,IEDB_151531,IEDB_152214,IEDB_174333,IEDB_190606,IEDB_241127,IEDB_423120,IEDB_461720,SB_115,SB_116,SB_129,SB_131,SB_157,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_195,SB_30,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 6942 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: 3'-sulfo-LeX
Contained glycoepitopes: IEDB_130646,IEDB_130654,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_145669,IEDB_149557,IEDB_150092,IEDB_151531,IEDB_152214,IEDB_174333,IEDB_190606,IEDB_423162,IEDB_461720,SB_118,SB_157,SB_165,SB_166,SB_187,SB_195,SB_30,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 6944 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: 6'-sulfo-sialyl-LeX
Contained glycoepitopes: IEDB_130646,IEDB_130654,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_140108,IEDB_140122,IEDB_141586,IEDB_141794,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_145669,IEDB_146100,IEDB_149174,IEDB_149557,IEDB_150092,IEDB_150933,IEDB_151531,IEDB_152214,IEDB_174333,IEDB_190606,IEDB_241127,IEDB_423120,IEDB_461720,SB_115,SB_116,SB_129,SB_131,SB_157,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_195,SB_30,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 6946 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: 6-sulfo-sialyl-LeX
Contained glycoepitopes: IEDB_130646,IEDB_130654,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_140108,IEDB_140122,IEDB_141586,IEDB_141794,IEDB_141807,IEDB_142354,IEDB_142489,IEDB_144562,IEDB_145669,IEDB_146100,IEDB_149174,IEDB_149557,IEDB_150092,IEDB_150933,IEDB_151531,IEDB_152214,IEDB_174333,IEDB_190606,IEDB_241119,IEDB_241120,IEDB_241127,IEDB_423120,IEDB_461720,SB_115,SB_116,SB_128,SB_129,SB_131,SB_157,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_195,SB_30,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 6947 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: 6,6'-sulfo-sialyl-LeX
Contained glycoepitopes: IEDB_130646,IEDB_130654,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_140108,IEDB_140122,IEDB_141586,IEDB_141794,IEDB_141807,IEDB_142354,IEDB_142489,IEDB_144562,IEDB_145669,IEDB_146100,IEDB_149174,IEDB_149557,IEDB_150092,IEDB_150933,IEDB_151531,IEDB_152214,IEDB_174333,IEDB_190606,IEDB_241119,IEDB_241120,IEDB_241127,IEDB_423120,IEDB_461720,SB_115,SB_116,SB_128,SB_129,SB_131,SB_157,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_195,SB_30,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 6948 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: Lewis y antigen
Contained glycoepitopes: IEDB_130644,IEDB_130646,IEDB_130654,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142489,IEDB_143250,IEDB_144562,IEDB_145669,IEDB_149555,IEDB_149557,IEDB_149561,IEDB_150092,IEDB_150948,IEDB_151531,IEDB_152214,IEDB_153553,IEDB_174333,IEDB_190606,IEDB_461719,IEDB_461720,IEDB_461721,SB_147,SB_154,SB_157,SB_165,SB_166,SB_187,SB_195,SB_30,SB_34,SB_7,SB_86,SB_88

• Article ID: 237
  Ge Z, Nora WC, Palcic MM, Taylor DE "Cloning and heterologous expression of an a-1,3-fucosyltransferase gene from the gastric pathogen Helicobacter pylori" - Journal of Biological Chemistry 272(34) (1997) 21357-21363
  

  Helicobacter pylori is an important human pathogen which causes both gastric and duodenal ulcers and is also associated with gastric cancer and lymphoma. This microorganism has been shown to express cell surface glycoconjugates including Lewis X and Lewis Y. These bacterial oligosaccharides are structurally similar to tumor-associated carbohydrate antigens found in mammals. In this study, we report the cloning of a novel a1,3-fucosyltranferase gene (HpfucT) involved in the biosynthesis of LeX within H. pylori. The deduced amino acid sequence of HpfucT consists of 478 residues with the calculated molecular mass of 56,194 daltons, which is approximately 100 amino acids longer than known mammalian a1,3/1,4 fucosyltransferases. The 52-kDa protein encoded by HpfucT was expressed in Escherichia coli CSRDE3 cells and gave rise to a1,3-fucosyltransferase activity but neither a1,4-fucosyltransferase nor a1,2-fucosyltransferase activity as characterized by radiochemical assays and cappilary zone electrophoresis. Truncation of the C-terminal 100 amino acids if HpfucT abolished the enzyme activity. An approximately 72-amino acids region of HpFucT exhibits significant sequence identity (40-45%) with the highly conserved C-terminal catalytic domain among known mammalian and chicken a1,3-fucosyltranserase. In addition, several structural features unique to HpfucT, including 10 direct repeats of seven amino acids and the lack of the transmembrane segment typical for known eukaryotic a1,3-fucosyltransferases, were revealed. Notably, the repeat region contains a leucine zipper motif previously demonstrated to be responsible for dimerization of various basic region-leucine zipper proteins, suggesting that the HpfucT protein could form dimers.

  lipopolysaccharides, expression, gene, cloning, bacteria, biological, sequencing, Helicobacter pylori, pathogen, gastric, genome, Helicobacter, heterologous

  NCBI PubMed ID: 9261149
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: diane.taylor@ualberta.ca
  Institutions: Departement of Medical Microbiology and Immunology, Department of Chemistry, Departement of Biological Sciences, University of Alberta, Edmonton, AB, Canada
  
   
  
  Helicobacter pylori
  CSDB ID 6920 (all data & tools)
• Article ID: 3186
  Nilsson C, Skoglund A, Moran AP, Annuk H, Engstrand L, Normark S "An enzymatic ruler modulates Lewis antigen glycosylation of Helicobacter pylori LPS during persistent infection" - Proceedings of the National Academy of Sciences of the USA 103(8) (2006) 2863-2868
  

  Helicobacter pylori persistently colonizes about half the human population and contributes to the development of peptic ulcer disease and gastric cancer. This organism has evolved means to structurally alter its surface characteristics to evade innate and adaptive immune responses. H. pylori produces LPS O-antigen units that can be posttranslationally fucosylated to generate Lewis antigens, structures also found on human epithelial cells. We demonstrate an extensive diversity of Lewis x and Lewis y expression in LPS O-antigen units, occurring over time and in different regions of the human stomach. Lewis expression patterns were correlated with the on/off status of the three fucosyltransferases (FucT), FutA, FutB, and FutC, which are regulated via slipped-strand mispairing in intragenic polyC tract regions of the corresponding genes. The α1,3-FucT, FutA and FutB, each contain a C-terminal heptad repeat region, consisting of a variable number of DD/NLRV/INY tandem repeats. Variations in the number of heptad repeats correlated to the sizes of O-antigen polymers to become decorated by fucose residues. Our data support a molecular ruler mechanism for how H. pylori varies its LPS fucosylation pattern, where one heptad repeat in the enzyme corresponds to one N-acetyl-β-lactosamine unit in the O-antigen polysaccharide.

  Phase variation, chronic, human stomach

  NCBI PubMed ID: 16477004
  Publication DOI: 10.1073/pnas.0511119103
  Journal NLM ID: 7505876
  Publisher: National Academy of Sciences
  Correspondence: christina.nilsson@mtc.ki.se
  Institutions: Department of Microbiology, National University of Ireland, Galway, Ireland, Microbiology and Tumor Biology Center, Karolinska Institutet, 171 77 Stockholm, Sweden, Department of Bacteriology, Swedish Institute for Infectious Disease Control, 171 82 Solna, Sweden
  Methods: serological methods, genetic methods
  
   
  
  Helicobacter pylori
  CSDB ID 20538 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: tetramethylrhodamine
Contained glycoepitopes: IEDB_130646,IEDB_130654,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_140108,IEDB_140122,IEDB_141586,IEDB_141794,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_145669,IEDB_146100,IEDB_149174,IEDB_149557,IEDB_150092,IEDB_150933,IEDB_151531,IEDB_152214,IEDB_174333,IEDB_190606,IEDB_241127,IEDB_423120,IEDB_461720,SB_115,SB_116,SB_129,SB_131,SB_157,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_195,SB_30,SB_39,SB_68,SB_7,SB_84,SB_86,SB_88

• Article ID: 237
  Ge Z, Nora WC, Palcic MM, Taylor DE "Cloning and heterologous expression of an a-1,3-fucosyltransferase gene from the gastric pathogen Helicobacter pylori" - Journal of Biological Chemistry 272(34) (1997) 21357-21363
  

  Helicobacter pylori is an important human pathogen which causes both gastric and duodenal ulcers and is also associated with gastric cancer and lymphoma. This microorganism has been shown to express cell surface glycoconjugates including Lewis X and Lewis Y. These bacterial oligosaccharides are structurally similar to tumor-associated carbohydrate antigens found in mammals. In this study, we report the cloning of a novel a1,3-fucosyltranferase gene (HpfucT) involved in the biosynthesis of LeX within H. pylori. The deduced amino acid sequence of HpfucT consists of 478 residues with the calculated molecular mass of 56,194 daltons, which is approximately 100 amino acids longer than known mammalian a1,3/1,4 fucosyltransferases. The 52-kDa protein encoded by HpfucT was expressed in Escherichia coli CSRDE3 cells and gave rise to a1,3-fucosyltransferase activity but neither a1,4-fucosyltransferase nor a1,2-fucosyltransferase activity as characterized by radiochemical assays and cappilary zone electrophoresis. Truncation of the C-terminal 100 amino acids if HpfucT abolished the enzyme activity. An approximately 72-amino acids region of HpFucT exhibits significant sequence identity (40-45%) with the highly conserved C-terminal catalytic domain among known mammalian and chicken a1,3-fucosyltranserase. In addition, several structural features unique to HpfucT, including 10 direct repeats of seven amino acids and the lack of the transmembrane segment typical for known eukaryotic a1,3-fucosyltransferases, were revealed. Notably, the repeat region contains a leucine zipper motif previously demonstrated to be responsible for dimerization of various basic region-leucine zipper proteins, suggesting that the HpfucT protein could form dimers.

  lipopolysaccharides, expression, gene, cloning, bacteria, biological, sequencing, Helicobacter pylori, pathogen, gastric, genome, Helicobacter, heterologous

  NCBI PubMed ID: 9261149
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: diane.taylor@ualberta.ca
  Institutions: Departement of Medical Microbiology and Immunology, Department of Chemistry, Departement of Biological Sciences, University of Alberta, Edmonton, AB, Canada
  
   
  
  Helicobacter pylori
  CSDB ID 6922 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: (1->7)aXDDmanHeppII of core oligosaccharide -lipid A (ID 7468)
Trivial name: O-chain region
Contained glycoepitopes: IEDB_130644,IEDB_130646,IEDB_130654,IEDB_130655,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_140108,IEDB_140122,IEDB_141500,IEDB_141794,IEDB_141807,IEDB_142489,IEDB_143250,IEDB_144556,IEDB_144562,IEDB_145669,IEDB_147455,IEDB_149555,IEDB_149557,IEDB_149561,IEDB_150092,IEDB_150787,IEDB_150939,IEDB_150948,IEDB_151531,IEDB_152214,IEDB_153553,IEDB_158546,IEDB_158550,IEDB_174333,IEDB_190606,IEDB_2151203,IEDB_2189046,IEDB_461719,IEDB_461720,IEDB_461721,IEDB_952752,SB_147,SB_154,SB_157,SB_165,SB_166,SB_173,SB_187,SB_195,SB_30,SB_34,SB_7,SB_86,SB_88

• Article ID: 310
  Logan SM, Conlan JW, Monteiro MA, Wakarchuk WW, Altman E "Functional genomics of Helicobacter pylori: identification of a b-1,4 galactosyltransferase and generation of mutants with altered lipopolysaccharide" - Molecular Microbiology 35(5) (2000) 1156-1167
  

  A previously annotated open reading frame (ORF) (HP0826) from Helicobacter pylori was cloned and expressed in Escherichia coli cells and determined to be a β-1,4-galactosyltransferase that used GlcNAc as an acceptor. Mutational analysis in H. pylori strains demonstrated that this enzyme plays a key role in the biosynthesis of the type 2 N-acetyl-lactosamine (LacNAc) polysaccharide O-chain backbone, by catalysing the addition of Gal to GlcNAc. To examine the potential role of this O-chain structure in bacterial colonization of the host stomach, the mutation was introduced into H. pylori strain SS1 which is known to be capable of colonizing the gastric mucosa of mice. Compared with the parental strain, mutated SS1 was less efficient at colonizing the murine stomach.

  Lipopolysaccharide, mutants, Helicobacter pylori, galactosyltransferase, Helicobacter, genomics

  NCBI PubMed ID: 10712696
  Publication DOI: 10.1046/j.1365-2958.2000.01784.x
  Journal NLM ID: 8712028
  Publisher: Blackwell Publishing
  Correspondence: susan.logan@nrc.ca
  Institutions: Institute for Biological Sciences, National Research Council of Canada, Ottawa, Ontario, Canada, K1A OR6.
  Methods: methylation, FAB-MS
  
   
  
  Helicobacter pylori 26695
  CSDB ID 635 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: LPS
Trivial name: Lewis X, Lewis X antigen, Lewis X antigenic determinant, Lewis X determinant
Contained glycoepitopes: IEDB_130646,IEDB_130654,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_145669,IEDB_149557,IEDB_150092,IEDB_151531,IEDB_152214,IEDB_174333,IEDB_190606,IEDB_461720,SB_157,SB_165,SB_166,SB_187,SB_195,SB_30,SB_7,SB_86,SB_88

• Article ID: 322
  Martin SL, Edbrooke MR, Hodgman TC, van den Eijnden DH, Bird MI "Lewis X biosynthesis in Helicobacter pylori" - Journal of Biological Chemistry 272(34) (1997) 21349-21356
  

  The lipopolysaccharide of certain strains of Helicobacter pylori was recently shown to contain the Lewis X (Lex) trisaccharide (Galβ-1,4-(Fucα(1,3))-GlcNAc). Lex is an oncofetal antigen which appears on human gastric epithelium, and its mimicry by carbohydrate structures on the surface of H. pylori may play an important part in the interaction of this pathogen with its host. Potential roles for bacterial Lex in mucosal adhesion, immune evasion, and autoantibody induction have been proposed (Moran, A. P., Prendergast, M. M., and Appelmelk, B. J. (1996) FEMS Immunol. Med. Microbiol. 16, 105-115). In mammals, the final step of Lex biosynthesis is the α(1,3)-fucosylation of GlcNAc in a terminal Galβ(1→4)GlcNAc unit, and a corresponding GDP-fucose:N-acetylglucosaminyl α(1,3) fucosyltransferase (α(1,3)-Fuc-T) activity was recently discovered in H. pylori extracts. We used part of a human α(1, 3)-Fuc-T amino acid sequence to search an H. pylori genomic data base for related sequences. Using a probe based upon weakly matching data base sequences, we retrieved clones from a plasmid library of H. pylori DNA. DNA sequence analysis of the library clones revealed a gene which we have named fucT, encoding a protein with localized homology to the human α(1,3)-Fuc-Ts. We have demonstrated that fucT encodes an active Fuc-T enzyme by expressing the gene in Escherichia coli. The recombinant enzyme shows a strong preference for type 2 (e.g. LacNAc) over type 1 (e.g. lacto-N-biose) acceptors in vitro. Certain residues in a short segment of the H. pylori protein are completely conserved throughout the α(1,3)-Fuc-T family, defining an α(1,3)-Fuc-T motif which may be of use in identifying new fucosyltransferase genes.

  Lipopolysaccharide, biosynthesis, LPS, O-antigen, transferase, Helicobacter pylori, Helicobacter, L-fucose, Lewis, Lewis x

  NCBI PubMed ID: 9261148
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: slm17885@ggr.co.uk
  Institutions: Glycobiology Unit and the Advanced Technologies and Informatics Unit, GlaxoWellcome Medicines Research Centre, Stevenage, Herts SGl, NY, United Kingdom and the Department of Medical Chemistry, Vrije Universiteit, Amsterdam, The Netherlands.
  
   
  
  Helicobacter pylori
  CSDB ID 7497 (all data & tools)
• 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 284 (all data & tools)
• Article ID: 858
  Knirel YA, Kocharova NA, Hynes SO, Widmalm G, Andersen LP, Jansson P, Moran AP "Structural stuidies on lipopolysaccharides of serologically non-typable strains of Helicobacter pylori, AFI and 007, expressing Lewis antigenic determinants" - European Journal of Biochemistry 266(1) (1999) 123-131
  

  In contrast to other Helicobacter pylori strains, which have serologically detectable Lewis(x)+ (Le(x)) and Lewis(y)++ (++Le(y)) antigenic determinants in the O-specific polysaccharide chains of the lipopolysaccharides, H. pylori AF1 and 007 were non-typable with anti-Le(x) and anti-Le(y) antibodies. The carbohydrate portions of the lipopolysaccharides were liberated by mild acid hydrolysis and subsequently studied by sugar and methylation analyses, 1H NMR spectroscopy and electrospray ionization-mass spectrometry. Compared with each other, and with lipopolysaccharides of strains studied previously, the lipopolysaccharides of both AF1 and 007 showed similarities, but also differences, in the structures of the core region and O-specific polysaccharide chains. The O-specific polysaccharide chains of both strains consisted of a short or long polyfucosylated poly-N-acetyl-β-lactosamine chains, which were distinguished from those of other strains by a high degree of fucosylation producing a polymeric Le(x)chain terminating with Le(x) or Le(y) units:[sequence: see text] where n = 0 or 1 in strain AF1 and 0 in strain 007, m = 0-2, 6-7 in strain AF1 and m = 0-2, 6-7 or approximately 40 in strain 007, the medium-size species being predominant. Therefore, compared with other strains, the lack of reactivity of lipopolysaccharide of H. pylori AF1 and 007 with anti-Le(x) and anti-Le(y) may reflect the presence of a polymeric Le(x) chain and has important implications for serological and pathogenesis studies. As the substitution pattern of a D-glycero-D-manno-heptose residue in the outer core varied in the two strains, and an extended DD-heptan chain was present in some lipopolysaccharide species but not in others, this region was less conservative than the inner core region. The inner core L-glycero-D-manno-heptose region of both strains carried a 2-aminoethyl phosphate group, rather than a phosphate group, as reported previously for other H. pylori strains.

  Lipopolysaccharide, O-antigen, core oligosaccharide, O-specific polysaccharide, Helicobacter pylori

  NCBI PubMed ID: 10542057
  Journal NLM ID: 0107600
  Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
  Correspondence: knirel@ioc.ac.ru
  Institutions: Clinical Research Centre, Huddinge Hospital, Huddinge, Sweden
  Methods: methylation, NMR, ESI-MS
  
   
  
  Helicobacter pylori AFI, Helicobacter pylori 007
  CSDB ID 2935 (all data & tools)
• Article ID: 1008
  Moran AP, Knirel YA, Senchenkova SN, Widmalm G, Hynes SO, Jansson P "Phenotypic variation in molecular mimicry between Helicobacter pylori lipopolysaccharides and human gastric epithelial cell surface glycoforms. Acid-induced phase variation in Lewisx and Lewisy expression by H. pylori lipopolysaccharides" - Journal of Biological Chemistry 277(8) (2002) 5785-5795
  

  Helicobacter pylori is an important gastroduodenal pathogen of humans whose survival in the gastric environment below pH 4 is dependent on bacterial production of urease, whereas above pH 4 urease-independent mechanisms are involved in survival, but that remain to be elucidated fully. Previous structural investigations on the lipopolysaccharides (LPSs) of H. pylori have shown that the majority of these surface glycolipids express partially fucosylated, glucosylated, or galactosylated N-acetyllactosamine (LacNAc) O-polysaccharide chains containing Lewis(x) (Le(x)) and/or Lewis(y) (Le(y)), although some strains also express type 1 determinants, Lewis(a), Lewis(b), and H-1 antigen. In this study, we investigated acid-induced changes in the structure and composition of LPS and cellular lipids of the genome-sequenced strain, H. pylori 26695. When grown in liquid medium at pH 7, the O-chain consisted of a type 2 LacNAc polysaccharide, which was glycosylated with α-1-fucose at O-3 of the majority of N-acetylglucosamine residues forming Le(x) units, including chain termination by a Le(x) unit. However, growth in liquid medium at pH 5 resulted in production of a more complex O-chain whose backbone of type 2 LacNAc units was partially glycosylated with α-L-fucose, thus forming Le(x), whereas the majority of the nonfucosylated N-acetylglucosamine residues were substituted at O-6 by α-D-galactose residues, and the chain was terminated by a Le(y) unit. In contrast, detailed chemical analysis of the core and lipid A components of LPS and analysis of cellular lipids did not show significant differences between H. pylori 26695 grown at pH 5 and 7. Although putative molecular mechanisms affecting Le(x) and Le(y) expression have been investigated previously, this is the first report identifying an environmental trigger inducing phase variation of Le(x) and Le(y) in H. pylori that can aid adaptation of the bacterium to its ecological niche.

  Lipopolysaccharide, structure, Phase variation, phenotype, O-antigen, Helicobacter pylori, Lewis x, blood group antigens, Lewis y

  NCBI PubMed ID: 11741906
  Publication DOI: 10.1074/jbc.M108574200
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: pererik.jansson@kfc.hs.sll.se
  Institutions: Department of Organic Chemistry, Arrhenius Laboratory, Stockholm University, Stockholm, Sweden, N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, Department of Microbiology, National University of Ireland, Galway, Ireland, Karolinska Institute, Clinical Research Centre, Huddinge University Hospital, Huddinge, Sweden
  Methods: methylation, NMR, ESI-MS
  
   
  
  Helicobacter pylori 26695
  CSDB ID 3558 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: O-chain-core oligosaccharide-lipid A
Trivial name: Lewis Y
Contained glycoepitopes: IEDB_130644,IEDB_130646,IEDB_130654,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142489,IEDB_143250,IEDB_144562,IEDB_145669,IEDB_149555,IEDB_149557,IEDB_149561,IEDB_150092,IEDB_150948,IEDB_151531,IEDB_152214,IEDB_153553,IEDB_174333,IEDB_190606,IEDB_461719,IEDB_461720,IEDB_461721,SB_147,SB_154,SB_157,SB_165,SB_166,SB_187,SB_195,SB_30,SB_34,SB_7,SB_86,SB_88

• Article ID: 310
  Logan SM, Conlan JW, Monteiro MA, Wakarchuk WW, Altman E "Functional genomics of Helicobacter pylori: identification of a b-1,4 galactosyltransferase and generation of mutants with altered lipopolysaccharide" - Molecular Microbiology 35(5) (2000) 1156-1167
  

  A previously annotated open reading frame (ORF) (HP0826) from Helicobacter pylori was cloned and expressed in Escherichia coli cells and determined to be a β-1,4-galactosyltransferase that used GlcNAc as an acceptor. Mutational analysis in H. pylori strains demonstrated that this enzyme plays a key role in the biosynthesis of the type 2 N-acetyl-lactosamine (LacNAc) polysaccharide O-chain backbone, by catalysing the addition of Gal to GlcNAc. To examine the potential role of this O-chain structure in bacterial colonization of the host stomach, the mutation was introduced into H. pylori strain SS1 which is known to be capable of colonizing the gastric mucosa of mice. Compared with the parental strain, mutated SS1 was less efficient at colonizing the murine stomach.

  Lipopolysaccharide, mutants, Helicobacter pylori, galactosyltransferase, Helicobacter, genomics

  NCBI PubMed ID: 10712696
  Publication DOI: 10.1046/j.1365-2958.2000.01784.x
  Journal NLM ID: 8712028
  Publisher: Blackwell Publishing
  Correspondence: susan.logan@nrc.ca
  Institutions: Institute for Biological Sciences, National Research Council of Canada, Ottawa, Ontario, Canada, K1A OR6.
  Methods: methylation, FAB-MS
  
   
  
  Helicobacter pylori 26695, Helicobacter pylori SS1
  CSDB ID 7539 (all data & tools)