Found 59 structures.
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1. Compound ID: 857
Structure type: oligomer
Contained glycoepitopes: IEDB_130646,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_149555,IEDB_150948,IEDB_151531,IEDB_152214,IEDB_153553,IEDB_174333,IEDB_190606,IEDB_461719,SB_154,SB_165,SB_166,SB_187,SB_195,SB_30,SB_34,SB_7,SB_86,SB_88
The structure is contained in the following publication(s):
- 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: 9261149Journal NLM ID: 2985121RPublisher: 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
- Article ID: 3235
Lin SW, Yuan TM, Li JR, Lin CH "Carboxyl Terminus of Helicobacter pylori a1,3-Fucosyltransferase Determines the Structure and Stability" -
Biochemistry 45(26) (2006) 8108-8116
Helicobacter pylori is well known as the primary cause of gastritis, duodenal ulcers, and gastric cancer. The pathogenic bacteria produces Lewis x and Lewis y epitopes in the O-antigens of lipopolysaccharides to mimic the carbohydrate antigens of gastric epithelial cells to avoid detection by the host's immune system. The enzyme α1,3-fucosyltransferase from H. pylori catalyzes the glycosyl addition of fucose from the donor GDP-fucose to the acceptor N-acetyllactosamine. The poor solubility of the enzyme was resolved by systematic deletion of the C-terminus. We report here the first structural analysis using CD spectroscopy and analytical ultracentrifugation. The results indicate that up to 80 residues, including the tail rich in hydrophobic and positively charged residues (sequence 434-478) and 5 of the 10 tandem repeats of 7 amino acids each (399-433), can be removed without significant change in structure and catalysis. Half of the heptad repeats are required to maintain both the secondary and native quaternary structures. Removal of more residues in the C-terminus led to major structural alteration, which was correlated with the loss of enzymatic activity. In accordance with the thermal denaturation studies, the results support the idea that a higher number of tandem repeats functioning to facilitate a dimeric structure helps to prevent the protein from unfolding during incubation at higher temperatures.
Lipopolysaccharide, structure, O-antigen, epitope, Helicobacter pylori, fucose, Lewis x, Lewis y, a1, 3-Fucosyltransferase
NCBI PubMed ID: 16800635Publication DOI: 10.1021/bi0601297Journal NLM ID: 0370623Publisher: American Chemical Society
Correspondence: chunhung@gate.sinica.edu.tw
Institutions: Institute of Biological Chemistry and Genomics Research Center, Academia Sinica, No. 128 Academia Road Section 2, Nan-Kang, Taipei 11529, Taiwan, and Institute of Biochemical Sciences, College of Life Science, National Taiwan University, Taipei 10617, Taiwan, Institute of Biological Chemistry and Genomics Research Center, Academia Sinica, No. 128 Academia Road Section 2, Nan-Kang, Taipei 11529, Taiwan, Institute of Biochemical Sciences, College of Life Science, National Taiwan University, Taipei 10617, Taiwan
Methods: biochemical methods
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2. Compound ID: 858
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
The structure is contained in the following publication(s):
- 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: 9261149Journal NLM ID: 2985121RPublisher: 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
- 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: 16477004Publication DOI: 10.1073/pnas.0511119103Journal NLM ID: 7505876Publisher: 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
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3. Compound ID: 1024
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a-L-Fucp-(1-3)-+
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a-L-Fucp-(1-2)-{{{-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-}}}D-gro-a-D-manHepp-(1-2)-D-gro-a-D-manHepp-(1-6)-D-gro-a-D-manHepp-(1--/(1->7)aXDDmanHeppII of core oligosaccharide -lipid A (ID 7468)/ |
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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
The structure is contained in the following publication(s):
- 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: 10712696Publication DOI: 10.1046/j.1365-2958.2000.01784.xJournal NLM ID: 8712028Publisher: 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
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4. Compound ID: 1067
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a-L-Fucp-(1-3)-+
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a-L-Fucp-(1-2)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1--/O-chain-core oligosaccharide-lipid A/ |
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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
The structure is contained in the following publication(s):
- 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: 10712696Publication DOI: 10.1046/j.1365-2958.2000.01784.xJournal NLM ID: 8712028Publisher: 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
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5. Compound ID: 1098
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a-L-Fucp-(1-3)-+
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a-L-Fucp-(1-2)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1--/core/ |
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Structure type: oligomer
Aglycon: core
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
The structure is contained in the following publication(s):
- 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: 9565568Journal NLM ID: 2985121RPublisher: 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
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6. Compound ID: 1309
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a-L-Fucp-(1-3)-+
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a-L-Fucp-(1-2)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1--/rest of the lipopolysaccharide/ |
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Structure type: oligomer
Aglycon: rest of the lipopolysaccharide
Trivial name: Lewis Y oligosaccharide
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
The structure is contained in the following publication(s):
- Article ID: 411
Wang G, Rasko DA, Sherburne R, Taylor DE "Molecular genetic basis for the variable expression of Lewis Y in Helicobacter pylori: analysis of the a(1,2)fucosyltransferase gene" -
Molecular Microbiology 31(4) (1999) 1265-1274
Helicobacter pylori lipopolysaccharides (LPS) express human oncofetal antigens Lewis X and Lewis Y. The synthesis of Lewis Y involves the actions of α (1,3) and α (1,2) fucosyltransferases (FucTs). Here, we report the molecular cloning and characterization of genes encoding H. pylori α (1,2) FucT (Hp fucT2) from various H. pylori strains. We constructed Hp fucT2 knock-out mutants and demonstrated the loss of Lewis Y production in these mutants by enzyme-linked immunosorbent assay (ELISA) and immunoelectron microscopy. The Hp fucT2 gene contains a hypermutable sequence [poly (C) and TAA repeats], which provides a possibility of frequent shifting into and out of coding frame by a polymerase slippage mechanism. Thus, the Hp fucT2 gene displays two major genotypes, consisting of either a single full-length open reading frame (ORF; as in the strain UA802) or truncated ORFs (as in the strain 26695). In vitro expression of Hp fucT2 genes demonstrated that both types of the gene have the potential to produce the full-length protein. The production of the full-length protein by the 26695 fucT2 gene could be attributed to translational-1 frameshifting, as a perfect translation frameshift cassette resembling that of the Escherichia coli dnaX gene is present. Examination of the strain UA1174 revealed that its fucT2 gene has a frameshifted ORF at the DNA level, which cannot be compensated by translation frameshifting, accounting for its Lewis Y off phenotype. In another strain, UA1218, the fucT2 gene is apparently turned off because of the loss of its promoter. Based on these data, we proposed a model for the variable expression of Lewis Y by H. pylori, in which regulation at the level of replication slippage (mutation), transcription and translation of the fucT2 gene may all be involved
biosynthesis, expression, gene, analysis, Helicobacter pylori, Helicobacter, Lewis, antigenic variation, fucosyltransferase, Lewis y
NCBI PubMed ID: 10096092Journal NLM ID: 8712028Publisher: Blackwell Publishing
Correspondence: diane.taylor@ualberta.ca
Institutions: Department of Medical Microbiology and Immunology, University of Alberta, Edmonton, AB, Canada
Methods: DNA sequencing, SDS-PAGE, ELISA, genetic methods, immunoblotting, immunoelectron microscopy
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7. Compound ID: 1450
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a-L-Fucp-(1-3)-+ a-L-Fucp-(1-3)-+ a-L-Fucp-(1-3)-+
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a-L-Fucp-(1-2)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-{{{-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-}}}{{{-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-}}}b-D-Galp-(1-4)-b-D-GlcpNAc-(1--/(1->7)aDDHepp-core oligosaccharide/ |
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Structure type: oligomer
Aglycon: (1->7)aDDHepp-core oligosaccharide
Trivial name: O-side chain antigen
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_150939,IEDB_150948,IEDB_151531,IEDB_152214,IEDB_153553,IEDB_158550,IEDB_174333,IEDB_190606,IEDB_2151203,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
The structure is contained in the following publication(s):
- Article ID: 461
Moran AP, Shiberu B, Ferris JA, Knirel YA, Senchenkova SN, Perepelov AV, Jansson P, Goldberg JB "Role of Helicobacter pylori rfaJ genes (HP0159 and HP1416) in lipopolysaccharide synthesis" -
FEMS Microbiology Letters 241(1) (2004) 57-65
The genome of Helicobacter pylori 26695 has been sequenced and the lipopolysaccharide (LPS) O sidechain of this strain has been shown to express both Lewis x and Lewis y units. To determine the role of HP0159 and HP1416, genes recognized as rfaJ homologs and implicated in LPS synthesis, isogenic mutants of H. pylori 26695 were generated. The LPS of mutant 26695::HP0159Kan did not express either Lewis epitope as detected by immunoblotting, whereas the control strain and 26695::HP1416Kan produced both epitopes. Structural analysis of the LPS of the mutants showed that HP0159 encodes an α(1,2/3)-glucosyltransferase whereas HP1416 encodes an α(1,2/4)-glucosyltransferase.
Lipopolysaccharide, core oligosaccharide, Helicobacter pylori, glycosyltransferase, Lewis antigen
NCBI PubMed ID: 15556710Publication DOI: 10.1016/j.femsle.2004.10.004Journal NLM ID: 7705721Publisher: Blackwell Publishing
Correspondence: jbg2b@virginia.edu
Institutions: Department of Microbiology, National University of Ireland, Galway, Ireland
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8. Compound ID: 1902
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a-L-Fucp-(1-3)-+
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?%a-L-Fucp-(1-2)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1--/LPS/ |
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Structure type: oligomer
Aglycon: LPS
Contained glycoepitopes: IEDB_130644,IEDB_130646,IEDB_130654,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142489,IEDB_143250,IEDB_144562,IEDB_145669,IEDB_147455,IEDB_149555,IEDB_149557,IEDB_149561,IEDB_150092,IEDB_150787,IEDB_150948,IEDB_151531,IEDB_152214,IEDB_153553,IEDB_158546,IEDB_174333,IEDB_190606,IEDB_2151203,IEDB_461719,IEDB_461720,IEDB_461721,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
The structure is contained in the following publication(s):
- Article ID: 614
Aspinall GO, Monteiro MA, Shaver RT, Kurjanczyk LA, Penner JL "Lipopolysaccharides of Helicobacter pylori serogroups O:3 and O:6. Structures of a class of lipopolysaccharides with reference to the location of oligomeric units of D-glycero-a-D-manno-heptose residues" -
European Journal of Biochemistry 248 (1997) 592-601
Lipopolysaccharides (LPS) from antigenically different strains assigned to serogroups O:3 and O:6 of Helicobacter pylori were isolated as water-soluble material of high Mr and as water-insoluble gels of low M,. Chemical and spectroscopic analyses of the soluble LPS and oligosaccharides liberated from the water-insoluble gels led to proposed structures with Lewis (Le) antigen determinants terminating regular repeating units of different types, linked in turn to inner core regions of invariable structure. The O:6 LPS has two populations of related molecules with chains of 3-linked D-glycero-a-D-manno-heptose residues similar to those in the MO19 strain, one with and the other without a single terminal Lewis (LeY') epitope. In contrast, in the O:3 LPS, Lewis (LeX and LeY) epitopes terminate a partially fucosylated N-acetyllactosaminoglycan, but a heptan chain similar to that in the O:6 LPS was shown to connect the outer chains to the inner core. These LPS provide examples of the molecular mimicry of cell-surface glycoconjugates. Structural variations of LPS between strains, and differences in some aspects of structure within strains, between high Mr and low Mr LPS indicate a class of LPS whose mechanisms of biosynthesis lead to overall architectures different from those characteristic of most LPS from enteric bacteria.
Lipopolysaccharide, LPS, core, O-antigen, core oligosaccharide, molecular mimicry, Helicobacter pylori, D-glycero-D-manno-heptose, Helicobacter, molecular mimicry.
NCBI PubMed ID: 9346320Journal NLM ID: 0107600Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
Institutions: Department of Chemistry, York University, Toronto, Ontario, Canada, Depanment of Chemistry, York University, Toronto, Ontario, Canada, Department of Microbiology, University of Toronto, Ontario, Canada
Methods: FAB-MS
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9. Compound ID: 1953
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a-D-Glcp-(1-3)-a-D-Glcp-(1-4)-b-D-Galp-(1-7)-+
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a-L-Fucp-(1-3)-+ a-L-Fucp-(1-3)-+ a-L-Fucp-(1-3)-+ a-L-Fucp-(1-3)-+ | P-7)-+
| | | | | |
a-L-Fucp-(1-2)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-7)-D-gro-a-D-manHepp-(1-2)-D-gro-a-D-manHepp-(1-2)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-Kdo |
Show graphically |
Structure type: oligomer
Contained glycoepitopes: IEDB_130644,IEDB_130646,IEDB_130650,IEDB_130654,IEDB_130655,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_140088,IEDB_140108,IEDB_140122,IEDB_141500,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_142489,IEDB_143250,IEDB_144556,IEDB_144562,IEDB_144998,IEDB_145669,IEDB_146664,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_2189047,IEDB_461719,IEDB_461720,IEDB_461721,IEDB_952752,IEDB_983931,SB_147,SB_154,SB_157,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_34,SB_7,SB_86,SB_88
The structure is contained in the following publication(s):
- Article ID: 613
Aspinall GO, Monteiro MA "Lipopolysaccharides of Helicobacter pylori strains P466 and MO19: Structures of the O antigen and core oligosaccharide regions" -
Biochemistry 35 (1996) 2498-2504
Lipopolysaccharides (LPS) from phenol-water extraction of dyspeptic (P466) and asymptomatic (MO19) strains of Helicobacter pylori were each isolated as water-soluble material of high relative molecular mass (high Mr) and as water-insoluble gels of low Mr. Chemical and spectroscopic analyses of the soluble LPS and oligosaccharides liberated from the water-insoluble gels led to proposed structures for chains comprising the O antigen, intervening, and core regions. As in the LPS from the type strain NCTC11637 [Aspinall, G. O., et al. (1996) Biochemistry 35, 000], the O antigen region of the P466 LPS is characterized by the presence of extended chains with fucosylated and nonfucosylated N-acetyllactosamine units, the former carrying a-L-fucopyranose units at O-3 of b-D-GlcNAc residues. This structure differs from that of the type strain in termination of the O chain by a Lewisy (Ley) antigenic determinant [a-LFuc(1-2)b-D-Gal(1-4)[a-L-Fuc(1-3)]b-D-GlcNAc] but also has internal Lewisx (Lex) units. The inner core region of the P466 LPS is indistinguishable from that in the type strain. In contrast, the O antigen region of the LPS from strain MO19 consists of a single Ley epitope linked via a 3-linked b-D-Gal to an intervening region on the basis of a sequence of 3-linked D-glycero-a-D-manno-heptose residues which is in turn linked to an inner core identical to that in the type strain and the P466 strain. Results in this and the preceding paper show that LPS from the three H. pylori strains display molecular mimicry of human cell surface glycoconjugates but may vary in the expression of Lex or Ley determinants, the degree of O antigen chain extension, or in the presence of an additional region between the inner core and the O antigen.
Lipopolysaccharide, antigen, lipopolysaccharides, LPS, oligosaccharide, structure, core, strain, O-antigen, O antigen, core oligosaccharide, region, Helicobacter pylori, Helicobacter
NCBI PubMed ID: 8652594Journal NLM ID: 0370623Publisher: American Chemical Society
Institutions: Department of Chemistry, York University, North York, Toronto, Ontario M3J 1P3, Canada
Methods: NMR-2D, defucosylation
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10. Compound ID: 2023
Structure type: oligomer
Aglycon: LPS
Trivial name: Lewis H type 2
Contained glycoepitopes: IEDB_130646,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_149555,IEDB_150948,IEDB_151531,IEDB_152214,IEDB_153553,IEDB_174333,IEDB_190606,IEDB_461719,SB_154,SB_165,SB_166,SB_187,SB_195,SB_30,SB_34,SB_7,SB_86,SB_88
The structure is contained in the following publication(s):
- 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: 10992504Journal NLM ID: 0246127Publisher: 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
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11. Compound ID: 2024
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a-L-Fucp-(1-3)-+
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a-L-Fucp-(1-2)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1--/LPS/ |
Show graphically |
Structure type: oligomer
Aglycon: LPS
Trivial name: Lewis Y, Lewis Y determinant, terminal Lewis Y unit
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
The structure is contained in the following publication(s):
- 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: 10992504Journal NLM ID: 0246127Publisher: 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
- 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: 11741906Publication DOI: 10.1074/jbc.M108574200Journal NLM ID: 2985121RPublisher: 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
- 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: 8675304Journal NLM ID: 0246127Publisher: American Society for Microbiology
Correspondence: BJ.Appelmelk.mm@med.vu.nl
Institutions: Department of Medical Microbiology, Vrije Universiteit, Medical School, Amsterdam, The Netherlands
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12. Compound ID: 2522
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a-L-Fucp-(1-3)-+
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a-L-Fucp-(1-2)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-Subst
Subst = O-antigen |
Show graphically |
Structure type: oligomer
Trivial name: Lewis Y antigenic determinant
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
The structure is contained in the following publication(s):
- 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: 10542057Journal NLM ID: 0107600Publisher: 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
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13. Compound ID: 2849
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a-D-Glcp-(1-3)-a-D-Glcp-(1-4)-b-D-Galp-(1-7)-+
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a-L-Fucp-(1-3)-+ | P-7)-+
| | |
a-L-Fucp-(1-2)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-7)-D-gro-a-D-manHepp-(1-2)-D-gro-a-D-manHepp-(1-2)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-Kdo-(2--/lipid A/ |
Show graphically |
Structure type: oligomer
Aglycon: lipid A
Trivial name: type 2 Lewis Y determinant
Contained glycoepitopes: IEDB_130644,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_143250,IEDB_144562,IEDB_144998,IEDB_145669,IEDB_146664,IEDB_149555,IEDB_149557,IEDB_149561,IEDB_150092,IEDB_150948,IEDB_151531,IEDB_152214,IEDB_153553,IEDB_174333,IEDB_190606,IEDB_2189046,IEDB_2189047,IEDB_461719,IEDB_461720,IEDB_461721,IEDB_983931,SB_147,SB_154,SB_157,SB_165,SB_166,SB_187,SB_192,SB_195,SB_30,SB_34,SB_7,SB_86,SB_88
The structure is contained in the following publication(s):
- 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: 10910974Publication DOI: 10.1093/glycob/10.7.701Journal NLM ID: 9104124Publisher: 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
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14. Compound ID: 2865
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a-D-Glcp-(1-3)-a-D-Glcp-(1-4)-b-D-Galp-(1-7)-+
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a-L-Fucp-(1-3)-+ {{{-a-D-Glcp-(1-6)-}}}a-D-Glcp-(1-2)-+ | P-7)-+
| | | |
a-L-Fucp-(1-2)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-D-gro-a-D-manHepp-(1-7)-D-gro-a-D-manHepp-(1-2)-D-gro-a-D-manHepp-(1-2)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-a-Kdo-(2--/lipid A/ |
Show graphically |
Structure type: oligomer
Aglycon: lipid A
Trivial name: Lewis Y antigenic determinant
Contained glycoepitopes: IEDB_130644,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_143250,IEDB_144562,IEDB_144998,IEDB_145669,IEDB_146664,IEDB_149555,IEDB_149557,IEDB_149561,IEDB_150092,IEDB_150948,IEDB_151531,IEDB_152214,IEDB_153553,IEDB_158538,IEDB_174333,IEDB_190606,IEDB_2189046,IEDB_2189047,IEDB_461719,IEDB_461720,IEDB_461721,IEDB_983931,SB_147,SB_154,SB_157,SB_165,SB_166,SB_187,SB_192,SB_195,SB_30,SB_34,SB_7,SB_86,SB_88
The structure is contained in the following publication(s):
- Article ID: 1006
Monteiro MA, Appelmelk BJ, Rasko DA, Moran AP, Hynes SO, MacLean LL, Chan KH, Michael FS, Logan SM, O'Rourke J, Lee A, Taylor DE, Perry MB "Lipopolysaccharide structures of Helicobacter pylori genomic strains 26695 and J99, mouse model H. pylori Sydney strain, H. pylori P466 carrying sialyl Lewis X, and H. pylori UA915 expressing Lewis B. Classification of H. pylori lipopolysaccharides into glycotype families" -
European Journal of Biochemistry 267(2) (2000) 305-320
This study describes the molecular makeup of the cell-wall lipopolysaccharides (LPSs) (O-chain polysaccharide→core oligosaccharide→lipid A) from five Helicobacter pylori strains: H. pylori 26695 and J99, the complete genome sequences of which have been published, the established mouse model Sydney strain (SS1), and the symptomatic strains P466 and UA915. All chemical and serological experiments were performed on the intact LPSs. H. pylori 26695 and SS1 possessed either a low-Mr semi-rough-form LPS carrying mostly a single Ley type-2 blood-group determinant in the O-chain region covalently attached to the core oligosaccharide or a high-Mr smooth-form LPS, as did strain J99, with an elongated partially fucosylated type-2 N-acetyllactosamine (polyLacNAc) O-chain polymer, terminated mainly by a Lex blood-group determinant, connected to the core oligosaccharide. In the midst of semi-rough-form LPS glycoforms, H. pylori 26695 and SS1 also expressed in the O-chain region a difucosylated antigen, α-L-Fucp(1-3)-α-L-Fucp(1-4)-β-D-GlcpNAc, and the cancer-cell-related type-1 or type-2 linear B-blood-group antigen, α-D-Galp(1-3)-β-D-Galp(1-3 or 4)-β-D-GlcpNAc. The LPS of H. pylori strain P466 carried the cancer-associated type-2 sialyl Lex blood-group antigen, and the LPS from strain UA915 expressed a type-1 Leb blood-group unit. These findings should aid investigations that focus on identifying and characterizing genes responsible for LPS biosynthesis in genomic strains 26695 and J99, and in understanding the role of H. pylori LPS in animal model studies. The LPSs from the H. pylori strains studied to date were grouped into specific glycotype families.
Lipopolysaccharide, structure, Helicobacter pylori, Lewis x, histo-blood groups, glycotypes
NCBI PubMed ID: 10632700Publication DOI: 10.1046/j.1432-1327.2000.01007.xJournal NLM ID: 0107600Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
Correspondence: Mario.Monteiro@nrc.ca
Institutions: Institute for Biological Sciences, National Research Council, Ottawa, Ontario, Canada
Methods: FAB-MS, NMR
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15. Compound ID: 2875
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a-D-Glcp-(1-3)-a-D-Glcp-(1-4)-b-D-Galp-(1-7)-+
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a-L-Fucp-(1-3)-+ | EtN-(1--P--7)--+
| | |
a-L-Fucp-(1-2)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-7)-D-gro-a-D-manHepp-(1-2)-D-gro-a-D-manHepp-(1-2)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-Kdo-(2--/lipid A/ |
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Structure type: oligomer
Aglycon: lipid A
Trivial name: Lewis Y antigenic determinant
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130644,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_143250,IEDB_144562,IEDB_144998,IEDB_145669,IEDB_146664,IEDB_149555,IEDB_149557,IEDB_149561,IEDB_150092,IEDB_150948,IEDB_151531,IEDB_152214,IEDB_153553,IEDB_174333,IEDB_190606,IEDB_2189046,IEDB_2189047,IEDB_461719,IEDB_461720,IEDB_461721,IEDB_983931,SB_147,SB_154,SB_157,SB_165,SB_166,SB_187,SB_192,SB_195,SB_30,SB_34,SB_7,SB_86,SB_88
The structure is contained in the following publication(s):
- Article ID: 1006
Monteiro MA, Appelmelk BJ, Rasko DA, Moran AP, Hynes SO, MacLean LL, Chan KH, Michael FS, Logan SM, O'Rourke J, Lee A, Taylor DE, Perry MB "Lipopolysaccharide structures of Helicobacter pylori genomic strains 26695 and J99, mouse model H. pylori Sydney strain, H. pylori P466 carrying sialyl Lewis X, and H. pylori UA915 expressing Lewis B. Classification of H. pylori lipopolysaccharides into glycotype families" -
European Journal of Biochemistry 267(2) (2000) 305-320
This study describes the molecular makeup of the cell-wall lipopolysaccharides (LPSs) (O-chain polysaccharide→core oligosaccharide→lipid A) from five Helicobacter pylori strains: H. pylori 26695 and J99, the complete genome sequences of which have been published, the established mouse model Sydney strain (SS1), and the symptomatic strains P466 and UA915. All chemical and serological experiments were performed on the intact LPSs. H. pylori 26695 and SS1 possessed either a low-Mr semi-rough-form LPS carrying mostly a single Ley type-2 blood-group determinant in the O-chain region covalently attached to the core oligosaccharide or a high-Mr smooth-form LPS, as did strain J99, with an elongated partially fucosylated type-2 N-acetyllactosamine (polyLacNAc) O-chain polymer, terminated mainly by a Lex blood-group determinant, connected to the core oligosaccharide. In the midst of semi-rough-form LPS glycoforms, H. pylori 26695 and SS1 also expressed in the O-chain region a difucosylated antigen, α-L-Fucp(1-3)-α-L-Fucp(1-4)-β-D-GlcpNAc, and the cancer-cell-related type-1 or type-2 linear B-blood-group antigen, α-D-Galp(1-3)-β-D-Galp(1-3 or 4)-β-D-GlcpNAc. The LPS of H. pylori strain P466 carried the cancer-associated type-2 sialyl Lex blood-group antigen, and the LPS from strain UA915 expressed a type-1 Leb blood-group unit. These findings should aid investigations that focus on identifying and characterizing genes responsible for LPS biosynthesis in genomic strains 26695 and J99, and in understanding the role of H. pylori LPS in animal model studies. The LPSs from the H. pylori strains studied to date were grouped into specific glycotype families.
Lipopolysaccharide, structure, Helicobacter pylori, Lewis x, histo-blood groups, glycotypes
NCBI PubMed ID: 10632700Publication DOI: 10.1046/j.1432-1327.2000.01007.xJournal NLM ID: 0107600Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
Correspondence: Mario.Monteiro@nrc.ca
Institutions: Institute for Biological Sciences, National Research Council, Ottawa, Ontario, Canada
Methods: FAB-MS, NMR
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Collapse this compound
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