Found 115 structures.
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1. Compound ID: 52
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Gal-(1-4)-b-D-GlcNAc-(1--/p-nitrophenyl/ |
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Structure type: oligomer
Aglycon: p-nitrophenyl
Contained glycoepitopes: IEDB_130646,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136095,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_150939,IEDB_151531,IEDB_190606,SB_165,SB_166,SB_173,SB_187,SB_195,SB_30,SB_7,SB_88
The structure is contained in the following publication(s):
- 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: 10521543Publication DOI: 10.1093/glycob/9.10.1061Journal NLM ID: 9104124Publisher: 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
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2. Compound ID: 283
|
L-gro-a-D-manHepp-(1-2)-L-gro-a-D-manHepp-(1-3)-+
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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)-D-gro-a-D-manHepp-(1-6)-b-D-Glcp-(1-4)-L-gro-a-D-manHepp-(1-5)-a-Kdop |
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Structure type: oligomer
Compound class: LOS
Contained glycoepitopes: IEDB_130646,IEDB_130650,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_137779,IEDB_138949,IEDB_139428,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_150939,IEDB_151531,IEDB_190606,IEDB_2189046,IEDB_2189047,IEDB_983931,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 75
Filiatrault MJ, Gibson BW, Schilling B, Sun SH, Munson RS, Campagnari AA "Construction and characterization of Haemophilus ducreyi lipooligosaccharide (LOS) mutants defective in expression of heptosyltransferase III and b1,4-glucosyltransferase: Identification of LOS glycoforms containing lactosamine repeats" -
Infection and Immunity 68(6) (2000) 3352-3361
To begin to understand the role of the lipooligosaccharide (LOS) molecule in chancroid infections, we constructed mutants defective in expression of glycosyltransferase genes. Pyocin lysis and immunoscreening was used to identify a LOS mutant of Haemophilus ducreyi 35000. This mutant, HD35000R, produced a LOS molecule that lacked the monoclonal antibody 3F11 epitope and migrated with an increased mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Structural studies indicated that the principal LOS glycoform contains lipid A, Kdo, and two of the three core heptose residues. HD35000R was transformed with a plasmid library of H. ducreyi 35000 DNA, and a clone producing the wild-type LOS was identified. Sequence analysis of the plasmid insert revealed one open reading frame (ORF) that encodes a protein with homology to the WaaQ (heptosyltransferase III) of Escherichia coli. A second ORF had homology to the LgtF (glucosyltransferase) of Neisseria meningitidis. Individual isogenic mutants lacking expression of the putative H. ducreyi heptosyltransferase III, the putative glucosyltransferase, and both glycosyltransferases were constructed and characterized. Each mutant was complemented with the representative wild-type genes in trans to restore expression of parental LOS and confirm the function of each enzyme. Matrix-assisted laser desorption ionization mass spectrometry and SDS-PAGE analysis identified several unique LOS glycoforms containing di-, tri-, and poly-N-acetyllactosamine repeats added to the terminal region of the main LOS branch synthesized by the heptosyltransferase III mutant. These novel H. ducreyi mutants provide important tools for studying the regulation of LOS assembly and biosynthesis
Haemophilus, Haemophilus ducreyi, Lipooligosaccharide, expression, LOS, characterization, identification, mutant, mutants, construction, heptosyltransferase, lactosamine
NCBI PubMed ID: 10816485Journal NLM ID: 0246127Publisher: American Society for Microbiology
Correspondence: AAC@acsu.buffalo.edu
Institutions: Department of Microbiology, Department of Medicine, Division of Infectious Diseases, and Center for Microbial Pathogenesis, University at Buffalo, Buffalo, New York 14214, Department of Pharmaceutical Chemistry, University of California, San Francisco, CA, USA3, and Children's Research Institute4 and Department of Molecular Virology, Immunology, and Medical Genetics,5 Ohio State University, Columbus, Ohio 43205-2696
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3. Compound ID: 284
|
L-gro-a-D-manHepp-(1-3)-+
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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)-D-gro-a-D-manHepp-(1-6)-b-D-Glcp-(1-4)-L-gro-a-D-manHepp-(1-5)-a-Kdop |
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Structure type: oligomer
Compound class: LOS
Contained glycoepitopes: IEDB_130646,IEDB_130650,IEDB_130655,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_139428,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_150939,IEDB_151531,IEDB_158550,IEDB_190606,IEDB_2189046,IEDB_2189047,IEDB_983931,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 75
Filiatrault MJ, Gibson BW, Schilling B, Sun SH, Munson RS, Campagnari AA "Construction and characterization of Haemophilus ducreyi lipooligosaccharide (LOS) mutants defective in expression of heptosyltransferase III and b1,4-glucosyltransferase: Identification of LOS glycoforms containing lactosamine repeats" -
Infection and Immunity 68(6) (2000) 3352-3361
To begin to understand the role of the lipooligosaccharide (LOS) molecule in chancroid infections, we constructed mutants defective in expression of glycosyltransferase genes. Pyocin lysis and immunoscreening was used to identify a LOS mutant of Haemophilus ducreyi 35000. This mutant, HD35000R, produced a LOS molecule that lacked the monoclonal antibody 3F11 epitope and migrated with an increased mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Structural studies indicated that the principal LOS glycoform contains lipid A, Kdo, and two of the three core heptose residues. HD35000R was transformed with a plasmid library of H. ducreyi 35000 DNA, and a clone producing the wild-type LOS was identified. Sequence analysis of the plasmid insert revealed one open reading frame (ORF) that encodes a protein with homology to the WaaQ (heptosyltransferase III) of Escherichia coli. A second ORF had homology to the LgtF (glucosyltransferase) of Neisseria meningitidis. Individual isogenic mutants lacking expression of the putative H. ducreyi heptosyltransferase III, the putative glucosyltransferase, and both glycosyltransferases were constructed and characterized. Each mutant was complemented with the representative wild-type genes in trans to restore expression of parental LOS and confirm the function of each enzyme. Matrix-assisted laser desorption ionization mass spectrometry and SDS-PAGE analysis identified several unique LOS glycoforms containing di-, tri-, and poly-N-acetyllactosamine repeats added to the terminal region of the main LOS branch synthesized by the heptosyltransferase III mutant. These novel H. ducreyi mutants provide important tools for studying the regulation of LOS assembly and biosynthesis
Haemophilus, Haemophilus ducreyi, Lipooligosaccharide, expression, LOS, characterization, identification, mutant, mutants, construction, heptosyltransferase, lactosamine
NCBI PubMed ID: 10816485Journal NLM ID: 0246127Publisher: American Society for Microbiology
Correspondence: AAC@acsu.buffalo.edu
Institutions: Department of Microbiology, Department of Medicine, Division of Infectious Diseases, and Center for Microbial Pathogenesis, University at Buffalo, Buffalo, New York 14214, Department of Pharmaceutical Chemistry, University of California, San Francisco, CA, USA3, and Children's Research Institute4 and Department of Molecular Virology, Immunology, and Medical Genetics,5 Ohio State University, Columbus, Ohio 43205-2696
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4. Compound ID: 285
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L-gro-a-D-manHepp-(1-3)-+
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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)-D-gro-a-D-manHepp-(1-6)-b-D-Glcp-(1-4)-L-gro-a-D-manHepp-(1-5)-a-Kdop |
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Structure type: oligomer
Compound class: LOS
Contained glycoepitopes: IEDB_130646,IEDB_130650,IEDB_130655,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_139428,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_150939,IEDB_151531,IEDB_158550,IEDB_190606,IEDB_2189046,IEDB_2189047,IEDB_983931,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 75
Filiatrault MJ, Gibson BW, Schilling B, Sun SH, Munson RS, Campagnari AA "Construction and characterization of Haemophilus ducreyi lipooligosaccharide (LOS) mutants defective in expression of heptosyltransferase III and b1,4-glucosyltransferase: Identification of LOS glycoforms containing lactosamine repeats" -
Infection and Immunity 68(6) (2000) 3352-3361
To begin to understand the role of the lipooligosaccharide (LOS) molecule in chancroid infections, we constructed mutants defective in expression of glycosyltransferase genes. Pyocin lysis and immunoscreening was used to identify a LOS mutant of Haemophilus ducreyi 35000. This mutant, HD35000R, produced a LOS molecule that lacked the monoclonal antibody 3F11 epitope and migrated with an increased mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Structural studies indicated that the principal LOS glycoform contains lipid A, Kdo, and two of the three core heptose residues. HD35000R was transformed with a plasmid library of H. ducreyi 35000 DNA, and a clone producing the wild-type LOS was identified. Sequence analysis of the plasmid insert revealed one open reading frame (ORF) that encodes a protein with homology to the WaaQ (heptosyltransferase III) of Escherichia coli. A second ORF had homology to the LgtF (glucosyltransferase) of Neisseria meningitidis. Individual isogenic mutants lacking expression of the putative H. ducreyi heptosyltransferase III, the putative glucosyltransferase, and both glycosyltransferases were constructed and characterized. Each mutant was complemented with the representative wild-type genes in trans to restore expression of parental LOS and confirm the function of each enzyme. Matrix-assisted laser desorption ionization mass spectrometry and SDS-PAGE analysis identified several unique LOS glycoforms containing di-, tri-, and poly-N-acetyllactosamine repeats added to the terminal region of the main LOS branch synthesized by the heptosyltransferase III mutant. These novel H. ducreyi mutants provide important tools for studying the regulation of LOS assembly and biosynthesis
Haemophilus, Haemophilus ducreyi, Lipooligosaccharide, expression, LOS, characterization, identification, mutant, mutants, construction, heptosyltransferase, lactosamine
NCBI PubMed ID: 10816485Journal NLM ID: 0246127Publisher: American Society for Microbiology
Correspondence: AAC@acsu.buffalo.edu
Institutions: Department of Microbiology, Department of Medicine, Division of Infectious Diseases, and Center for Microbial Pathogenesis, University at Buffalo, Buffalo, New York 14214, Department of Pharmaceutical Chemistry, University of California, San Francisco, CA, USA3, and Children's Research Institute4 and Department of Molecular Virology, Immunology, and Medical Genetics,5 Ohio State University, Columbus, Ohio 43205-2696
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5. Compound ID: 286
|
L-gro-a-D-manHepp-(1-3)-+
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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-(1-3)-b-D-Galp-(1-4)-D-gro-a-D-manHepp-(1-6)-b-D-Glcp-(1-4)-L-gro-a-D-manHepp-(1-5)-a-Kdop |
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Structure type: oligomer
Compound class: LOS
Contained glycoepitopes: IEDB_130646,IEDB_130650,IEDB_130655,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_139428,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_150939,IEDB_151531,IEDB_158550,IEDB_190606,IEDB_2189046,IEDB_2189047,IEDB_983931,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 75
Filiatrault MJ, Gibson BW, Schilling B, Sun SH, Munson RS, Campagnari AA "Construction and characterization of Haemophilus ducreyi lipooligosaccharide (LOS) mutants defective in expression of heptosyltransferase III and b1,4-glucosyltransferase: Identification of LOS glycoforms containing lactosamine repeats" -
Infection and Immunity 68(6) (2000) 3352-3361
To begin to understand the role of the lipooligosaccharide (LOS) molecule in chancroid infections, we constructed mutants defective in expression of glycosyltransferase genes. Pyocin lysis and immunoscreening was used to identify a LOS mutant of Haemophilus ducreyi 35000. This mutant, HD35000R, produced a LOS molecule that lacked the monoclonal antibody 3F11 epitope and migrated with an increased mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Structural studies indicated that the principal LOS glycoform contains lipid A, Kdo, and two of the three core heptose residues. HD35000R was transformed with a plasmid library of H. ducreyi 35000 DNA, and a clone producing the wild-type LOS was identified. Sequence analysis of the plasmid insert revealed one open reading frame (ORF) that encodes a protein with homology to the WaaQ (heptosyltransferase III) of Escherichia coli. A second ORF had homology to the LgtF (glucosyltransferase) of Neisseria meningitidis. Individual isogenic mutants lacking expression of the putative H. ducreyi heptosyltransferase III, the putative glucosyltransferase, and both glycosyltransferases were constructed and characterized. Each mutant was complemented with the representative wild-type genes in trans to restore expression of parental LOS and confirm the function of each enzyme. Matrix-assisted laser desorption ionization mass spectrometry and SDS-PAGE analysis identified several unique LOS glycoforms containing di-, tri-, and poly-N-acetyllactosamine repeats added to the terminal region of the main LOS branch synthesized by the heptosyltransferase III mutant. These novel H. ducreyi mutants provide important tools for studying the regulation of LOS assembly and biosynthesis
Haemophilus, Haemophilus ducreyi, Lipooligosaccharide, expression, LOS, characterization, identification, mutant, mutants, construction, heptosyltransferase, lactosamine
NCBI PubMed ID: 10816485Journal NLM ID: 0246127Publisher: American Society for Microbiology
Correspondence: AAC@acsu.buffalo.edu
Institutions: Department of Microbiology, Department of Medicine, Division of Infectious Diseases, and Center for Microbial Pathogenesis, University at Buffalo, Buffalo, New York 14214, Department of Pharmaceutical Chemistry, University of California, San Francisco, CA, USA3, and Children's Research Institute4 and Department of Molecular Virology, Immunology, and Medical Genetics,5 Ohio State University, Columbus, Ohio 43205-2696
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6. Compound ID: 361
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a-D-GlcpNAc-(1-2)-L-gro-a-D-manHepp-(1-3)-+ a-Kdop-(2-4)-+
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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-Glcp-(1-4)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/ |
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Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_130646,IEDB_130650,IEDB_130659,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_146664,IEDB_149144,IEDB_150939,IEDB_151531,IEDB_158549,IEDB_190606,IEDB_2189047,IEDB_226300,IEDB_418762,IEDB_418764,IEDB_418767,IEDB_418769,IEDB_419429,IEDB_983931,SB_145,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_6,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 106
Tong Y, Arking D, Ye S, Reinhold B, Reinhold V, Stein DC "Neisseria gonorrhoeae strain PID2 simultaneously expresses six chemically related lipooligosaccharide structures" -
Glycobiology 12(9) (2002) 523-533
Neisseria gonorrhoeae strain PID2 was isolated from a woman suffering from pelvic inflammatory disease. When LOS expressed by this strain is analyzed on SDS-PAGE gels, at least six different lipooligosaccharide (LOS) components are visualized. We characterized the LOSs made by this strain by exoglycosidase digestion, sugar composition analysis, mass spectrometry, and analysis of the genes needed for its synthesis. DNA sequence analysis showed that the lgt gene cluster in this strain has undergone a rearrangement and that it possesses two copies of lgtA, one copy of lgtB and lgtC, and a hybrid gene containing sequences from lgtB and lgtE. We determined that the hybrid lgtB/E gene retained the lgtE gene function. DNA sequence analysis of the gene organization suggested that an intramolecular recombination between lgtA and lgtD and lgtB and lgtE had occurred via homologous recombination between similar sequences. Our studies demonstrated that fluorophore-assisted carbohydrate electrophoresis can be utilized to rapidly determine the composition of LOS. By combining exoglycosidase digestion, in combination with mass spectrometry analysis and compositional analysis, the data indicate that all of the LOS components produced by PID2 extend off of the alpha chain. The longest alpha chain oligosaccharide structure is Gal-GlcNAc-Gal-GlcNAc-Gal-Glc-Heptose I, and the six LOS components are built up by sequentially adding sugars onto the first heptose. PID2 LOS is the first Neisserial LOS to be shown to be devoid of phosphoethanolamine modifications. Because PID2 can surface express its LOS, it indicates that the addition of phosphoethanolamine is not required for LOS surface expression.
LOS, mass spectrometry, carbohydrate epitopes, FACE analysis, lipooligosaccharide structure
NCBI PubMed ID: 12213785Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Methods: mild acid hydrolysis, MS, serological methods, electrophoresis
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7. Compound ID: 832
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+
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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)-D-GlcNAc |
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Structure type: oligomer
Trivial name: antigen type I
Contained glycoepitopes: IEDB_130646,IEDB_130655,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_150939,IEDB_151531,IEDB_153529,IEDB_153531,IEDB_153557,IEDB_158533,IEDB_158548,IEDB_158550,IEDB_190606,SB_165,SB_166,SB_173,SB_187,SB_195,SB_30,SB_7,SB_88
The structure is contained in the following publication(s):
- 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: 11421348Journal NLM ID: 8603310Publisher: Kluwer Academic Publishers
Correspondence: t.feizi@ic.ac.uk
Institutions: The Glycosciences Laboratory, Imperial College School of Medicine, Harrow, United Kingdom
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8. Compound ID: 833
|
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)-D-GlcNAc |
Show graphically |
Structure type: oligomer
Trivial name: antigen type i
Contained glycoepitopes: IEDB_130646,IEDB_130655,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_150939,IEDB_151531,IEDB_158550,IEDB_190606,SB_165,SB_166,SB_173,SB_187,SB_195,SB_30,SB_7,SB_88
The structure is contained in the following publication(s):
- 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: 11421348Journal NLM ID: 8603310Publisher: Kluwer Academic Publishers
Correspondence: t.feizi@ic.ac.uk
Institutions: The Glycosciences Laboratory, Imperial College School of Medicine, Harrow, United Kingdom
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9. Compound ID: 848
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L-gro-a-D-manHepp-(1-3)-+
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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)-D-gro-a-D-manHepp-(1-6)-b-D-Glcp-(1-4)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/ |
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Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_130646,IEDB_130650,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_139428,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_150939,IEDB_151531,IEDB_190606,IEDB_2189046,IEDB_2189047,IEDB_983931,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 233
Filiatrault MJ, Munson RS, Campagnari AA "Genetic analysis of a pyocin-resistant lipooligosaccharide (LOS) mutant of Haemophilus ducreyi: Restoration of full-length LOS restores pyocin sensitivity" -
Journal of Bacteriology 183(19) (2001) 5756-5761
DNA sequence and Southern blot analyses were used to determine the genetic defect of a Haemophilus ducreyi pyocin-resistant lipooligosaccharide (LOS) mutant, HD35000R. The region of the HD35000R chromosome containing the suspected mutation was amplified, and sequence analysis detected a 3,189-bp deletion. This deletion resulted in the loss of the entire waaQ gene, another open reading frame that encodes a putative homolog to a hypothetical protein (HI0461) of H. influenzae, the gene encoding an argininosuccinate synthase homolog, and a change in the 3' sequence of the lgtF gene. Southern blot analysis confirmed that no genomic rearrangements had occurred. Isogenic LOS mutants and the respective complemented mutants were evaluated for susceptibility to pyocin C. The mutants expressing truncated LOS were resistant to lysis by pyocin C, and complementation restored sensitivity to the pyocin. We conclude that HD35000R is defective in both glycosyltransferase genes and that pyocin resistance is due to truncation of the full-length LOS molecule
genetic, Haemophilus, Haemophilus ducreyi, Lipooligosaccharide, LOS, analysis, mutant, pyocin, sensitivity
NCBI PubMed ID: 11544241Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Correspondence: aac@ascu.buffalo.edu
Institutions: Department of Microbiology, State University of New York at Buffalo, Buffalo, New York 14214, USA
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10. Compound ID: 849
|
L-gro-a-D-manHepp-(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)-D-gro-a-D-manHepp-(1-6)-b-D-Glcp-(1-4)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/ |
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Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_130646,IEDB_130650,IEDB_130655,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_139428,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_150939,IEDB_151531,IEDB_158550,IEDB_190606,IEDB_2189046,IEDB_2189047,IEDB_983931,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 233
Filiatrault MJ, Munson RS, Campagnari AA "Genetic analysis of a pyocin-resistant lipooligosaccharide (LOS) mutant of Haemophilus ducreyi: Restoration of full-length LOS restores pyocin sensitivity" -
Journal of Bacteriology 183(19) (2001) 5756-5761
DNA sequence and Southern blot analyses were used to determine the genetic defect of a Haemophilus ducreyi pyocin-resistant lipooligosaccharide (LOS) mutant, HD35000R. The region of the HD35000R chromosome containing the suspected mutation was amplified, and sequence analysis detected a 3,189-bp deletion. This deletion resulted in the loss of the entire waaQ gene, another open reading frame that encodes a putative homolog to a hypothetical protein (HI0461) of H. influenzae, the gene encoding an argininosuccinate synthase homolog, and a change in the 3' sequence of the lgtF gene. Southern blot analysis confirmed that no genomic rearrangements had occurred. Isogenic LOS mutants and the respective complemented mutants were evaluated for susceptibility to pyocin C. The mutants expressing truncated LOS were resistant to lysis by pyocin C, and complementation restored sensitivity to the pyocin. We conclude that HD35000R is defective in both glycosyltransferase genes and that pyocin resistance is due to truncation of the full-length LOS molecule
genetic, Haemophilus, Haemophilus ducreyi, Lipooligosaccharide, LOS, analysis, mutant, pyocin, sensitivity
NCBI PubMed ID: 11544241Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Correspondence: aac@ascu.buffalo.edu
Institutions: Department of Microbiology, State University of New York at Buffalo, Buffalo, New York 14214, USA
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11. Compound ID: 850
|
L-gro-a-D-manHepp-(1-3)-+
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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)-D-gro-a-D-manHepp-(1-6)-b-D-Glcp-(1-4)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/ |
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Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_130646,IEDB_130650,IEDB_130655,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_139428,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_150939,IEDB_151531,IEDB_158550,IEDB_190606,IEDB_2189046,IEDB_2189047,IEDB_983931,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 233
Filiatrault MJ, Munson RS, Campagnari AA "Genetic analysis of a pyocin-resistant lipooligosaccharide (LOS) mutant of Haemophilus ducreyi: Restoration of full-length LOS restores pyocin sensitivity" -
Journal of Bacteriology 183(19) (2001) 5756-5761
DNA sequence and Southern blot analyses were used to determine the genetic defect of a Haemophilus ducreyi pyocin-resistant lipooligosaccharide (LOS) mutant, HD35000R. The region of the HD35000R chromosome containing the suspected mutation was amplified, and sequence analysis detected a 3,189-bp deletion. This deletion resulted in the loss of the entire waaQ gene, another open reading frame that encodes a putative homolog to a hypothetical protein (HI0461) of H. influenzae, the gene encoding an argininosuccinate synthase homolog, and a change in the 3' sequence of the lgtF gene. Southern blot analysis confirmed that no genomic rearrangements had occurred. Isogenic LOS mutants and the respective complemented mutants were evaluated for susceptibility to pyocin C. The mutants expressing truncated LOS were resistant to lysis by pyocin C, and complementation restored sensitivity to the pyocin. We conclude that HD35000R is defective in both glycosyltransferase genes and that pyocin resistance is due to truncation of the full-length LOS molecule
genetic, Haemophilus, Haemophilus ducreyi, Lipooligosaccharide, LOS, analysis, mutant, pyocin, sensitivity
NCBI PubMed ID: 11544241Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Correspondence: aac@ascu.buffalo.edu
Institutions: Department of Microbiology, State University of New York at Buffalo, Buffalo, New York 14214, USA
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12. Compound ID: 851
|
L-gro-a-D-manHepp-(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-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-D-gro-a-D-manHepp-(1-6)-b-D-Glcp-(1-4)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/ |
Show graphically |
Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_130646,IEDB_130650,IEDB_130655,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_139428,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_150939,IEDB_151531,IEDB_158550,IEDB_190606,IEDB_2189046,IEDB_2189047,IEDB_983931,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 233
Filiatrault MJ, Munson RS, Campagnari AA "Genetic analysis of a pyocin-resistant lipooligosaccharide (LOS) mutant of Haemophilus ducreyi: Restoration of full-length LOS restores pyocin sensitivity" -
Journal of Bacteriology 183(19) (2001) 5756-5761
DNA sequence and Southern blot analyses were used to determine the genetic defect of a Haemophilus ducreyi pyocin-resistant lipooligosaccharide (LOS) mutant, HD35000R. The region of the HD35000R chromosome containing the suspected mutation was amplified, and sequence analysis detected a 3,189-bp deletion. This deletion resulted in the loss of the entire waaQ gene, another open reading frame that encodes a putative homolog to a hypothetical protein (HI0461) of H. influenzae, the gene encoding an argininosuccinate synthase homolog, and a change in the 3' sequence of the lgtF gene. Southern blot analysis confirmed that no genomic rearrangements had occurred. Isogenic LOS mutants and the respective complemented mutants were evaluated for susceptibility to pyocin C. The mutants expressing truncated LOS were resistant to lysis by pyocin C, and complementation restored sensitivity to the pyocin. We conclude that HD35000R is defective in both glycosyltransferase genes and that pyocin resistance is due to truncation of the full-length LOS molecule
genetic, Haemophilus, Haemophilus ducreyi, Lipooligosaccharide, LOS, analysis, mutant, pyocin, sensitivity
NCBI PubMed ID: 11544241Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Correspondence: aac@ascu.buffalo.edu
Institutions: Department of Microbiology, State University of New York at Buffalo, Buffalo, New York 14214, USA
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13. Compound ID: 914
|
L-gro-a-D-manHepp-(1-2)-L-gro-a-D-manHepp-(1-3)-+ P-?)-+
| |
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)-D-gro-a-D-manHepp-(1-6)-b-D-Glcp-(1-4)-L-gro-a-D-manHepp-(1-?)-a-Kdop-(2--/lipid A/ |
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Structure type: oligomer
Aglycon: lipid A
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130646,IEDB_130650,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_137777,IEDB_137778,IEDB_137779,IEDB_138949,IEDB_139428,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_150939,IEDB_151531,IEDB_190606,IEDB_2189046,IEDB_2189047,IEDB_983931,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 261
Holst O "On the occurrence of D-glycero-D-manno-heptose in lipopolysaccharides" -
Polish Journal of Chemistry 73 (1999) 1055-1067
Lipopolysaccharides (LPS) consist of three regions, i.e. the lipid A, the core region, and the O-specific polysaccharide. The core region and the lipid A represent a common structural unit occurring in all LPS. The structures of the core region of various bacteria have been investigated intensively for the past ten years, and several core regions containing D-glycero-D-manno-heptose which is the biosynthetic precursor of the common core constituent L-glycero-D-manno-heptose have been identified. In this review, these core structures are summarized and briefly discussed.
Lipopolysaccharide, lipopolysaccharides, core, D-glycero-D-manno-heptose, composition, occurrence
Journal NLM ID: 7901356WWW link: http://www.ichf.edu.pl/pjch/pj-1999/pj0799.htm#1055Publisher: Państwowe Wydawnictwo Naukowe
Institutions: Research Center Borstel, Center for Medicine and Biosciences, 23845 Borstel, Germany
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14. Compound ID: 931
|
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-Glcp-(1--/diphosphoryl lipoidal moiety/ |
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Structure type: oligomer
Aglycon: diphosphoryl lipoidal moiety
Compound class: LOS
Contained glycoepitopes: IEDB_130646,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_146664,IEDB_149144,IEDB_150939,IEDB_151531,IEDB_158549,IEDB_190606,IEDB_983931,SB_145,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_6,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 271
John CM, Schneider H, Griffiss JM "Neisseria gonorrhoeae that infect men have lipooligosaccharides with terminal N-acetyllactosamine repeats" -
Journal of Biological Chemistry 274(2) (1999) 1017-1025
Infectious Neisseria gonorrhoeae make relatively large lipooligosaccharides (LOS) that structurally resemble human glycosphingolipids. MS11mkC is an LOS variant of N. gonorrhoeae strain MS11 which was isolated from men at the onset of dysuria (Schneider, H., Griffiss, J. M., Boslego, J. W., Hitchcock, P. J., Zahos, K. M., and Apicella, M. A. (1991) J. Exp. Med. 174, 1601-1605). Delayed extraction matrix-assisted laser desorption and ionization and electrospray ionization mass spectrometry of O-deacylated MS11mkC LOS produced ions consistent with known LOS which have lacto-N-neotetraose (Gal β1→4 GlcNAc β1→3 Gal β1→4 Glc; paraglobosyl; monoclonal antibodies (mAbs) 1B2(+) and 06B4(+)) and GalNAc→lacto-N-neotetraose (gangliosyl; mAb 1-1-M+) oligosaccharides. Ion peaks for a larger LOS which also bound mAb 1B2 indicated the addition of a hexose (+162 Da) to gangliosyl LOS or the addition of a hexose and a N-acetylhexosamine (+365 Da) to paraglobosyl LOS. Analysis of HF-treated and O-deacylated LOS revealed three major components present in a phosphoethanolamine (PEA)0 and a PEA1 series. Digestion of MS11mkC LOS by β-N-acetylhexosaminidase and β-galactosidase, alone and sequentially, combined with mAb binding patterns, confirmed the presence of a nonreducing terminal repeating LacNAc ((Gal β1→4 GlcNAc)2) on the largest LOS, rather than a parallel oligosaccharide structure.
Neisseria, Gonorrhoeae, Neisseria gonorrhoeae, lipooligosaccharides, N-acetyllactosamine
NCBI PubMed ID: 9873046Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: cjohn@vacom.ucsf.edu.net
Institutions: Centre for Immunochemistry and the Department of Laboratory Medicine, University of California, San Francisco, California 94121 and the Department of Bacterial Diseases, Walter Reed Army Institute of Research, Washington, D. C. 20307.
Methods: ESI-MS, MALDI-MS
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15. Compound ID: 1024
|
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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Next 15 structure(s)
Total list of structure IDs on all result pages of the current query:
Total list of corresponding CSDB IDs (record IDs):
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