Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_130679,IEDB_136044,IEDB_136794,IEDB_137472,IEDB_141794,IEDB_142487,IEDB_142488,IEDB_144998,IEDB_146100,IEDB_146664,IEDB_149174,IEDB_150933,IEDB_190606,IEDB_983931,SB_116,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_192,SB_195,SB_37,SB_39,SB_6,SB_68,SB_7,SB_76,SB_84,SB_88

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

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

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

  NCBI PubMed ID: 10521543
  Publication DOI: 10.1093/glycob/9.10.1061
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Institutions: Department of Chemistry, Swedish University of Agricultural Sciences, Uppsala, Sweden, Department of Medical Chemistry, Vrije Universiteit, Van der Boechorstraat 7, 1081 BT Amsterdam, The Netherlands
  Methods: 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, enzyme-assisted synthesis, DNA techniques, glycosyltransferase assays, kinetics assays
  
   
  
  Escherichia coli
  CSDB ID 1723 (all data & tools)
• Article ID: 379
  Simon PM, Goode PL, Mobasseri A, Zopf D "Inhibition of Helicobacter pylori binding to gastrointestinal epithelial cells by sialic acid-containing oligosaccharides" - Infection and Immunity 65(2) (1997) 750-757
  

  Helicobacterpylori, the ulcer pathogen residing in the human stomach, binds to epithelial cells of the gastric antrum. We have examined binding of 13 bacterial isolates to epithelial cell lines by use of a sensitive microtiter plate method in which measurement of bacterial urease activity provides the means for quantitation of bound organisms. Several established human gastrointestinal carcinoma cell lines grown as monolayers were compared for suitability in these assays, and the duodenum-derived cell line HuTu-80 was selected for testing bacterial binding inhibitors. When bacteria are pretreated with oligosaccharides, glycoproteins, and glycolipids, a complex picture of bacterial-epithelial adherence specificities emerges. Among the monovalent inhibitors tested, 3'-sialyllactose (NeuAc α2-3Gal β1-4Glc; 3'SL) was the most active oligosaccharide, inhibiting adherence for recent clinical isolates of H. pylori with a millimolar 50% inhibitory concentration (IC50). Its α2-6 isomer (6'SL) was less active. Most of the recent clinical isolates examined were inhibited by sialyllactose, whereas long-passaged isolates were insensitive. Among the long-passaged bacterial strains whose binding was not inhibited by 3'SL was the strain ATCC 43504, also known as NCTC 11637 and CCUG 17874, in which the proposed sialyllactose adhesin was recently reported to lack surface expression (P. G. O'Toole, L. Janzon, P. Doig, J. Huang, M. Kostrzynska, and T. H. Trust, J. Bacteriol. 177:6049-6057, 1995). Pretreatment of the epithelial monolayer with neuraminidase reduced the extent of binding by those bacteria that are sensitive to inhibition by 3'SL. Other potent inhibitors of bacterial binding are the glycoproteins α1-acid glycoprotein, fetuin, porcine gastric and bovine submaxillary mucins, and the glycolipid sulfatide, all of which present multivalent sialylated and/or sulfated galactosyl residues under the conditions of the binding assay. Consistent with this pattern, a multivalent neoglycoconjugate containing 20 mol of 3'SL per mol of human serum albumin inhibited bacterial binding with micromolar IC50. The H. pylori isolate most sensitive to inhibition by 3'SL was least sensitive to inhibition by sulfatide, gastric mucin, and other sulfated oligosaccharides. Bacteria that have been allowed to bind epithelial cells are also effectively detached by 3'SL. These results describe a heterogeneous adherence repertoire for these bacteria, but they also confirm the critical role of the 3'SL structure on human gastric epithelial cells as an adherence ligand for recent isolates of H. pylori.

  Oligosaccharides, sialic acid, Helicobacter pylori, inhibition, binding, epithelial cells

  NCBI PubMed ID: 9009338
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Correspondence: SimonPM@AOL.com
  Institutions: Neose Technologies, Inc., Horsham, Pennsylvania 19044
  Methods: serological methods
  
   
  
  Helicobacter pylori
  CSDB ID 8320 (all data & tools)
• Article ID: 2536
  Ono E, Abe K, Nakazawa M, Naiki M "Ganglioside epitope recognized by K99 fimbriae from enterotoxigenic Escherichia coli" - Infection and Immunity 57 (1989) 907-911
  

  The receptor structure recognized by Escherichia coli possessing K99 fimbriae and by isolated K99 fimbrial fractions was examined by using an equine erythrocyte hemagglutination inhibition test. Both K99-positive organisms (strain B41) and fimbrial preparations reacted with N-glycolylneuraminyl-lactosyl-ceramide (NeuGcLacCer) purified from equine erythrocytes with very high potency. Fimbrial preparations were 253 times more potent than intact organisms, indicating that isolated fimbriae more precisely recognize the structure of NeuGcLacCer than do fimbriae located on the bacterial cell wall. Structurally, the N-glycolyl group of the sialic acid was shown to be essential because substitution of the N-acetyl group for the N-glycolyl group caused the reactivity to completely disappear. The substitution of the O-acetyl group for the C4 hydroxyl group of the sialic acid (4-O-Ac-NeuGcLacCer) also diminished the reactivity by about 500 times, indicating that the fine structure of NeuGc is necessary for recognition. N-Glycolylneuraminyl-neolactotetraosyl-ceramide (NeuGcnLc4Cer) and N-glycolylneuraminyl-neolactohexaosyl-ceramide (NeuGcnLc6Cer), both of which have identical disaccharides at the nonreducing terminal and longer carbohydrate chains, showed reduced reactivity, indicating that the ceramide of NeuGcLacCer is also involved in the recognition. Indeed, NeuGcLac oligosaccharides altered by cleavage of the ceramide or the terminal sialic acid (NeuGc) showed dramatically reduced reactivities. Ten other E. coli strains (isolated from diseased calves) and two strains (isolated from diseased piglets) which possessed the same K99 antigen and various O antigens were used for the recognition test. The results obtained were similar to those mentioned above.

  NCBI PubMed ID: 2465273
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Institutions: Department of Biochemistry, Faculty of Veterinary Genetics, Hokkaido University, Sapporo, Japan
  
   
  
  Escherichia coli B41
  CSDB ID 130226 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130659,IEDB_130679,IEDB_136044,IEDB_136794,IEDB_137472,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_144998,IEDB_146100,IEDB_146664,IEDB_149174,IEDB_150933,IEDB_151531,IEDB_175430,IEDB_190606,IEDB_2189047,IEDB_226300,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_419430,IEDB_983931,SB_116,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_192,SB_195,SB_37,SB_39,SB_6,SB_68,SB_7,SB_76,SB_84,SB_88

• Article ID: 121
  Tsai CM, Kao G, Zhu P "Influence of the length of the lipooligosaccharide a chain on its sialylation in Neisseria meningitidis" - Infection and Immunity 70(1) (2002) 407-411
  

  The sialylation of lipooligosaccharide (LOS) in Neisseria meningitidis plays a role in the resistance of the organism to killing by normal human serum. The length of the alpha chain extending out from the heptose I [Hep (I)] moiety of LOS influenced sialylation of N. meningitidis LOS in vitro and in vivo. The alpha chain required a terminal Gal and a trisaccharide or longer oligosaccharide to serve as an acceptor for sialylation. The disaccharide lactose (Galβ1-4Glc) in the alpha chain of immunotype L8 LOS could not function as an acceptor for the sialyltransferase, probably due to steric hindrance imposed by the neighboring Hep (II) with phosphorylethanolamine and another group attached.

  Lipooligosaccharide, Neisseria meningitidis, sialyltransferase, structure-activity relationship, Substrate Specificity

  NCBI PubMed ID: 11748209
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Correspondence: tsai@cber.fda.gov
  Institutions: Division of Bacterial, Parasitic, and Allergenic Products, Center for Biologics, Food and Drug Administration, Bethesda, MD, USA
  Methods: SDS-PAGE
  
   
  
  Neisseria meningitidis 7880 (L10)
  CSDB ID 5376 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130648,IEDB_130650,IEDB_130679,IEDB_130683,IEDB_136044,IEDB_136794,IEDB_137472,IEDB_137473,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141794,IEDB_142487,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_149174,IEDB_150933,IEDB_190606,IEDB_2189047,IEDB_983931,SB_116,SB_144,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_192,SB_195,SB_25,SB_37,SB_39,SB_6,SB_68,SB_7,SB_76,SB_84,SB_88

• Article ID: 335
  Neisser A, Bernheimer H, Berger T, Moran AP, Schwerer B "Serum antibodies against gangliosides and Campylobacter jejuni lipopolysaccharides in Miller-Fisher syndrome" - Infection and Immunity 65(10) (1997) 4038-4042
  

  Seven patients with Miller Fisher syndrome (MFS), six in the acute phase and one in the recovery phase, were investigated for serum antibodies against gangliosides and purified lipopolysaccharides (LPS) from different strains of Campylobacter jejuni, including the MFS-associated serotypes O:2 and O:23. Immunoglobulin G antibodies against gangliosides GT1a and GQ1b were found in five of six patients in the acute phase of disease. Three of these patients also displayed antibodies to ganglioside GD2, a finding not previously reported for MFS. All anti-GT1a- and anti-GQ1b-seropositive patients showed antibody binding to C. jejuni LPS, predominantly to O:2 and O:23 LPS. Antibody cross-reactivity between gangliosides GT1a and GQ1b and O:2 and O:23 LPS was demonstrated by adsorption studies. This cross-reactivity between gangliosides and C.jejuni LPS, which is obviously due to oligosaccharide homologies, may be an important pathogenetic factor in the development of MFS after C. jejuni infection

  lipopolysaccharides, antibodies, Campylobacter, Campylobacter jejuni, gangliosides, Miller-Fisher syndrome

  NCBI PubMed ID: 9317004
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Correspondence: andrea.neisser@univie.ac.at
  Institutions: Institute of Neurology and Department of Neurology, University of Vienna, Vienna, Austria, Department of Microbiology, University College, Galway, Ireland
  Methods: serological methods, TLC-immunostaining
  
   
  
  Campylobacter jejuni O23
  CSDB ID 7830 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: GQ1b
Compound class: ganglioside
Contained glycoepitopes: IEDB_130648,IEDB_130675,IEDB_130676,IEDB_130678,IEDB_130679,IEDB_130680,IEDB_130681,IEDB_130683,IEDB_130684,IEDB_130686,IEDB_134627,IEDB_136044,IEDB_136095,IEDB_136794,IEDB_137339,IEDB_137472,IEDB_137473,IEDB_141794,IEDB_142487,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_147450,IEDB_147451,IEDB_149174,IEDB_150933,IEDB_150937,IEDB_153198,IEDB_153199,IEDB_190606,IEDB_433718,IEDB_547903,IEDB_858580,IEDB_983931,SB_116,SB_13,SB_14,SB_144,SB_164,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_192,SB_195,SB_2,SB_22,SB_23,SB_24,SB_25,SB_28,SB_3,SB_35,SB_37,SB_38,SB_39,SB_4,SB_41,SB_42,SB_5,SB_6,SB_68,SB_7,SB_70,SB_71,SB_76,SB_8,SB_84,SB_88,SB_94,SB_95,SB_96,SB_97,SB_98

• Article ID: 335
  Neisser A, Bernheimer H, Berger T, Moran AP, Schwerer B "Serum antibodies against gangliosides and Campylobacter jejuni lipopolysaccharides in Miller-Fisher syndrome" - Infection and Immunity 65(10) (1997) 4038-4042
  

  Seven patients with Miller Fisher syndrome (MFS), six in the acute phase and one in the recovery phase, were investigated for serum antibodies against gangliosides and purified lipopolysaccharides (LPS) from different strains of Campylobacter jejuni, including the MFS-associated serotypes O:2 and O:23. Immunoglobulin G antibodies against gangliosides GT1a and GQ1b were found in five of six patients in the acute phase of disease. Three of these patients also displayed antibodies to ganglioside GD2, a finding not previously reported for MFS. All anti-GT1a- and anti-GQ1b-seropositive patients showed antibody binding to C. jejuni LPS, predominantly to O:2 and O:23 LPS. Antibody cross-reactivity between gangliosides GT1a and GQ1b and O:2 and O:23 LPS was demonstrated by adsorption studies. This cross-reactivity between gangliosides and C.jejuni LPS, which is obviously due to oligosaccharide homologies, may be an important pathogenetic factor in the development of MFS after C. jejuni infection

  lipopolysaccharides, antibodies, Campylobacter, Campylobacter jejuni, gangliosides, Miller-Fisher syndrome

  NCBI PubMed ID: 9317004
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Correspondence: andrea.neisser@univie.ac.at
  Institutions: Institute of Neurology and Department of Neurology, University of Vienna, Vienna, Austria, Department of Microbiology, University College, Galway, Ireland
  Methods: serological methods, TLC-immunostaining
  
   
  
  Campylobacter jejuni
  CSDB ID 7831 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: GT1b
Compound class: ganglioside
Contained glycoepitopes: IEDB_130648,IEDB_130678,IEDB_130679,IEDB_130683,IEDB_130686,IEDB_134627,IEDB_136044,IEDB_136095,IEDB_136794,IEDB_137339,IEDB_137472,IEDB_137473,IEDB_141794,IEDB_142487,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_147450,IEDB_147451,IEDB_149174,IEDB_150933,IEDB_150937,IEDB_153198,IEDB_153199,IEDB_190606,IEDB_547903,IEDB_983931,SB_116,SB_13,SB_144,SB_164,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_192,SB_195,SB_2,SB_22,SB_23,SB_24,SB_25,SB_3,SB_35,SB_37,SB_39,SB_4,SB_41,SB_42,SB_5,SB_6,SB_68,SB_7,SB_70,SB_71,SB_76,SB_8,SB_84,SB_88,SB_96,SB_97,SB_98

• Article ID: 335
  Neisser A, Bernheimer H, Berger T, Moran AP, Schwerer B "Serum antibodies against gangliosides and Campylobacter jejuni lipopolysaccharides in Miller-Fisher syndrome" - Infection and Immunity 65(10) (1997) 4038-4042
  

  Seven patients with Miller Fisher syndrome (MFS), six in the acute phase and one in the recovery phase, were investigated for serum antibodies against gangliosides and purified lipopolysaccharides (LPS) from different strains of Campylobacter jejuni, including the MFS-associated serotypes O:2 and O:23. Immunoglobulin G antibodies against gangliosides GT1a and GQ1b were found in five of six patients in the acute phase of disease. Three of these patients also displayed antibodies to ganglioside GD2, a finding not previously reported for MFS. All anti-GT1a- and anti-GQ1b-seropositive patients showed antibody binding to C. jejuni LPS, predominantly to O:2 and O:23 LPS. Antibody cross-reactivity between gangliosides GT1a and GQ1b and O:2 and O:23 LPS was demonstrated by adsorption studies. This cross-reactivity between gangliosides and C.jejuni LPS, which is obviously due to oligosaccharide homologies, may be an important pathogenetic factor in the development of MFS after C. jejuni infection

  lipopolysaccharides, antibodies, Campylobacter, Campylobacter jejuni, gangliosides, Miller-Fisher syndrome

  NCBI PubMed ID: 9317004
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Correspondence: andrea.neisser@univie.ac.at
  Institutions: Institute of Neurology and Department of Neurology, University of Vienna, Vienna, Austria, Department of Microbiology, University College, Galway, Ireland
  Methods: serological methods, TLC-immunostaining
  
   
  
  Campylobacter jejuni
  CSDB ID 7832 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: GD2
Compound class: ganglioside
Contained glycoepitopes: IEDB_130648,IEDB_130676,IEDB_130679,IEDB_130683,IEDB_130684,IEDB_136044,IEDB_136095,IEDB_136794,IEDB_137339,IEDB_137472,IEDB_137473,IEDB_141794,IEDB_142487,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_149174,IEDB_150933,IEDB_150937,IEDB_153198,IEDB_153199,IEDB_190606,IEDB_433718,IEDB_858580,IEDB_983931,SB_116,SB_144,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_192,SB_195,SB_25,SB_3,SB_35,SB_37,SB_39,SB_4,SB_41,SB_42,SB_5,SB_6,SB_68,SB_7,SB_71,SB_76,SB_84,SB_88,SB_94,SB_95

• Article ID: 335
  Neisser A, Bernheimer H, Berger T, Moran AP, Schwerer B "Serum antibodies against gangliosides and Campylobacter jejuni lipopolysaccharides in Miller-Fisher syndrome" - Infection and Immunity 65(10) (1997) 4038-4042
  

  Seven patients with Miller Fisher syndrome (MFS), six in the acute phase and one in the recovery phase, were investigated for serum antibodies against gangliosides and purified lipopolysaccharides (LPS) from different strains of Campylobacter jejuni, including the MFS-associated serotypes O:2 and O:23. Immunoglobulin G antibodies against gangliosides GT1a and GQ1b were found in five of six patients in the acute phase of disease. Three of these patients also displayed antibodies to ganglioside GD2, a finding not previously reported for MFS. All anti-GT1a- and anti-GQ1b-seropositive patients showed antibody binding to C. jejuni LPS, predominantly to O:2 and O:23 LPS. Antibody cross-reactivity between gangliosides GT1a and GQ1b and O:2 and O:23 LPS was demonstrated by adsorption studies. This cross-reactivity between gangliosides and C.jejuni LPS, which is obviously due to oligosaccharide homologies, may be an important pathogenetic factor in the development of MFS after C. jejuni infection

  lipopolysaccharides, antibodies, Campylobacter, Campylobacter jejuni, gangliosides, Miller-Fisher syndrome

  NCBI PubMed ID: 9317004
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Correspondence: andrea.neisser@univie.ac.at
  Institutions: Institute of Neurology and Department of Neurology, University of Vienna, Vienna, Austria, Department of Microbiology, University College, Galway, Ireland
  Methods: serological methods, TLC-immunostaining
  
   
  
  Campylobacter jejuni
  CSDB ID 7833 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: LPS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130648,IEDB_130650,IEDB_130679,IEDB_130683,IEDB_136044,IEDB_136794,IEDB_137472,IEDB_137473,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141794,IEDB_142487,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_149174,IEDB_150933,IEDB_190606,IEDB_2189047,IEDB_983931,SB_116,SB_144,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_192,SB_195,SB_25,SB_37,SB_39,SB_6,SB_68,SB_7,SB_76,SB_84,SB_88

• Article ID: 360
  Ritter G, Fortunato SR, Cohen L, Noguchi I, Bernard EM, Stockert E, Old LJ "Induction of antibodies reactive with GM2 ganglioside after immunization with lipopolysaccharides from Campylobacter jejuni" - Radiation oncology investigations = International Journal of Cancer 66 (1996) 184-190
  

  Ganglioside GM2, expressed on the surface of some human cancers, is a promising target for immune therapy, since GM2 antibodies are cytotoxic, can be induced in humans by vaccination, and the presence of GM2 antibodies is associated with a better prognosis in melanoma patients. In our efforts to induce long-lived, cytotoxic GM2 antibodies, we investigated lipopolysaccharides (LPS) containing "GM2-like" oligosaccharides. LPS were prepared from Campylobacter jejuni serotypes O:1, O:23, or O:36 (all sharing the oligosaccharide structure GalNAcβ1-4Gal(113NeuAc)-Hex with ganglioside GM2), and tested for their ability to induce GM2-reactive antibodies. Immunization of NZW rabbits (2 animals per vaccine) with LPS from C. jejuni serotype O:1 in Freund's adjuvant resulted in production of high-titer IgG antibodies reactive with purified bovine brain GM2 in ELISA, dot-blot immune strains and immune thin-layer chromatography, and with GM2 derived from various human tumors by immune thin-layer chromatography. These rabbit antibodies bound to cancer cell lines expressing GM2 on their cell surface, as determined by mixed hemadsorption assays, mediating strong antibody-dependent cellular cytotoxicity (ADCC) with tumor cells expressing cell-surface GM2. Antibodies induced by vaccination with C. jejuni serotype O:1 were higher-titer (IgG ELISA titer > 1:60,000) than antibodies induced by immunization with purified GM2 (IgG ELISA titer > 1:200). Immunization with LPS from C. jejuni serotype O:36 resulted in production of moderately high-titer IgM and low-titer IgG GM2 antibodies. Immunization with LPS from C. jejuni serotype O:23 did not elicit GM2-reactive antibodies. No clinical symptoms were observed in animals immunized with these LPS preparations, with purified GM2 ganglioside, or with LPS derived from C. jejuni serotype O:19 (containing a GM1-like oligosaccharide). Our results indicate that lipopolysaccharides sharing carbohydrate epitopes with gangliosides may be useful immunogens for inducing antibodies to ganglioside antigens.

  lipopolysaccharides, antibodies, Campylobacter, Campylobacter jejuni, ganglioside

  NCBI PubMed ID: 8603809
  Journal NLM ID: 9437448
  Publisher: New York, NY: Wiley-Liss
  Institutions: Ludwi Institute for Cancer Research, New York Branch, Infectious Diseases Service, Memorial Sloan-Kettering Cancer Center, New York, NY, USA
  Methods: serological methods
  
   
  
  Campylobacter jejuni O1
  CSDB ID 8103 (all data & tools)
• Article ID: 2441
  Aspinall GO, McDonald AG, Raju TS, Pang H, Moran AP, Penner JL "Chemical structures of the core regions of Campylobacter jejuni serotypes O:1, O:4, O:23, and O:36 lipopolysaccharides" - European Journal of Biochemistry 213 (1993) 1017-1027
  
  Journal NLM ID: 0107600
  Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
  
   
  
  Campylobacter jejuni 23, Campylobacter jejuni 36
  CSDB ID 124133 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_130650,IEDB_130679,IEDB_136044,IEDB_136794,IEDB_137472,IEDB_137779,IEDB_138949,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141794,IEDB_142487,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_149174,IEDB_150933,IEDB_190606,IEDB_2189047,IEDB_983931,SB_116,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_192,SB_195,SB_37,SB_39,SB_6,SB_68,SB_7,SB_76,SB_84,SB_88

• Article ID: 398
  Tullius MV, Phillips NJ, Scheffler NK, Samuels NM, Munson JR, Hansen EJ, Stevens-Riley M, Campagnari AA, Gibson BW "The lbgAB gene cluster of Haemophilus ducreyi encodes a b-1,4-galactosyltransferase and an a-1,6-DD-heptosyltransferase involved in lipooligosaccharide biosynthesis" - Infection and Immunity 70(6) (2002) 2853-2861
  

  All Haemophilus ducreyi strains examined contain a lipooligosaccharide (LOS) consisting of a single but variable branch oligosaccharide that emanates off the first heptose (Hep-I) of a conserved Hep(3)-phosphorylated 3-deoxy-D-manno-octulosonic acid-lipid A core. In a previous report, identification of tandem genes, lbgA and lbgB, that are involved in LOS biosynthesis was described (Stevens et al., Infect. Immun. 65:651-660, 1997). In a separate study, the same gene cluster was identified and the lbgB (losB) gene was found to be required for transfer of the second sugar, D-glycero-D-manno-heptose (DD-Hep), of the major branch structure (Gibson et al., J. Bacteriol. 179:5062-5071, 1997). In this study, we identified the function of the neighboring upstream gene, lbgA, and found that it is necessary for addition of the third sugar in the dominant oligosaccharide branch, a galactose-linked β1→4, to the DD-Hep. LOS from an lbgA mutant and an lbgAB double mutant were isolated and were characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, carbohydrate analysis, mass spectrometry, and nuclear magnetic resonance spectroscopy. The results showed that the mutant strains synthesize truncated LOS glycoforms that terminate after addition of the first glucose (lbgAB) or the disaccharide DDHep α1→6 Glcβ1 (lbgA) that is attached to the heptose core. Both mutants show a significant reduction in the ability to adhere to human keratinocytes. Although minor differences were observed after two-dimensional gel electrophoresis of total proteins from the wild-type and mutant strains, the expression levels of the vast majority of proteins were unchanged, suggesting that the differences in adherence and invasion are due to differences in LOS. These studies add to the mounting evidence for a role of full-length LOS structures in the pathophysiology of H. ducreyi infection.

  Haemophilus, lipopolysaccharides, Haemophilus ducreyi, Molecular Sequence Data, gene cluster, glycosyltransferases, Magnetic Resonance Spectroscopy, Bacterial Adhesion, Keratinocytes

  NCBI PubMed ID: 12010972
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Correspondence: bgibson@buckinstitute.org
  Institutions: Department of Pharmaceutical Chemistry, University of California, San Francisco, CA, USA, Children's Research Institute and The Ohio State University, Columbus, Ohio 43205-26962, Southwestern Medical Center, University of Texas, Dallas, Texas 75235-90483, State University of New York, Buffalo, New York 142144, and Buck Institute for Age Research, Novato, California 949455
  Methods: NMR, MS, composition analysis, genetic methods, linkage analysis
  
   
  
  Haemophilus ducreyi 35000
  CSDB ID 8415 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: LPS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130648,IEDB_130650,IEDB_130679,IEDB_136044,IEDB_136794,IEDB_137472,IEDB_137473,IEDB_1391961,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141584,IEDB_141794,IEDB_142487,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_149174,IEDB_150933,IEDB_153215,IEDB_190606,IEDB_2189047,IEDB_885822,IEDB_983931,SB_116,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_192,SB_195,SB_37,SB_39,SB_6,SB_68,SB_7,SB_76,SB_84,SB_88

• Article ID: 422
  Wood AC, Oldfield NJ, O'Dwyer CA, Ketley JM "Cloning, mutation and distribution of a putative lipopolysaccharide biosynthesis locus in Campylobacter jejuni" - Microbiology 145(2) (1999) 379-388
  

  A region encoding ORFs with homology to known lipopolysaccharide (LPS) biosynthesis genes was isolated from two strains of Campylobacter jejuni. One of the strains produces LPS, but the second strain is reported to produce only lipooligosaccharide (LOS) and therefore lacks the O-chain. The two strains shared six predicted ORFs, but an additional ORF, orfE, of unknown function was identified in the LOS-producing strain. Mutation of the shared wbeE (rfbE) homologue (orfF) or deletion of five of the seven genes reduced core reactivity with specific antiserum without affecting O-chain production. Mutation of either the capD homologue (orfG) or the unique orfE had no detectable effect on LOS or LPS production. The presence or absence of orfE in 36 isolates of C. jejuni did not correlate with LOS/LPS phenotype or serotype. However, after insertion of orfE into a LPS-producing orfE-negative strain the O-chain ladder was no longer detectable on Western blots. We were not able to disrupt the wbaP (rfbP) homologue (orfC) in C jejuni

  Lipopolysaccharide, genetics, Campylobacter, mutation, distribution

  NCBI PubMed ID: 10075420
  Journal NLM ID: 0376646
  Publisher: Washington, DC: Kluwer Academic/Plenum Publishers
  Correspondence: ket!le.ac.uk
  Institutions: Department of Genetics, University of Leicester, University Road, Leicester LE1 7RH, UK
  Methods: PCR, DNA sequencing, SDS-PAGE
  
   
  
  Campylobacter jejuni O23 (NCTC 11351)
  CSDB ID 8714 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: LOS, LPS
Contained glycoepitopes: IEDB_115009,IEDB_116046,IEDB_120354,IEDB_123890,IEDB_130646,IEDB_130648,IEDB_130650,IEDB_130651,IEDB_130679,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136794,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137473,IEDB_137776,IEDB_137777,IEDB_137779,IEDB_138949,IEDB_1391964,IEDB_1391966,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_140624,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_144987,IEDB_146100,IEDB_146664,IEDB_149144,IEDB_149174,IEDB_150933,IEDB_151528,IEDB_151531,IEDB_152217,IEDB_190606,IEDB_2189047,IEDB_241118,IEDB_423106,IEDB_423120,IEDB_742247,IEDB_983931,SB_115,SB_116,SB_131,SB_145,SB_165,SB_166,SB_167,SB_170,SB_171,SB_172,SB_173,SB_178,SB_187,SB_192,SB_195,SB_25,SB_30,SB_31,SB_37,SB_39,SB_6,SB_62,SB_68,SB_7,SB_76,SB_84,SB_88

• Article ID: 558
  Hood DW, Randle G, Cox AD, Makepeace K, Li J, Schweda EK, Richards JC, Moxon ER "Biosynthesis of cryptic lipopolysaccharide glycoforms in Haemophilus influenzae involves a mechanism similar to that required for O-antigen synthesis" - Journal of Bacteriology 186(21) (2004) 7429-7439
  

  It is generally thought that mucosal bacterial pathogens of the genera Haemophilus, Neisseria, and Moraxella elaborate lipopolysaccharide (LPS) that is fundamentally different from that of enteric organisms that express O-specific polysaccharide side chains. Haemophilus influenzae elaborates short-chain LPS that has a role in the pathogenesis of H. influenzae infections. We show that the synthesis of LPS in this organism can no longer be as clearly distinguished from that in other gram-negative bacteria that express an O antigen. We provide evidence that a region of the H. influenzae genome, the hmg locus, is involved in the synthesis of glycoforms in which tetrasaccharide units are added en bloc, not stepwise, to the normal core glycoforms, similar to the biosynthesis of an O-antigen.

  Lipopolysaccharide, antigen, Haemophilus influenzae, Pathogenesis, Neisseria, O-specific polysaccharide, Moraxella, Gram-negative bacteria

  NCBI PubMed ID: 15489455
  Journal NLM ID: 2985120R
  Publisher: American Society for Microbiology
  Correspondence: derek.hood@paediatrics.oxford.ac.uk
  Institutions: Molecular Infectious Diseases Group, University of Oxford Department of Paediatrics, Weatherall Institute of Molecular Medicine, John Radcliffe Hospital, Headington, Oxford OX3 9DS, United Kingdom
  Methods: PCR, SDS-PAGE, ESI-MS
  
   
  
  Haemophilus influenzae RM118
  CSDB ID 9602 (all data & tools)
• Article ID: 4395
  Spahich NA, Hood DW, Moxon ER, St GJ "Inactivation of Haemophilus influenzae lipopolysaccharide biosynthesis genes interferes with outer membrane localization of the hap autotransporter" - Journal of Bacteriology 194(7) (2012) 1815-1822
  

  Nontypeable Haemophilus influenzae is a major cause of localized respiratory tract disease and initiates infection by colonizing the nasopharynx. Colonization requires adherence to host epithelial cells, which is mediated by surface proteins such as the Hap adhesin. In this study, we identified a relationship between Hap levels in the outer membrane and lipopolysaccharide (LPS) biosynthesis enzymes. We found that mutation of the rfaF, pgmB, lgtC, kfiC, orfE, rfbP, lsgB, or lsgD genes, which are involved in the synthesis of the LPS oligosaccharide core in H. influenzae strain Rd/HapS243A, resulted in loss of Hap in the bacterial outer membrane and a decrease in hap transcript levels. In contrast, the same mutations had no effect on outer membrane localization of H. influenzae P5 or IgA1 protease or levels of p5 or iga1 transcripts, suggesting a Hap-specific effect. Elimination of the HtrA periplasmic protease resulted in a return of Hap to the outer membrane and restoration of hap transcript levels. Consistently, in lgtC phase-off bacteria, Hap was absent from the outer membrane, and hap transcript levels were reduced. Hap localization and hap transcript levels were not related to LPS size but to the functions of the LPS biosynthesis enzymes themselves. We speculate that the lack of certain LPS biosynthesis enzymes causes Hap to mislocalize and accumulate in the periplasm, where it is degraded by HtrA. This degradation then leads to a decrease in hap transcript levels. Together, these data highlight a novel interplay between Hap and LPS biosynthesis that can influence H. influenzae interactions with the host.

  Lipopolysaccharide, biosynthesis, Haemophilus influenzae, gene, mutation, epithelial cells, bacterial outer membrane proteins, nasopharynx

  NCBI PubMed ID: 22287523
  Publication DOI: 10.1128/JB.06316-11
  Journal NLM ID: 2985120R
  Publisher: American Society for Microbiology
  Correspondence: j.stgeme@duke.edu (Joseph W. St. Geme III)
  Institutions: Departments of Pediatrics and Molecular Genetics and Microbiology, Duke University Medical Center, Children's Health Center, Durham, NC, USA
  Methods: PCR, SDS-PAGE, Western blotting, genetic methods
  
   
  
  Haemophilus influenzae
  CSDB ID 27324 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: LOS, LPS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130648,IEDB_130650,IEDB_130679,IEDB_130683,IEDB_136044,IEDB_136794,IEDB_137472,IEDB_137473,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141794,IEDB_142487,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_149174,IEDB_150933,IEDB_190606,IEDB_2189047,IEDB_983931,SB_116,SB_144,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_192,SB_195,SB_25,SB_37,SB_39,SB_6,SB_68,SB_7,SB_76,SB_84,SB_88

• Article ID: 647
  Gilbert M, Karwaski MF, Bernatchez S, Young NM, Taboada E, Michniewicz J, Cunningham AM, Wakarchuk WW "The genetic bases for the variation in the lipo-oligosaccharide of the mucosal pathogen, Campylobacter jejuni. Biosynthesis of sialylated ganglioside mimics in the core oligosaccharide" - Journal of Biological Chemistry 277(1) (2002) 327-337
  

  We have compared the lipo-oligosaccharide (LOS) biosynthesis loci from 11 Campylobacter jejuni strains expressing a total of 8 different ganglioside mimics in their LOS outer cores. Based on the organization of the genes, the 11 corresponding loci could be classified into three classes, with one of them being clearly an intermediate evolutionary step between the other two. Comparative genomics and expression of specific glycosyltransferases combined with in vitro activity assays allowed us to identify at least five distinct mechanisms that allow C. jejuni to vary the structure of the LOS outer core as follows: 1) different gene complements; 2) phase variation because of homopolymeric tracts; 3) gene inactivation by the deletion or insertion of a single base (without phase variation); 4) single mutation leading to the inactivation of a glycosyltransferase; and 5) single or multiple mutations leading to 'allelic' glycosyltransferases with different acceptor specificities. The differences in the LOS outer core structures expressed by the 11 C. jejuni strains examined can be explained by one or more of the five mechanisms described in this work

  biosynthesis, genetic, Phase variation, Lipooligosaccharide, gene, Campylobacter jejuni, ganglioside, glycosyltransferase, Chromosome Mapping

  NCBI PubMed ID: 11689567
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: michel.gilbert@nrc.ca
  Institutions: Institute for Biological Sciences, National Research Council of Canada, 100 Sussex Dr., Ottawa, Ontario K1A 0R6, Canada
  
   
  
  Campylobacter jejuni ATCC 43449, Campylobacter jejuni ATCC 43456, Campylobacter jejuni O23, Campylobacter jejuni O36
  CSDB ID 586 (all data & tools)
• Article ID: 3484
  Kanipes MI, Tan X, Akelaitis A, Li J, Rockabrand D, Guerry P, Monteiro MA "Genetic analysis of lipooligosaccharide core biosynthesis in Campylobacter jejuni 81-176" - Journal of Bacteriology 190(5) (2008) 1568-1574
  

  We report isolation and characterization of Campylobacter jejuni 81-176 lgtF and galT lipooligosaccharide (LOS) core mutants. It has been suggested that the lgtF gene of C. jejuni encodes a two-domain glucosyltransferase that is responsible for the transfer of a β-1,4-glucose residue on heptosyltransferase I (Hep I) and for the transfer of a β-1,2-glucose residue on Hep II. A site-specific mutation in the lgtF gene of C. jejuni 81-176 resulted in expression of a truncated LOS, and complementation of the mutant in trans restored the core mobility to that of the wild type. Mass spectrometry and nuclear magnetic resonance of the truncated LOS confirmed the loss of two glucose residues, a β-1,4-glucose on Hep I and a β-1,2-glucose on Hep II. Mutation of another gene, galT, encoding a glycosyltransferase, which maps outside the region defined as the LOS biosynthetic locus in C. jejuni 81-176, resulted in loss of the β-(1,4)-galactose residue and all distal residues in the core. Both mutants invaded intestinal epithelial cells in vitro at levels comparable to the wild-type levels, in marked contrast to a deeper inner core waaC mutant. These studies have important implications for the role of LOS in the pathogenesis of Campylobacter-mediated infection

  biosynthesis, core, Lipooligosaccharide, Campylobacter jejuni, mutants, glycosyltransferase

  NCBI PubMed ID: 18156268
  Journal NLM ID: 2985120R
  Publisher: American Society for Microbiology
  Correspondence: patricia.guerry@med.navy.mil
  Institutions: Department of Chemistry, North Carolina Agricultural and Technical State University, Greensboro, North Carolina 27411, USA
  Methods: 13C NMR, 1H NMR, GLC-MS, GC-MS, sugar analysis, 31P NMR, ESI-MS, acid hydrolysis, genetic methods
  
   
  
  Campylobacter jejuni 81-176
  CSDB ID 22662 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: core oligosaccharide, LPS
Contained glycoepitopes: IEDB_115009,IEDB_116046,IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130679,IEDB_136044,IEDB_136794,IEDB_137472,IEDB_137777,IEDB_137779,IEDB_138949,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_140624,IEDB_141794,IEDB_142487,IEDB_142488,IEDB_144998,IEDB_144999,IEDB_146100,IEDB_146664,IEDB_149174,IEDB_150933,IEDB_190606,IEDB_2189047,IEDB_241118,IEDB_983931,SB_116,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_192,SB_195,SB_37,SB_39,SB_6,SB_68,SB_7,SB_76,SB_84,SB_88

• Article ID: 979
  Mansson M, Bauer SHJ, Hood DW, Richards JC, Moxon ER, Schweda EKH "A new structural type for Haemophilus influenzae lipopolysaccharide - Structural analysis of the lipopolysaccharide from nontypeable Haemophilus influenzae strain 486" - European Journal of Biochemistry 268(7) (2001) 2148-2159
  

  Structural elucidation of the sialylated lipopolysaccharide (LPS) of non-typeable Haemophilus influenzae (NTHi) strain 486 has been achieved by the application of high-field NMR techniques and ESI-MS along with composition and linkage analyses on O-deacylated LPS and oligosaccharide samples. It was found that the LPS contains the common element of H. influenzae, L-α-D-Hepp-(1→2)-[PEtn→6]-L-α-D-Hepp-(1→3)-[β-D-Glcp-(1→4)]-L-α-D-Hepp-(1→5)-[PPEtn→4]-α-Kdop-(2→6)-Lipid A, but instead of glycosyl substitution of the terminal heptose residue (HepIII) at the O2 position observed in other H. influenzae strains, HepIII is chain elongated at the O3 position by either lactose or sialyllactose (i.e. α-Neu5Ac-(2→3)-β-D-Galp-(1→4)-β-D-Glcp). The LPS is substituted by an O-acetyl group linked to the O2 position of HepIII and phosphocholine (PCho) which was located at the O6 position of a terminal α-D-Glcp residue attached to the central heptose, a molecular environment different from what has been reported earlier for PCho. In addition, minor substitution by O-linked glycine to the LPS was observed. By investigation of LPS from a lpsA mutant of NTHi strain 486, it was demonstrated that the lpsA gene product also is responsible for chain extension from HepIII in this strain. The involvement of lic1 in expression of PCho was established by investigation of a lic1 mutant of NTHi strain 486.

  Lipopolysaccharide, Haemophilus, Haemophilus influenzae, strain, structural, analysis, structural analysis, type, Phosphocholine, sialic acid

  NCBI PubMed ID: 11277939
  Journal NLM ID: 0107600
  Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
  Correspondence: elke.schweda@kfcmail.hs.sll.se
  Institutions: University College of South Stockholm, Clinical Reseach Center,Huddinge,Sweden
  Methods: NMR
  
   
  
  Haemophilus influenzae 486
  CSDB ID 3424 (all data & tools)
• Article ID: 1459
  Holst O "Chemical structure of the core region of lipopolysaccharides - an update" - Trends in Glycoscience and Glycotechnology 14(76) (2002) 87-103
  

  Lipopolysaccharides (LPS) are the endotoxins of Gram-negative bacteria and very well known for their immunological, pharmacological and pathophysiological effects displayed in eucaryotic cells and organisms. To date, much emphasis has been put on the elucidation of the chemical structures of LPS and on their relation, or that of substructures, to the various biological effects. The lipid part of LPS, the lipid A, was proven to represent the toxic principle of endotoxin. However, lipid A toxicity depends strongly on its structure, and is influenced by a second region of LPS, the core region, that is covalently linked to lipid A. Also, the core region possesses immunogenic properties. Therefore, complete structural analyses of the core region and the comparison of its structures with biological features of LPS are of high importance for a better understanding of LPS action, and one prerequesite for strategies aimed at the treatment of endotoxicosis. In the past, quite a number of structures of the core regions from various Gram-negative bacteria were published and summarized in several overviews. The present review adds to this knowledge those structures that were published between October 1998 and December 2001.

  lipopolysaccharides, heptose, Kdo, chemical structure, core region, tructure

  Publication DOI: 10.4052/tigg.14.87
  Journal NLM ID: 9425898
  Correspondence: oholst@fz-borstel.de
  Institutions: Structural Biochemistry, Research Center Borstel, Center for Medicine and Biosciences, Borstel, Germany
  
   
  
  Haemophilus influenzae 486
  CSDB ID 31802 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: O-deacylated lipid A
Compound class: LPS
Contained glycoepitopes: IEDB_115009,IEDB_116046,IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130679,IEDB_136044,IEDB_136794,IEDB_137472,IEDB_137777,IEDB_137779,IEDB_138949,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_140624,IEDB_141794,IEDB_142487,IEDB_142488,IEDB_144998,IEDB_144999,IEDB_146100,IEDB_146664,IEDB_149174,IEDB_150933,IEDB_190606,IEDB_2189047,IEDB_241118,IEDB_983931,SB_116,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_192,SB_195,SB_37,SB_39,SB_6,SB_68,SB_7,SB_76,SB_84,SB_88

• Article ID: 979
  Mansson M, Bauer SHJ, Hood DW, Richards JC, Moxon ER, Schweda EKH "A new structural type for Haemophilus influenzae lipopolysaccharide - Structural analysis of the lipopolysaccharide from nontypeable Haemophilus influenzae strain 486" - European Journal of Biochemistry 268(7) (2001) 2148-2159
  

  Structural elucidation of the sialylated lipopolysaccharide (LPS) of non-typeable Haemophilus influenzae (NTHi) strain 486 has been achieved by the application of high-field NMR techniques and ESI-MS along with composition and linkage analyses on O-deacylated LPS and oligosaccharide samples. It was found that the LPS contains the common element of H. influenzae, L-α-D-Hepp-(1→2)-[PEtn→6]-L-α-D-Hepp-(1→3)-[β-D-Glcp-(1→4)]-L-α-D-Hepp-(1→5)-[PPEtn→4]-α-Kdop-(2→6)-Lipid A, but instead of glycosyl substitution of the terminal heptose residue (HepIII) at the O2 position observed in other H. influenzae strains, HepIII is chain elongated at the O3 position by either lactose or sialyllactose (i.e. α-Neu5Ac-(2→3)-β-D-Galp-(1→4)-β-D-Glcp). The LPS is substituted by an O-acetyl group linked to the O2 position of HepIII and phosphocholine (PCho) which was located at the O6 position of a terminal α-D-Glcp residue attached to the central heptose, a molecular environment different from what has been reported earlier for PCho. In addition, minor substitution by O-linked glycine to the LPS was observed. By investigation of LPS from a lpsA mutant of NTHi strain 486, it was demonstrated that the lpsA gene product also is responsible for chain extension from HepIII in this strain. The involvement of lic1 in expression of PCho was established by investigation of a lic1 mutant of NTHi strain 486.

  Lipopolysaccharide, Haemophilus, Haemophilus influenzae, strain, structural, analysis, structural analysis, type, Phosphocholine, sialic acid

  NCBI PubMed ID: 11277939
  Journal NLM ID: 0107600
  Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
  Correspondence: elke.schweda@kfcmail.hs.sll.se
  Institutions: University College of South Stockholm, Clinical Reseach Center,Huddinge,Sweden
  Methods: NMR
  
   
  
  Haemophilus influenzae 486
  CSDB ID 3605 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130648,IEDB_130650,IEDB_130679,IEDB_130683,IEDB_136044,IEDB_136794,IEDB_137472,IEDB_137473,IEDB_140088,IEDB_141794,IEDB_142487,IEDB_142488,IEDB_144998,IEDB_146100,IEDB_146664,IEDB_149174,IEDB_150933,IEDB_190606,IEDB_2189047,IEDB_983931,SB_116,SB_144,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_192,SB_195,SB_25,SB_37,SB_39,SB_6,SB_68,SB_7,SB_76,SB_84,SB_88

• Article ID: 1355
  Ang CW, Noordzij PG, De Klerk MA, Endtz HP, Van Doorn PA, Laman JD "Ganglioside mimicry of Campylobacter jejuni lipopolysaccharides determines antiganglioside specificity in rabbits" - Infection and Immunity 70(9) (2002) 5081-5085
  

  The core oligosaccharides of Campylobacter jejuni lipopolysaccharides (LPS) display molecular mimicry with gangliosides. Cross-reactive anti-LPS-antiganglioside antibodies have been implicated to show a crucial role in the pathogenesis of the Guillain-Barré and Miller Fisher syndrome. The specificity of the antiganglioside response is thought to depend on the oligosaccharide structure of the ganglioside mimic. To test this hypothesis and to investigate the potential of LPS from Campylobacter strains from enteritis patients to induce an antiganglioside response, we immunized rabbits with purified LPS from eight Campylobacter jejuni reference strains with biochemically well-defined distinct ganglioside mimics and determined the presence of antiganglioside antibodies. All rabbits produced immunoglobulin G (IgM) and IgG anti-LPS antibodies, and the specificity of the cross-reactive antiganglioside response indeed corresponded with the biochemically defined mimic. Most rabbits also had antibody reactivity against additional gangliosides, and there were slight differences in the fine specificity of the antibody response between rabbits that had been immunized with LPS from the same Campylobacter strain. High anti-LPS and antiganglioside titers persisted over a 10-month period. In conclusion, the structure of the LPS only partly determines the antiganglioside specificity. Other strain-specific as well as host-related factors influence the induction and fine-specificity of the cross-reactive anti-LPS-antiganglioside response.

  Lipopolysaccharide, biosynthesis, lipopolysaccharides, LPS, oligosaccharide, core, chemistry, Bacterial, human, molecular, antibodies, Oligosaccharides, animal, Campylobacter, Campylobacter jejuni, Carbohydrate Sequence, core oligosaccharide, etiology, ganglioside, gangliosides, Guillain-Barre syndrome, immunization, Immunoglobulin M, immunology, mimicry, molecular mimicry, Molecular Sequence Data, antibody specificity, Cross Reactions, specificity, Miller Fisher syndrome, rabbit, immunoglobulin G, Rabbits

  NCBI PubMed ID: 12183556
  Publication DOI: 10.1128/IAI.70.9.5081-5085.2002
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Correspondence: Ang@Bacl.azr.nl
  Institutions: Department of Medical Microbiology and Infectious Diseases, Erasmus University Medical Centre, Rotterdam, The Netherlands
  
   
  
  Campylobacter jejuni O23 (CCUG 10954), Campylobacter jejuni O36 (CCUG 10966)
  CSDB ID 6312 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Contained glycoepitopes: IEDB_115009,IEDB_116046,IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130679,IEDB_136044,IEDB_136794,IEDB_137472,IEDB_137777,IEDB_137779,IEDB_138949,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_140624,IEDB_141794,IEDB_142487,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_149174,IEDB_150933,IEDB_190606,IEDB_2189047,IEDB_241118,IEDB_983931,SB_116,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_192,SB_195,SB_37,SB_39,SB_6,SB_68,SB_7,SB_76,SB_84,SB_88

• Article ID: 1382
  Bouchet V, Hood DW, Brisson J, Randle GA, Martin A, Li Z, Goldstein R, Schweda E, Pelton SI, Richards JC, Moxon ER "Host-derived sialic acid is incorporated into Haemophilus influenzae lipopolysaccharide and is a major virulence factor in experimental otitis media" - Proceedings of the National Academy of Sciences of the USA 100(15) (2003) 8898-8903
  

  Otitis media, a common and often recurrent bacterial infection of childhood, is a major reason for physician visits and the prescription of antimicrobials. Haemophilus influenzae is the cause of approximately 20% of episodes of bacterial otitis media, but most strains lack the capsule, a factor known to play a critical role in the virulence of strains causing invasive H. influenzae disease. Here we show that in capsule-deficient (nontypeable) strains, sialic acid, a terminal residue of the core sugars of H. influenzae lipopolysaccharide (LPS), is a critical virulence factor in the pathogenesis of experimental otitis media in chinchillas. We used five epidemiologically distinct H. influenzae isolates, representative of the genetic diversity of strains causing otitis media, to inoculate the middle ear of chinchillas. All animals developed acute bacterial otitis media that persisted for up to 3 wk, whereas isogenic sialic acid-deficient mutants (disrupted sialyltransferase or CMP-acetylneuraminic acid synthetase genes) were profoundly attenuated. MS analysis indicated that WT bacteria used to inoculate animals lacked any sialylated LPS glycoforms. In contrast, LPS of ex vivo organisms recovered from chinchilla middle ear exudates was sialylated. We conclude that sialylated LPS glycoforms play a key role in pathogenicity of nontypeable H. influenzae and depend on scavenging the essential precursors from the host during the infection.

  mass spectrometry, phylogeny, ex vivo isolate

  NCBI PubMed ID: 12855765
  Publication DOI: 10.1073/pnas.1432026100
  Journal NLM ID: 7505876
  Publisher: National Academy of Sciences
  Correspondence: Richard.Moxon@paediatrics.ox.ac.uk
  Institutions: Maxwell Finland Laboratory for Infectious Diseases, Division of Pediatric Infectious Diseases, Boston University School of Medicine, Boston Medical Center, 774 Albany Street, Boston, MA 02118, USA, University of Oxford Department of Paediatrics, Molecular Infectious Diseases Group, Weatherall Institute of Molecular Medicine, John Radcliffe Hospital, Oxford, United Kingdom, Institute for Biological Sciences, National Research Council of Canada, 100 Sussex Drive, Ottawa, ON, Canada K1A 0R6, Clinical Research Centre, Karolinska Institutet and University College of South Stockholm, NOVUM, S-141 86 Huddinge, Sweden
  
   
  
  Haemophilus influenzae 375
  CSDB ID 6281 (all data & tools)