Found 49 structures.
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1. Compound ID: 106
a-Neup5Ac-(2-8)-a-Neup5Ac-(2-3)-+
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a-Neup5Ac-(2-8)-a-Neup5Ac-(2-3)-b-D-Galp-(1-3)-b-D-GalpNAc-(1-4)-b-D-Galp-(1--/Glcp(1-1)ceramide (ganglioside GQ1b) or the inner core-lipid A (lipopolysaccharide)/ |
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Structure type: oligomer
Aglycon: Glcp(1-1)ceramide (ganglioside GQ1b) or the inner core-lipid A (lipopolysaccharide)
Trivial name: ganglioside GQ1b
Contained glycoepitopes: IEDB_130648,IEDB_134627,IEDB_136044,IEDB_136794,IEDB_137472,IEDB_137473,IEDB_141794,IEDB_146100,IEDB_147450,IEDB_147451,IEDB_149174,IEDB_150933,IEDB_150937,IEDB_153198,IEDB_153199,IEDB_190606,SB_116,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_195,SB_23,SB_24,SB_25,SB_35,SB_39,SB_42,SB_68,SB_7,SB_70,SB_8,SB_84,SB_88,SB_96,SB_97
The structure is contained in the following publication(s):
- Article ID: 20
Bowes T, Wagner ER, Boffey J, Nicholl D, Cochrane L, Benboubetra M, Conner J, Furukawa K, Willison HJ "Tolerance to self gangliosides is the major factor restricting the antibody response to lipopolysaccharide core oligosaccharides in Campylobacter jejuni strains associated with Guillain-Barre syndrome" -
Infection and Immunity 70(9) (2002) 5008-5018
Guillain-Barre syndrome following Campylobacter jejuni infection is frequently associated with anti-ganglioside autoantibodies mediated by molecular mimicry with ganglioside-like oligosaccharides on bacterial lipopolysaccharide (LPS). The regulation of antibody responses to these T-cell-independent antigens is poorly understood, and only a minority of Campylobacter-infected individuals develop anti-ganglioside antibodies. This study investigates the response to gangliosides and LPS in strains of mice by using a range of immunization strategies. In normal mice following intraperitoneal immunization, antibody responses to gangliosides and LPS are low level but can be enhanced by the antigen format or coadministration of protein to recruit T-cell help. Class switching from the predominant immunoglobulin M (IgM) response to IgG3 occurs at low levels, suggesting B1-cell involvement. Systemic immunization results in poor responses. In GalNAc transferase knockout mice that lack all complex gangliosides and instead express high levels of GM3 and GD3, generation of anti-ganglioside antibodies upon immunization with either complex gangliosides or ganglioside-mimicking LPS is greatly enhanced and exhibits class switching to T-cell- dependent IgG isotypes and immunological memory, indicating that tolerance to self gangliosides is a major regulatory factor. Responses to GD3 are suppressed in knockout mice compared with wild-type mice, in which responses to GD3 are induced specifically by GD3 and as a result of polyclonal B-cell activation by LPS. The anti-ganglioside response generated in response to LPS is also dependent on the epitope density of the ganglioside mimicked and can be further manipulated by providing secondary signals via lipid A and CD40 ligation
Lipopolysaccharide, biosynthesis, antigen, lipopolysaccharides, LPS, oligosaccharide, core, chemistry, Bacterial, genetics, human, metabolism, pathogenicity, strain, molecular, transferase, antibodies, antibody, epitope, lipid, lipid A, Oligosaccharides, activation, animal, anti-ganglioside, antibody response, antigens, CD40, Autoantibodies, autoantibody, B cell, B-cell, Campylobacter, Campylobacter Infections, Campylobacter jejuni, Carbohydrate Sequence, class, complex, complications, core oligosaccharide, deficiency, density, enhanced, etiology, factor, Female, ganglioside, gangliosides, generation, Guillain-Barre syndrome, high, IgG, IgM, immunization, immunoglobulin, Immunoglobulin M, immunological, immunological memory, immunology, induced, infection, involvement, level, lipopolysaccharide core, lipopolysaccharide core oligosaccharide, liposomes, memory, mice, Inbred BALB C, Inbred C3H, Knockout, mimicry, molecular mimicry, Molecular Sequence Data, N-Acetylgalactosaminyltransferases, predominant, protein, regulation, response, Self Tolerance, signal, syndrome, T cell, tolerance, wild type
NCBI PubMed ID: 12183547Journal NLM ID: 0246127Publisher: American Society for Microbiology
Correspondence: h.j.willison@udcf.gla.ac.uk
Institutions: University Department of Neurology, Institute of Neurological Sciences, Southern General Hospital, Glasgow, Scotland G51 4TF
Methods: ELISA
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2. Compound ID: 109
a-Neup5Ac-(2-3)-+
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a-Neup5Ac-(2-3)-b-D-Galp-(1-3)-b-D-GalpNAc-(1-4)-b-D-Galp-(1--/Glcp(1-1)ceramide (ganglioside GD1a) or the inner core-lipid A (lipopolysaccharide)/ |
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Structure type: oligomer
Aglycon: Glcp(1-1)ceramide (ganglioside GD1a) or the inner core-lipid A (lipopolysaccharide)
Trivial name: GD3
Contained glycoepitopes: IEDB_130648,IEDB_134627,IEDB_136044,IEDB_136794,IEDB_137472,IEDB_137473,IEDB_141794,IEDB_146100,IEDB_147450,IEDB_147451,IEDB_149174,IEDB_150933,IEDB_190606,SB_116,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_195,SB_23,SB_24,SB_25,SB_39,SB_68,SB_7,SB_70,SB_8,SB_84,SB_88,SB_96,SB_97
The structure is contained in the following publication(s):
- Article ID: 20
Bowes T, Wagner ER, Boffey J, Nicholl D, Cochrane L, Benboubetra M, Conner J, Furukawa K, Willison HJ "Tolerance to self gangliosides is the major factor restricting the antibody response to lipopolysaccharide core oligosaccharides in Campylobacter jejuni strains associated with Guillain-Barre syndrome" -
Infection and Immunity 70(9) (2002) 5008-5018
Guillain-Barre syndrome following Campylobacter jejuni infection is frequently associated with anti-ganglioside autoantibodies mediated by molecular mimicry with ganglioside-like oligosaccharides on bacterial lipopolysaccharide (LPS). The regulation of antibody responses to these T-cell-independent antigens is poorly understood, and only a minority of Campylobacter-infected individuals develop anti-ganglioside antibodies. This study investigates the response to gangliosides and LPS in strains of mice by using a range of immunization strategies. In normal mice following intraperitoneal immunization, antibody responses to gangliosides and LPS are low level but can be enhanced by the antigen format or coadministration of protein to recruit T-cell help. Class switching from the predominant immunoglobulin M (IgM) response to IgG3 occurs at low levels, suggesting B1-cell involvement. Systemic immunization results in poor responses. In GalNAc transferase knockout mice that lack all complex gangliosides and instead express high levels of GM3 and GD3, generation of anti-ganglioside antibodies upon immunization with either complex gangliosides or ganglioside-mimicking LPS is greatly enhanced and exhibits class switching to T-cell- dependent IgG isotypes and immunological memory, indicating that tolerance to self gangliosides is a major regulatory factor. Responses to GD3 are suppressed in knockout mice compared with wild-type mice, in which responses to GD3 are induced specifically by GD3 and as a result of polyclonal B-cell activation by LPS. The anti-ganglioside response generated in response to LPS is also dependent on the epitope density of the ganglioside mimicked and can be further manipulated by providing secondary signals via lipid A and CD40 ligation
Lipopolysaccharide, biosynthesis, antigen, lipopolysaccharides, LPS, oligosaccharide, core, chemistry, Bacterial, genetics, human, metabolism, pathogenicity, strain, molecular, transferase, antibodies, antibody, epitope, lipid, lipid A, Oligosaccharides, activation, animal, anti-ganglioside, antibody response, antigens, CD40, Autoantibodies, autoantibody, B cell, B-cell, Campylobacter, Campylobacter Infections, Campylobacter jejuni, Carbohydrate Sequence, class, complex, complications, core oligosaccharide, deficiency, density, enhanced, etiology, factor, Female, ganglioside, gangliosides, generation, Guillain-Barre syndrome, high, IgG, IgM, immunization, immunoglobulin, Immunoglobulin M, immunological, immunological memory, immunology, induced, infection, involvement, level, lipopolysaccharide core, lipopolysaccharide core oligosaccharide, liposomes, memory, mice, Inbred BALB C, Inbred C3H, Knockout, mimicry, molecular mimicry, Molecular Sequence Data, N-Acetylgalactosaminyltransferases, predominant, protein, regulation, response, Self Tolerance, signal, syndrome, T cell, tolerance, wild type
NCBI PubMed ID: 12183547Journal NLM ID: 0246127Publisher: American Society for Microbiology
Correspondence: h.j.willison@udcf.gla.ac.uk
Institutions: University Department of Neurology, Institute of Neurological Sciences, Southern General Hospital, Glasgow, Scotland G51 4TF
Methods: ELISA
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3. Compound ID: 110
a-Neup5Ac-(2-3)-+
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a-Neup5Ac-(2-8)-a-Neup5Ac-(2-3)-b-D-Galp-(1-3)-b-D-GalpNAc-(1-4)-b-D-Galp-(1--/Glcp(1-1)ceramide (ganglioside GT1a) or the inner core-lipid A (lipopolysaccharide)/ |
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Structure type: oligomer
Aglycon: Glcp(1-1)ceramide (ganglioside GT1a) or the inner core-lipid A (lipopolysaccharide)
Trivial name: GT1a
Contained glycoepitopes: IEDB_130648,IEDB_134627,IEDB_136044,IEDB_136794,IEDB_137472,IEDB_137473,IEDB_141794,IEDB_146100,IEDB_147450,IEDB_147451,IEDB_149174,IEDB_150933,IEDB_150937,IEDB_153198,IEDB_153199,IEDB_190606,SB_116,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_195,SB_23,SB_24,SB_25,SB_35,SB_39,SB_42,SB_68,SB_7,SB_70,SB_8,SB_84,SB_88,SB_96,SB_97
The structure is contained in the following publication(s):
- Article ID: 20
Bowes T, Wagner ER, Boffey J, Nicholl D, Cochrane L, Benboubetra M, Conner J, Furukawa K, Willison HJ "Tolerance to self gangliosides is the major factor restricting the antibody response to lipopolysaccharide core oligosaccharides in Campylobacter jejuni strains associated with Guillain-Barre syndrome" -
Infection and Immunity 70(9) (2002) 5008-5018
Guillain-Barre syndrome following Campylobacter jejuni infection is frequently associated with anti-ganglioside autoantibodies mediated by molecular mimicry with ganglioside-like oligosaccharides on bacterial lipopolysaccharide (LPS). The regulation of antibody responses to these T-cell-independent antigens is poorly understood, and only a minority of Campylobacter-infected individuals develop anti-ganglioside antibodies. This study investigates the response to gangliosides and LPS in strains of mice by using a range of immunization strategies. In normal mice following intraperitoneal immunization, antibody responses to gangliosides and LPS are low level but can be enhanced by the antigen format or coadministration of protein to recruit T-cell help. Class switching from the predominant immunoglobulin M (IgM) response to IgG3 occurs at low levels, suggesting B1-cell involvement. Systemic immunization results in poor responses. In GalNAc transferase knockout mice that lack all complex gangliosides and instead express high levels of GM3 and GD3, generation of anti-ganglioside antibodies upon immunization with either complex gangliosides or ganglioside-mimicking LPS is greatly enhanced and exhibits class switching to T-cell- dependent IgG isotypes and immunological memory, indicating that tolerance to self gangliosides is a major regulatory factor. Responses to GD3 are suppressed in knockout mice compared with wild-type mice, in which responses to GD3 are induced specifically by GD3 and as a result of polyclonal B-cell activation by LPS. The anti-ganglioside response generated in response to LPS is also dependent on the epitope density of the ganglioside mimicked and can be further manipulated by providing secondary signals via lipid A and CD40 ligation
Lipopolysaccharide, biosynthesis, antigen, lipopolysaccharides, LPS, oligosaccharide, core, chemistry, Bacterial, genetics, human, metabolism, pathogenicity, strain, molecular, transferase, antibodies, antibody, epitope, lipid, lipid A, Oligosaccharides, activation, animal, anti-ganglioside, antibody response, antigens, CD40, Autoantibodies, autoantibody, B cell, B-cell, Campylobacter, Campylobacter Infections, Campylobacter jejuni, Carbohydrate Sequence, class, complex, complications, core oligosaccharide, deficiency, density, enhanced, etiology, factor, Female, ganglioside, gangliosides, generation, Guillain-Barre syndrome, high, IgG, IgM, immunization, immunoglobulin, Immunoglobulin M, immunological, immunological memory, immunology, induced, infection, involvement, level, lipopolysaccharide core, lipopolysaccharide core oligosaccharide, liposomes, memory, mice, Inbred BALB C, Inbred C3H, Knockout, mimicry, molecular mimicry, Molecular Sequence Data, N-Acetylgalactosaminyltransferases, predominant, protein, regulation, response, Self Tolerance, signal, syndrome, T cell, tolerance, wild type
NCBI PubMed ID: 12183547Journal NLM ID: 0246127Publisher: American Society for Microbiology
Correspondence: h.j.willison@udcf.gla.ac.uk
Institutions: University Department of Neurology, Institute of Neurological Sciences, Southern General Hospital, Glasgow, Scotland G51 4TF
Methods: ELISA
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4. Compound ID: 871
a-Neup5Ac-(2-3)-+
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a-Neup5Ac-(2-8)-a-Neup5Ac-(2-3)-b-D-Galp-(1-3)-b-D-GalpNAc-(1-4)-b-D-Galp-(1--/lipid A/ |
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Structure type: oligomer
Aglycon: lipid A
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130648,IEDB_134627,IEDB_136044,IEDB_136794,IEDB_137472,IEDB_137473,IEDB_141794,IEDB_146100,IEDB_147450,IEDB_147451,IEDB_149174,IEDB_150933,IEDB_150937,IEDB_153198,IEDB_153199,IEDB_190606,SB_116,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_195,SB_23,SB_24,SB_25,SB_35,SB_39,SB_42,SB_68,SB_7,SB_70,SB_8,SB_84,SB_88,SB_96,SB_97
The structure is contained in the following publication(s):
- Article ID: 242
Goodyear CS, O'Hanlon GM, Plomp JJ, Wagner ER, Morrison I, Veitch J, Cochrane L, Bullens RWM, Molenaar PC, Conner J, Willison HJ "Monoclonal antibodies raised against Guillain-Barre syndrome- associated Campylobacter jejuni lipopolysaccharides react with neuronal gangliosides and paralyze muscle-nerve preparations" -
Journal of Clinical Investigation 104(6) (1999) 697-708
Guillain-Barre syndrome and its variant, Miller-Fisher syndrome, are acute, postinfectious, autoimmune neuropathies that frequently follow Campylobacter jejuni enteritis. The pathogenesis is believed to involve molecular mimicry between sialylated epitopes on C. jejuni LPSs and neural gangliosides. More than 90% of Miller-Fisher syndrome cases have serum anti-GQ1b and anti-GT1a ganglioside antibodies that may also react with other disialylated gangliosides including GD3 and GD1b. Structural studies on LPS from neuropathy-associated C. jejuni strains have revealed GT1a-like and GD3-like core oligosaccharides. To determine whether this structural mimicry results in pathogenic autoantibodies, we immunized mice with GT1a/GD3-like C. jejuni LPS and then cloned mAb's that reacted with both the immunizing LPS and GQ1b/GT1a/GD3 gangliosides. Immunohistology demonstrated antibody binding to ganglioside-rich sites including motor nerve terminals. In ex vivo electrophysiological studies of nerve terminal function, application of antibodies either ex vivo or in vivo via passive immunization induced massive quantal release of acetylcholine, followed by neurotransmission block. This effect was complement-dependent and associated with extensive deposits of IgM and C3c at nerve terminals. These data provide strong support for the molecular mimicry hypothesis as a mechanism for the induction of cross-reactive pathogenic anti-ganglioside/LPS antibodies in postinfectious neuropathies
Lipopolysaccharide, lipopolysaccharides, antibodies, antibody, monoclonal, monoclonal antibodies, monoclonal antibody, Campylobacter, Campylobacter jejuni, ganglioside, gangliosides, syndrome, preparation, neuronal
NCBI PubMed ID: 10491405Journal NLM ID: 7802877Publisher: Ann Arbor, MI: American Society for Clinical Investigation
Correspondence: gora13@udcf.gla.ac.uk
Institutions: University Department of Neurology, Southern General Hospital, Glasgow G51 4TF, Scotland, Department of Biological Sciences, Glasgow Caledonian University, Glasgow G4 OBA, Scotland, Department of Neurology, Department of Physiology, Leiden University Medical Centre, 2300 RC Leiden, the Netherlands
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5. Compound ID: 1116
a-Neup5Ac-(2-8)-a-Neup5Ac-(2-3)-+
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a-Neup5Ac-(2-8)-a-Neup5Ac-(2-3)-b-D-Galp-(1-3)-b-D-GalpNAc-(1-4)-b-D-Gal-(1-4)-b-D-Glcp-(1-?)-CER |
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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
The structure is contained in the following publication(s):
- 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: 9317004Journal NLM ID: 0246127Publisher: 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
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6. Compound ID: 1117
a-Neup5Ac-(2-3)-+
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a-Neup5Ac-(2-8)-a-Neup5Ac-(2-3)-b-D-Galp-(1-3)-b-D-GalpNAc-(1-4)-b-D-Gal-(1-4)-b-D-Glcp-(1-?)-CER |
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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
The structure is contained in the following publication(s):
- 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: 9317004Journal NLM ID: 0246127Publisher: 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
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7. Compound ID: 1177
a-Neup5Ac-(2-3)-+ EtN-(1--P--6)--+
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a-Neup5Ac-(2-3)-b-D-Galp-(1-3)-b-D-GalpNAc-(1-4)-b-D-Galp-(1-3)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-Kdo
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b-D-Glcp-(1-4)-+ |
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Structure type: oligomer
Compound class: core oligosaccharide, LPS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130648,IEDB_130650,IEDB_134627,IEDB_136044,IEDB_136794,IEDB_137472,IEDB_137473,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141794,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_147450,IEDB_147451,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_23,SB_24,SB_25,SB_39,SB_68,SB_7,SB_70,SB_8,SB_84,SB_88,SB_96,SB_97
The structure is contained in the following publication(s):
- 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: 8603809Journal NLM ID: 9437448Publisher: 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
- Article ID: 369
Schwerer B, Neisser A, Polt RJ, Bernheimer H, Moran AP "Antibody cross-reactivities between gangliosides and lipopolysaccharide of Campylobacter jejuni serotypes associated with Guillain-Barre syndrome" -
Journal of Endotoxin Research 2 (1995) 395-403
Ganglioside-antibodies produced subsequent to Campylobacter jejuni infection may play a role in the pathogenesis of the neurological sidorder Guillain-Barre syndrome (GBS). Since lipopolysaccharides (LPS) of certain C. jejuni serotypes associated with GBS (O:2, O:4, O:19) exhibit structural mimicry of gangliosides in their core oligosaccharides, we investigated antibody and ligand cross-reactivities between gangliosides and LPS of thewe C. jejuni serotypes. GM1-antibody reacted with O:19 LPS reflecting GM1 mimicry by the O:19 core oligosaccharide. On the other hand, asialoGM1-antibody bound to O:2 and L:19 LPS indicating a shared epitope not dependent on ganglioside mimicry. Serum IgA from GBS patients after C. jejuni infection reacted with gangliosides, predominantly GM1, and LPS of all three serotypes. Cholera toxin (GM1 ligand) recognized O:4 and O:19 LPS, whereas peanut agglutinin (Galb(1-3)GalNAc Ligand) recognized LPS of all three serotypes, thereby confirming strucutral mimicry. These results suggest that LPS from certain C. jejuni strains may function as cross-reactive antigens for anti-ganglioside B cells.
LPS, Serotypes, antibodies, Campylobacter jejuni, gangliosides, Guillain-Barre syndrome, mimicry, cross-reactivity
Publication DOI: 10.1177/096805199600200602Journal NLM ID: 9433350Publisher: Maney Publishing
Institutions: Klinisches Institut fur Neurologie, University of Vienna, Vienna, Austria, Department of Microbiology, University College, Galwas, Ireland
Methods: TLC, serological methods
- Article ID: 1773
Aspinall GO, McDonald AG, Pang H, Kurjanczyk LA, Penner JL "Lipopolysaccharides of Campylobacter jejuni Serotype O:19: Structures of core oligosaccharide regions from the serostrain and two bacterial isolates from patients with the Guillain-Barre syndrome" -
Biochemistry 33 (1994) 241-249
Lipopolysaccharides from phenol-water extraction of cells of Campylobacter jejuni serotype O:19 were separated into a water-soluble gel of low M(r) and a water-soluble component of high M(r). Acetic acid hydrolysis of the ketosidic linkages to lipid A furnished respectively a core oligosaccharide, the structure of which is reported herein, and an O antigenic polysaccharide. Structural investigations were performed on the O-deacetylated lipopolysaccharide of low M(r), the liberated core oligosaccharide and the various products from removal of neuraminic acid and phosphate residues, and from the Smith degradation. It is concluded that the lipopolysaccharide from the serostrain has a core region with two types of closely related oligosaccharide chains showing striking homologies with gangliosides, the first with a single N-acetylneuraminic acid residue in an outer chain resembling GM1 and the second with two N-acetyl-neuraminic acid residues with a terminal region resembling GD1a. Similar experiments were carried out on lipopolysaccharides of low M(r) from bacterial isolates OH 4384 and OH 4382 serotyped as O:19 that had been obtained from two patients who subsequently developed the Guillain-Barré syndrome. The core oligosaccharide region of lipopolysaccharide from the former isolate differed only slightly from that of the serostrain, whereas that from the latter isolate was distinctly shorter.
NCBI PubMed ID: 8286348Journal NLM ID: 0370623Publisher: American Chemical Society
Institutions: Department of Chemistry, York University, North York, Toronto, Ontario, Canada
Methods: 13C NMR, 1H NMR, FAB-MS
- 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: 0107600Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
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8. Compound ID: 1184
a-Neup5Ac-(2-3)-+ b-D-Glcp-(1-4)-+
| |
a-Neup5Ac-(2-8)-a-Neup5Ac-(2-3)-b-D-Galp-(1-3)-b-D-GalpNAc-(1-4)-b-D-Galp-(1-3)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-Kdo
|
P-7)-+ |
Show graphically |
Structure type: oligomer
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130648,IEDB_130650,IEDB_134627,IEDB_136044,IEDB_136794,IEDB_137472,IEDB_137473,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141794,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_147450,IEDB_147451,IEDB_149174,IEDB_150933,IEDB_150937,IEDB_153198,IEDB_153199,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_23,SB_24,SB_25,SB_35,SB_39,SB_42,SB_68,SB_7,SB_70,SB_8,SB_84,SB_88,SB_96,SB_97
The structure is contained in the following publication(s):
- Article ID: 365
Salloway S, Mermel LA, Seamans M, Aspinall GO, Nam Shin JE, Kurjanczyk LA, Penner JL "Miller-Fisher syndrome associated with Campylobacter jejuni bearing lipopolysaccharide molecules that mimic human ganglioside GD3" -
Infection and Immunity 64 (1996) 2945-2949
A Campylobacter jejuni strain of serotype O:10 was isolated from a patient who had Miller-Fisher syndrome. In its biochemical reactions and cellular morphology, the isolate was characteristic of typical C. jejuni. Antibodies against extracted lipopolysaccharide (LPS) were detected by passive hemagglutination in the acute- and convalescent-phase patient sera. By sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoblotting with the O:10 antiserum, it was demonstrated that the strain possessed both low- and high-molecular-weight molecules. Chemical analysis of the LPS revealed that the core oligosaccharide has a terminal trisaccharide epitope consisting of two molecules of sialic acid linked to galactose, a structure reflecting the terminal region of human ganglioside GD3. As this trisaccharide is also present in LPS cores of serotype O:19 strains from patients with Guillain-Barre syndrome but not in cores of nonneuropathic C. jejuni, a possible role for the trisaccharide in the etiology of neuropathies is indicated, and a difference for distinguishing neuropathic strains from nonneuropathic strains may be the presence of a sialyltransferase required for the synthesis of this trisaccharide.
LPS, Campylobacter, Campylobacter jejuni, ganglioside, Guillain-Barre syndrome, mimicry, Miller-Fisher syndrome
NCBI PubMed ID: 8757818Journal NLM ID: 0246127Publisher: American Society for Microbiology
Institutions: Department of Neurology, Division of Infectious Diseases, Rhode Island Hospital, Providence, Rhode Island 02903, Department of Chemistry, York University, Toronto, Ontario, Canada M3J 1P3, Deparment of Microbiology, University of Toronto, Toronto, Ontario, Canada M5G 1L5
Methods: serological methods
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9. Compound ID: 1186
b-D-Glcp-(1-2)-+ b-D-Glcp-(1-4)-+
| |
a-Neup5Ac-(2-8)-a-Neup5Ac-(2-3)-b-D-Galp-(1-3)-b-D-GalpNAc-(1-4)-b-D-Galp-(1-3)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-Kdo
|
P-7)-+ |
Show graphically |
Structure type: oligomer
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130648,IEDB_130650,IEDB_134627,IEDB_136044,IEDB_136794,IEDB_137472,IEDB_137473,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141794,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_147450,IEDB_149174,IEDB_150933,IEDB_150937,IEDB_153198,IEDB_153199,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_23,SB_24,SB_25,SB_35,SB_39,SB_42,SB_68,SB_7,SB_70,SB_8,SB_84,SB_88,SB_97
The structure is contained in the following publication(s):
- Article ID: 365
Salloway S, Mermel LA, Seamans M, Aspinall GO, Nam Shin JE, Kurjanczyk LA, Penner JL "Miller-Fisher syndrome associated with Campylobacter jejuni bearing lipopolysaccharide molecules that mimic human ganglioside GD3" -
Infection and Immunity 64 (1996) 2945-2949
A Campylobacter jejuni strain of serotype O:10 was isolated from a patient who had Miller-Fisher syndrome. In its biochemical reactions and cellular morphology, the isolate was characteristic of typical C. jejuni. Antibodies against extracted lipopolysaccharide (LPS) were detected by passive hemagglutination in the acute- and convalescent-phase patient sera. By sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoblotting with the O:10 antiserum, it was demonstrated that the strain possessed both low- and high-molecular-weight molecules. Chemical analysis of the LPS revealed that the core oligosaccharide has a terminal trisaccharide epitope consisting of two molecules of sialic acid linked to galactose, a structure reflecting the terminal region of human ganglioside GD3. As this trisaccharide is also present in LPS cores of serotype O:19 strains from patients with Guillain-Barre syndrome but not in cores of nonneuropathic C. jejuni, a possible role for the trisaccharide in the etiology of neuropathies is indicated, and a difference for distinguishing neuropathic strains from nonneuropathic strains may be the presence of a sialyltransferase required for the synthesis of this trisaccharide.
LPS, Campylobacter, Campylobacter jejuni, ganglioside, Guillain-Barre syndrome, mimicry, Miller-Fisher syndrome
NCBI PubMed ID: 8757818Journal NLM ID: 0246127Publisher: American Society for Microbiology
Institutions: Department of Neurology, Division of Infectious Diseases, Rhode Island Hospital, Providence, Rhode Island 02903, Department of Chemistry, York University, Toronto, Ontario, Canada M3J 1P3, Deparment of Microbiology, University of Toronto, Toronto, Ontario, Canada M5G 1L5
Methods: serological methods
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10. Compound ID: 1334
-4)-a-D-Galp-(1-4)-a-Neup5Ac-(2-3)-b-D-Galp-(1-3)-b-D-GalpNAc-(1- |
Show graphically |
Structure type: suggested polymer biological repeating unit
Aglycon: core
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_130648,IEDB_134627,IEDB_136044,IEDB_136794,IEDB_136906,IEDB_137472,IEDB_137473,IEDB_141794,IEDB_146100,IEDB_147450,IEDB_149174,IEDB_150933,IEDB_151528,IEDB_190606,SB_116,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_195,SB_23,SB_24,SB_25,SB_39,SB_68,SB_7,SB_70,SB_8,SB_84,SB_88,SB_97
The structure is contained in the following publication(s):
- Article ID: 416
Wang L, Briggs CE, Rothemund D, Fratamico P, Luchansky JB, Reeves PR "Sequence of the E. coli O104 antigen gene cluster and identification of O104 specific genes" -
Gene 270(1-2) (2001) 231-236
The Escherichia coli O104 polysaccharide is an important antigen, which contains sialic acid and is often associated with EHEC clones. Sialic acid is a component of many animal tissues, and its presence in bacterial polysaccharides may contribute to bacterial pathogenicity. We sequenced the genes responsible for O104 antigen synthesis and have found genes which from their sequences are identified as an O antigen polymerase gene, an O antigen flippase gene, three CMP-sialic acid synthesis genes, and three potential glycosyl transferase genes. The E. coli K9 group IB capsular antigen has the same structure as the O104 O antigen, and we find using gene by gene PCR that the K9 gene cluster is essentially the same as that for O104. It appears that the distinction between presence as group IB capsule or O antigen for this structure does not involve any difference in genes present in the O antigen gene cluster. By PCR testing against representative strains for the 166 E. coli O antigens and some randomly selected Gram-negative bacteria, we identified three O antigen genes which are highly specific to O104/K9. This work provides the basis for a sensitive test for rapid detection of O104 E. coli. This is important both for decisions on patient care as early treatment may reduce the risk of life-threatening complications and for a faster response in control of food borne outbreaks
biosynthesis, antigen, Escherichia, Escherichia coli, transferase, gene cluster, serotyping, Pathogenic E. coli, Molecular typing
NCBI PubMed ID: 11404020Journal NLM ID: 7706761Publisher: Amsterdam: Elsevier
Correspondence: reeves@angis.org.au
Institutions: Department of Microbiology (GO8), The University of Sydney, Sydney 2006, NSW, Australia, Microbial Food Safety Research Unit, Eastern Regional Research Center, Agricultural Research Service, U.S. Department of Agriculture, 600 East Mermaid Lane, Wyndmoor, PA 19038-8595, USA
Methods: PCR, DNA sequencing
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11. Compound ID: 1358
a-Neup5Ac-(2-3)-+
|
b-D-GalpNAc-(1-4)-b-D-Gal-(1-3)-b-D-GalpNAc-(1--/GD1a/ |
Show graphically |
Structure type: oligomer
Aglycon: GD1a
Trivial name: oligosaccharide epitope
Contained glycoepitopes: IEDB_130648,IEDB_134627,IEDB_136044,IEDB_136095,IEDB_136794,IEDB_137472,IEDB_137473,IEDB_141794,IEDB_146100,IEDB_147450,IEDB_149174,IEDB_150933,IEDB_190606,SB_116,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_195,SB_23,SB_24,SB_25,SB_39,SB_68,SB_7,SB_70,SB_8,SB_84,SB_88,SB_97
The structure is contained in the following publication(s):
- Article ID: 430
Yuki N, Taki T, Handa S "Antibody to GalNAc-GD1a and GalNAc-GMlb in Guillain-Barre syndrome subsequent to Campylobacter jejuni enteritis" -
Journal of Neuroimmunology 71 (1996) 155-161
N-Acetylgalactosaminyl GD1a (GalNAc-GD1a) is a proposed target molecule for serum antibody in some patients with Guillain-Barre syndrome (GBS) (Kusunoki et al., 1994). We examined autoantibody to GalNAc-GD1a in sera from 58 GBS patients. Eight GBS patients had high IgG anti-GalNAc-GD1a antibody titers, 3 of whom also had high IgM anti-GalNAc-GD1a antibody titers. These 8 patients had experienced gastrointestinal infection before the onset of their neurological symptoms. Campylobacter jejuni was isolated from 4 of them. An absorption test indicated the presence of the GalNAc-GD1a epitope in lipopolysaccharides of C. jejuni. Sera that had anti-GalNAc-GD1a antibody reacted with several acidic glycolipids in bovine peripheral nerve, one of which was identified as N-acetylgalactosaminyl GM1b (GalNAc-GM1b). Serum binding to GalNAc-GM1b was decreased by absorption with GalNAc-GD1a. The presence of GalNAc-GM1b as well as GalNAc-GD1a has been reported in human peripheral nerves. We assume that C. jejuni, which bears the [GalNAc β 1-4 (NeuAc α 2-3) Gal β 1-3 GalNAc β 1-] epitope, is the immunogen and that the glycoconjugates with the epitope are target molecules for the autoantibody in peripheral nerves of some GBS patients.
Lipopolysaccharide, autoantibody, Campylobacter jejuni, Guillain-Barre syndrome, Ga1NAc-GD1a, Ga1NAc-GM1b
NCBI PubMed ID: 8982115Journal NLM ID: 8109498Publisher: Elsevier
Correspondence: yuki@dokkyomed.ac.jp
Institutions: Department of Biochemistry, Faculty of Medicine, Tokyo Medical and Dental University, Japan
Methods: ELISA, TLC-immunostaining
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12. Compound ID: 1501
a-Neup5Ac-(2-3)-+ EtN-(1--P--6)--+
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a-Neup5Ac-(2-3)-b-D-Galp-(1-3)-b-D-GalpNAc-(1-4)-b-D-Galp-(1-3)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHep-(1-5)-Kdo
|
b-D-Glcp-(1-4)-+ |
Show graphically |
Structure type: oligomer
Compound class: LOS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130648,IEDB_130650,IEDB_134627,IEDB_136044,IEDB_136794,IEDB_137472,IEDB_137473,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141794,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_147450,IEDB_147451,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_23,SB_24,SB_25,SB_39,SB_68,SB_7,SB_70,SB_8,SB_84,SB_88,SB_96,SB_97
The structure is contained in the following publication(s):
- Article ID: 477
Gilbert M, Godschalk PC, Karwaski MF, Ang CW, Van Belkum A, Li J, Wakarchuk WW, Endtz HP "Evidence for acquisition of the lipooligosaccharide biosynthesis locus in Campylobacter jejuni GB11, a strain isolated from a patient with Guillain-Barre syndrome, by horizontal exchange" -
Infection and Immunity 72(2) (2004) 1162-1165
Campylobacter jejuni GB11, a strain isolated from a patient with Guillain-Barre syndrome, has been shown to be genetically closely related to the completely sequenced strain C. jejuni NCTC 11168 by various molecular typing and serotyping methods. However, we observed that the lipooligosaccharide (LOS) biosynthesis genes strongly diverged between GB11 and NCTC 11168. We sequenced the LOS biosynthesis locus of GB11 and found that it was nearly identical to the class A LOS locus from the C. jejuni HS:19 Penner serotype strain (ATCC 43446). Analysis of the DNA sequencing data showed that a horizontal exchange event involving at least 14.26 kb had occurred in the LOS biosynthesis locus of GB11 between galE (Cj1131c in NCTC 11168) and gmhA (Cj1149 in NCTC 11168). Mass spectrometry of the GB11 LOS showed that GB11 expressed an LOS outer core that mimicked the carbohydrate portion of the gangliosides GM1a and GD1a, similar to C. jejuni ATCC 43446. The serum from the GB11-infected patient was shown to react with the LOS from both GB11 and ATCC 43446 but not with that from NCTC 11168. These data indicate that the antiganglioside response in the GB11-infected patient was raised against the structures synthesized by the acquired class A LOS locus.
biosynthesis, lipopolysaccharides, structure, core, Lipooligosaccharide, chemistry, gene, genetics, human, LOS, metabolism, microbiology, DNA, strain, Support, Non-U.S.Gov't, serotype, analysis, carbohydrate, molecular, Research, locus, Campylobacter, Campylobacter jejuni, class, ganglioside, gangliosides, Guillain-Barre syndrome, immunology, Molecular Sequence Data, response, syndrome, spectrometry, biological, DNA sequencing, mass spectrometry, sequencing, method, methods, serotyping, Base Sequence, serum, acquisition, Chromosome Mapping, event, exchange, galE, U.S.Gov't, Non-P.H.S., typing, PDF
NCBI PubMed ID: 14742567Journal NLM ID: 0246127Publisher: American Society for Microbiology
Correspondence: michel.gilbert@nrc.cnrc.gc.ca
Institutions: Institute for Biological Sciences, National Research Council Canada, Ottawa, Ontario, Canada
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13. Compound ID: 1861
b-D-Glcp-(1-2)-+ EtN-(1--P--6)--+
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a-Neup5Ac-(2-8)-a-Neup5Ac-(2-3)-b-D-Galp-(1-3)-b-D-GalpNAc-(1-3)-b-D-Galp-(1-3)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/
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b-D-Glcp-(1-4)-+ |
Show graphically |
Structure type: oligomer
Aglycon: lipid A
Compound class: LPS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130648,IEDB_130650,IEDB_134627,IEDB_136044,IEDB_136794,IEDB_137472,IEDB_137473,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141794,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_147450,IEDB_149174,IEDB_150933,IEDB_150937,IEDB_153198,IEDB_153199,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_21,SB_23,SB_24,SB_35,SB_39,SB_42,SB_68,SB_7,SB_70,SB_8,SB_84,SB_88,SB_97
The structure is contained in the following publication(s):
- Article ID: 600
Ang CW, Laman JD, Willison HJ, Wagner ER, Endtz HP, De Klerk MA, Tio-Gillen AP, Van Den BN, Jacobs BC, Doorn PA "Structure of Campylobacter jejuni lipopolysaccharides determines antiganglioside specificity and clinical features of Guillain-Barre and Miller Fisher patients" -
Infection and Immunity 70(3) (2002) 1202-1208
Ganglioside mimicry in the lipopolysaccharide (LPS) fraction of Campylobacter jejuni isolated from Guillain-Barre syndrome (GBS) and Miller Fisher syndrome (MFS) patients was compared with isolates from patients with an uncomplicated enteritis. The antibody response to C. jejuni LPS and gangliosides in neuropathy patients and controls was compared as well. LPS from GBS and MFS-associated isolates more frequently contained ganglioside-like epitopes compared to control isolates. Almost all neuropathy patients showed a strong antibody response against LPS and multiple gangliosides in contrast to enteritis patients. Isolates from GBS patients more frequently had a GM1-like epitope than isolates from MFS patients. GQ1b-like epitopes were present in all MFS-associated isolates and was associated with anti- GQ1b antibody reactivity and the presence of oculomotor symptoms. These results demonstrate that the expression of ganglioside mimics is a risk factor for the development of post-Campylobacter neuropathy. This study provides additional evidence for the hypothesis that the LPS fraction determines the antiganglioside specificity and clinical features in post-Campylobacter neuropathy patients
lipopolysaccharides, antibody response, Campylobacter jejuni, ganglioside, GQ1b, Miller Fisher syndrome
NCBI PubMed ID: 11854201Journal NLM ID: 0246127Publisher: American Society for Microbiology
Correspondence: Ang@bacl.azr.nl
Institutions: Departments of Neurology. Immunology. Microbiology and Infectious Diseases, Erasmus University/Academic Hospital Dijkzigt Rotterdam, Rotterdam, The Netherlands. Department of Neurology, Southern General Hospital, Glasgow G51 4TF, Scotland
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14. Compound ID: 1862
a-Neup5Ac-(2-3)-+ EtN-(1--P--6)--+
| |
a-Neup5Ac-(2-3)-b-D-Galp-(1-3)-b-D-GalpNAc-(1-4)-b-D-Galp-(1-3)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/
|
b-D-Glcp-(1-4)-+ |
Show graphically |
Structure type: oligomer
Aglycon: lipid A
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130648,IEDB_130650,IEDB_134627,IEDB_136044,IEDB_136794,IEDB_137472,IEDB_137473,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141794,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_147450,IEDB_147451,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_23,SB_24,SB_25,SB_39,SB_68,SB_7,SB_70,SB_8,SB_84,SB_88,SB_96,SB_97
The structure is contained in the following publication(s):
- Article ID: 600
Ang CW, Laman JD, Willison HJ, Wagner ER, Endtz HP, De Klerk MA, Tio-Gillen AP, Van Den BN, Jacobs BC, Doorn PA "Structure of Campylobacter jejuni lipopolysaccharides determines antiganglioside specificity and clinical features of Guillain-Barre and Miller Fisher patients" -
Infection and Immunity 70(3) (2002) 1202-1208
Ganglioside mimicry in the lipopolysaccharide (LPS) fraction of Campylobacter jejuni isolated from Guillain-Barre syndrome (GBS) and Miller Fisher syndrome (MFS) patients was compared with isolates from patients with an uncomplicated enteritis. The antibody response to C. jejuni LPS and gangliosides in neuropathy patients and controls was compared as well. LPS from GBS and MFS-associated isolates more frequently contained ganglioside-like epitopes compared to control isolates. Almost all neuropathy patients showed a strong antibody response against LPS and multiple gangliosides in contrast to enteritis patients. Isolates from GBS patients more frequently had a GM1-like epitope than isolates from MFS patients. GQ1b-like epitopes were present in all MFS-associated isolates and was associated with anti- GQ1b antibody reactivity and the presence of oculomotor symptoms. These results demonstrate that the expression of ganglioside mimics is a risk factor for the development of post-Campylobacter neuropathy. This study provides additional evidence for the hypothesis that the LPS fraction determines the antiganglioside specificity and clinical features in post-Campylobacter neuropathy patients
lipopolysaccharides, antibody response, Campylobacter jejuni, ganglioside, GQ1b, Miller Fisher syndrome
NCBI PubMed ID: 11854201Journal NLM ID: 0246127Publisher: American Society for Microbiology
Correspondence: Ang@bacl.azr.nl
Institutions: Departments of Neurology. Immunology. Microbiology and Infectious Diseases, Erasmus University/Academic Hospital Dijkzigt Rotterdam, Rotterdam, The Netherlands. Department of Neurology, Southern General Hospital, Glasgow G51 4TF, Scotland
- 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: 12183556Publication DOI: 10.1128/IAI.70.9.5081-5085.2002Journal NLM ID: 0246127Publisher: American Society for Microbiology
Correspondence: Ang@Bacl.azr.nl
Institutions: Department of Medical Microbiology and Infectious Diseases, Erasmus University Medical Centre, Rotterdam, The Netherlands
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15. Compound ID: 2042
a-Neup5Ac-(2-3)-+
|
a-Neup5Ac-(2-3)-b-D-Galp-(1-3)-b-D-GalpNAc-(1-4)-b-D-Galp-(1-3)-HEP-(?--/inner core/ |
Show graphically |
Structure type: oligomer
Aglycon: inner core
Compound class: LOS
Contained glycoepitopes: IEDB_130648,IEDB_134627,IEDB_136044,IEDB_136794,IEDB_137472,IEDB_137473,IEDB_141794,IEDB_146100,IEDB_147450,IEDB_147451,IEDB_149174,IEDB_150933,IEDB_190606,SB_116,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_195,SB_23,SB_24,SB_25,SB_39,SB_68,SB_7,SB_70,SB_8,SB_84,SB_88,SB_96,SB_97
The structure is contained in the following publication(s):
- Article ID: 646
Gilbert M, Brisson J, Karwaski M, Michniewicz J, Cunningham A, Wu Y, Young NM, Wakarchuk WW "Biosynthesis of ganglioside mimics in Campylobacter jejuni OH4384. Identification of the glycosyltransferase genes, enzymatic synthesis of model compounds, and characterization of nanomole amounts by 600-MHz 1H and 13C NMR analysis" -
Journal of Biological Chemistry 275(6) (2000) 3896-3906
We have applied two strategies for the cloning of four genes responsible for the biosynthesis of the GT1a ganglioside mimic in the lipooligosaccharide (LOS) of a bacterial pathogen, Campylobacter jejuni OH4384, which has been associated with Guillain-Barre syndrome. We first cloned a gene encoding an α-2, 3-sialyltransferase (cst-I) using an activity screening strategy. We then used nucleotide sequence information from the recently completed sequence from C. jejuni NCTC11168 to amplify a region involved in LOS biosynthesis from C. jejuni OH4384. The LOS biosynthesis locus from C. jejuni OH4384 is 11.47 kilobase pairs and encodes 13 partial or complete open reading frames, while the corresponding locus in C. jejuni NCTC11168 spans 13.49 kilobase pairs and contains 15 open reading frames, indicating a different organization between these two strains. Potential glycosyltransferase genes were cloned individually, expressed in Escherichia coli, and assayed using synthetic fluorescent oligosaccharides as acceptors. We identified genes encoding a β-1,4-N-acetylgalactosaminyl-transferase (cgtA), a β-1,3-galactosyltransferase (cgtB), and a bifunctional sialyltransferase (cst-II), which transfers sialic acid to O-3 of galactose and to O-8 of a sialic acid that is linked α-2,3- to a galactose. The linkage specificity of each identified glycosyltransferase was confirmed by NMR analysis at 600 MHz on nanomole amounts of model compounds synthesized in vitro. Using a gradient inverse broadband nano-NMR probe, sequence information could be obtained by detection of (3)J(C,H) correlations across the glycosidic bond. The role of cgtA and cst-II in the synthesis of the GT1a mimic in C. jejuni OH4384 were confirmed by comparing their sequence and activity with corresponding homologues in two related C. jejuni strains that express shorter ganglioside mimics in their LOS.
Lipooligosaccharide, gene, Campylobacter jejuni, ganglioside, sialyltransferase, glycosyltransferase, NMR analysis, enzymatic synthesis
NCBI PubMed ID: 10660542Publication DOI: 10.1074/jbc.275.6.3896Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: warren.wakarchuk@nrc.ca
Institutions: Institute for Biological Sciences, National Research Council of Canada, Ottawa, Ontario K1A 0R6, Canada.
Methods: NMR-2D
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