Found 52 structures.
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1. Compound ID: 106
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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: 108
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a-Neup5Ac-(2-8)-a-Neup5Ac-(2-3)-b-D-Galp-(1--/Glcp(1-1)ceramide (ganglioside GD3) or the inner core-lipid A (lipopolysaccharide))/ |
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Structure type: oligomer
Aglycon: Glcp(1-1)ceramide (ganglioside GD3) or the inner core-lipid A (lipopolysaccharide))
Trivial name: GD1a
Contained glycoepitopes: IEDB_136044,IEDB_136794,IEDB_137472,IEDB_141794,IEDB_146100,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_35,SB_39,SB_42,SB_68,SB_7,SB_84,SB_88
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
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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: 870
Structure type: oligomer
Aglycon: lipid A
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_136044,IEDB_136794,IEDB_137472,IEDB_141794,IEDB_146100,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_35,SB_39,SB_42,SB_68,SB_7,SB_84,SB_88
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: 871
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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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6. Compound ID: 1116
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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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7. Compound ID: 1117
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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 |
Show graphically |
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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8. Compound ID: 1118
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b-D-GalpNAc-(1-4)-+
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a-Neup5Ac-(2-8)-a-Neup5Ac-(2-3)-b-D-Gal-(1-4)-b-D-Glcp-(1-?)-CER |
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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
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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9. Compound ID: 1184
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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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10. Compound ID: 1185
|
b-D-Glcp-(1-4)-+
|
a-Neup5Ac-(2-8)-a-Neup5Ac-(2-3)-b-D-Galp-(1-3)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-Kdo
|
P-6)-+ |
Show graphically |
Structure type: oligomer
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130650,IEDB_136044,IEDB_136794,IEDB_137472,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141794,IEDB_142488,IEDB_146100,IEDB_146664,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_35,SB_39,SB_42,SB_68,SB_7,SB_84,SB_88
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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11. 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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12. Compound ID: 1427
|
a-D-Glcp-(1-4)-+
|
a-Neup5Ac-(2-8)-a-Neup5Ac-(2-3)-b-D-Galp-(1-3)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1--/Kdo-lipid A/ |
Show graphically |
Structure type: oligomer
Aglycon: Kdo-lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_136044,IEDB_136794,IEDB_137472,IEDB_140088,IEDB_141794,IEDB_142488,IEDB_144998,IEDB_146100,IEDB_146664,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_35,SB_39,SB_42,SB_68,SB_7,SB_84,SB_88
The structure is contained in the following publication(s):
- Article ID: 450
Hori K, Sawada N, Ando H, Ishida H, Kiso M "Synthetic study on Campylobacter jejuni lipopolysaccharides: an improved synthesis of a branched, heptose-containing trisaccharide core structure and its conversion into ganglioside GD3 related hexasaccharide" -
European Journal of Organic Chemistry (19) (2003) 3752-3760
The first synthesis of the oligosaccharide skeleton of the Campylobacter jejuni lipooligosaccharide composed of a branched, heptose-containing trisaccharide core structure and, including a substantially improved preparation of the core structure, the ganglioside GD3 related trisaccharide epitope is reported.
carbohydrates, heptose, Oligosaccharides, natural products, Bioorganic chemistry, Ganglioside GD3
Publication DOI: 10.1002/ejoc.200300309Journal NLM ID: 9805750Publisher: Wiley-VCH
Correspondence: ishida@cc.gifu-u.ac.jp
Institutions: Synthetic Studies on Sialoglycoconjugates, Department of Applied Bioorganic Chemistry, Gifu University, Gifu 501-1193, Japan
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13. Compound ID: 1861
|
b-D-Glcp-(1-2)-+ EtN-(1--P--6)--+
| |
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/
|
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: 2043
|
b-D-Glcp-(1-2)-+ EtN-(1--P--7)--+
| |
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
|
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_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: 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: 11689567Journal NLM ID: 2985121RPublisher: 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
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15. Compound ID: 2157
|
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
|
/Variants 0/-+
/Variants 0/ is:
P-7)-
OR (exclusively)
P-6)- |
Show graphically |
Structure type: oligomer
Compound class: LOS
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: 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: 11689567Journal NLM ID: 2985121RPublisher: 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
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Next 15 structure(s)
Total list of structure IDs on all result pages of the current query:
Total list of corresponding CSDB IDs (record IDs):
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