Found 64 structures.
Displayed structures from 1 to 15
Next 15 structure(s)
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1. Compound ID: 106
a-Neup5Ac-(2-8)-a-Neup5Ac-(2-3)-+
|
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: 107
a-Neup5Ac-(2-3)-+
|
b-D-Galp-(1-3)-b-D-GalpNAc-(1-4)-b-D-Galp-(1--/Glcp(1-1)ceramide (ganglioside GM1) or the inner core-lipid A (lipopolysaccharide)/ |
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Structure type: oligomer
Aglycon: Glcp(1-1)ceramide (ganglioside GM1) or the inner core-lipid A (lipopolysaccharide)
Trivial name: ganglioside GM1
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_8,SB_84,SB_88,SB_96
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: 109
a-Neup5Ac-(2-3)-+
|
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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4. Compound ID: 110
a-Neup5Ac-(2-3)-+
|
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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5. Compound ID: 170
b-D-Glcp-(1-2)-+
|
a-D-Galp-(1-2)-+ |
| |
a-Neup5Ac-(2-3)-+ | | /Variants 0/-+
| | | |
b-D-Galp-(1-3)-b-D-GalpNAc-(1-4)-b-D-Galp-(1-3)-b-D-Galp-(1-3)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-Kdop-(2--/lipid A/
|
b-D-Glcp-(1-4)-+
/Variants 0/ is:
P-6)-
OR (exclusively)
EtN-(1--P--6)-- |
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Structure type: oligomer
Aglycon: lipid A
Compound class: core oligosaccharide, LPS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130648,IEDB_130650,IEDB_131186,IEDB_134627,IEDB_135818,IEDB_136044,IEDB_136794,IEDB_136906,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_151528,IEDB_167072,IEDB_190606,IEDB_2189047,IEDB_742245,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_8,SB_84,SB_88,SB_96
The structure is contained in the following publication(s):
- Article ID: 36
Caroff M, Karibian D "Structure of bacterial lipopolysaccharides" -
Carbohydrate Research 338(23) (2003) 2431-2447
Bacterial lipopolysaccharides are the major components of the outer surface of Gram-negative bacteria They are often of interest in medicine for their immunomodulatory properties. In small amounts they can be beneficial, but in larger amounts they may cause endotoxic shock. Although they share a common architecture, their structural details exert a strong influence on their activity. These molecules comprise: a lipid moiety, called lipid A, which is considered to be the endotoxic component, a glycosidic part consisting of a core of approximately 10 monosaccharides and, in 'smooth-type' lipopolysaccharides, a third region, named O-chain, consisting of repetitive subunits of one to eight monosaccharides responsible for much of the immunospecificity of the bacterial cell.
Lipopolysaccharide, structure, core, lipid A, endotoxin, O-chains
NCBI PubMed ID: 14670707Publication DOI: 10.1016/j.carres.2003.07.010Journal NLM ID: 0043535Publisher: Elsevier
Correspondence: martine.carloff@bbmpc.u-psud.fr
Institutions: Equipe Endotoxines, UMR 8619 du Centre National de la Recherche Scientifique, IBBMC, Université de Paris-Sud, F-Orsay, France
- Article ID: 3820
Banoub JH, El Aneed A, Cohen AM, Joly N "Structural investigation of bacterial lipopolysaccharides by mass spectrometry and tandem mass spectrometry" -
Mass Spectrometry Reviews 29(4) (2010) 606-650
Mass spectrometric studies are now playing a leading role in the elucidation of lipopolysaccharide (LPS) structures through the characterization of antigenic polysaccharides, core oligosaccharides and lipid A components including LPS genetic modifications. The conventional MS and MS/MS analyses together with CID fragmentation provide additional structural information complementary to the previous analytical experiments, and thus contribute to an integrated strategy for the simultaneous characterization and correct sequencing of the carbohydrate moiety.
LPS, O-antigen, lipid A, core oligosaccharide, MS and MS/MS analyses
NCBI PubMed ID: 20589944Publication DOI: 10.1002/mas.20258Journal NLM ID: 8219702Publisher: Wiley
Correspondence: joe.banoub@dfo-mpo.gc.ca
Institutions: Fisheries and Oceans Canada, Science Branch, Special Projects, P.O. Box 5667, St. John's, Newfoundland, Canada A1C 5X1, Department of Chemistry, Memorial University of Newfoundland, St. John's, Newfoundland, Canada A1B 3V6, College of Pharmacy and Nutrition, University of Saskatchewan, Thorvaldson Building, 110 Science Place, Saskatoon, Saskatchewan, Canada S7N 5C9, Unité de Catalyse et de Chimie du Solide, Site de l'Artois—UMR CNRS 8181, I.U.T. de Béthune, Département Chimie, 1230 rue de l'Université, BP819, 62408 Béthune Cedex, France, Institute for Marine Biosciences Room 219A, (NRC-IMB), National Research Council of Canada, Government of Canada, 1411 Oxford Street, Halifax, NS, Canada B3H 3Z1
Methods: MS/MS, MS
- Article ID: 3868
Kabanov DS, Prokhorenko IR "Structural analysis of lipopolysaccharides from Gram-negative bacteria" -
Biochemistry (Moscow) 75(4) (2010) 383-404
This review covers data on composition and structure of lipid A, core, and O-polysaccharide of the known lipopolysaccharides from Gram-negative bacteria. The relationship between the structure and biological activity of lipid A is discussed. The data on roles of core and O-polysaccharide in biological activities of lipopolysaccharides are presented. The structural homology of some oligosaccharide sequences of lipopolysaccharides to gangliosides of human cell membranes is considered.
core, Lipooligosaccharide, O-antigen, lipid A, gangliosides, cytokines, lipopolysaccharide (endotoxin)
NCBI PubMed ID: 20618127Publication DOI: 10.1134/S0006297910040012Journal NLM ID: 0376536Publisher: Nauka/Interperiodica
Correspondence: kabanovd1@rambler.ru
Institutions: Institute of Basic Biological Problems, Russian Academy of Sciences, Pushchino, Russia
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6. Compound ID: 869
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_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_8,SB_84,SB_88,SB_96
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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7. Compound ID: 871
a-Neup5Ac-(2-3)-+
|
a-Neup5Ac-(2-8)-a-Neup5Ac-(2-3)-b-D-Galp-(1-3)-b-D-GalpNAc-(1-4)-b-D-Galp-(1--/lipid A/ |
Show graphically |
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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8. Compound ID: 1116
a-Neup5Ac-(2-8)-a-Neup5Ac-(2-3)-+
|
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: 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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9. Compound ID: 1117
a-Neup5Ac-(2-3)-+
|
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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10. Compound ID: 1165
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)-Kdo
|
b-D-Glcp-(1-4)-+ |
Show graphically |
Structure type: oligomer
Compound class: core oligosaccharide
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_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_8,SB_84,SB_88,SB_96
The structure is contained in the following publication(s):
- Article ID: 354
Prendergast MM, Lastovica AJ, Moran AP "Lipopolysaccharides from Campylobacter jejuni O:41 strains associated with Guillain-Barre syndrome exhibit mimicry of GM1 ganglioside" -
Infection and Immunity 66(8) (1998) 3649-3655
Three Campylobacter jejuni, biotype 2, serotype O:41 strains that were isolated from patients who developed Guillain-Barre syndrome (GBS) and one C. jejuni isolate from a patient who developed enteritis only were examined. The aim of the study was to determine the structure of the core oligosaccharide (OS) of the lipopolysaccharide (LPS) of C. jejuni serotype O:41, a serotype rarely associated with the development of GBS, and to determine if the LPS shares similar epitopes with any of the major human gangliosides. Electrophoretic analysis with silver staining or immunoblotting demonstrated that the strains had LPS profiles characteristic of low-molecular-weight LPS. Colorimetric analysis detected N-acetylneuraminic (sialic) acid in the core OSs of all the strains. Thin-layer chromatography with immunostaining showed that antisera raised against the GBS strains reacted with the GM1 ganglioside, suggesting that C. jejuni serotype O:41 LPSs and the GM1 ganglioside have similar epitopes. Furthermore, polyclonal anti-GM1 and anti-asialoGM1 antibodies cross-reacted with each C. jejuni O:41 LPS tested, suggesting that the serotype O:41 core OS has a GM1- and asialoGM1-like structure. LPSs extracted from C. jejuni serostrains O:2, O:3, and O:19 were also used in the study. Cholera toxin (a GM1 ligand) and peanut agglutinin (a Galβ1-3GalNAc ligand) recognized all serotype O:41 LPSs and the serostrain O:2 LPS. Immunoadsorption results confirmed GM1 relatedness. Moreover, the core OS was isolated from a GBS-associated C. jejuni O:41 LPS by gel permeation chromatography. An analysis by gas-liquid chromatography (GLC), GLC-mass spectrometry, and nuclear magnetic resonance showed the core OS of one of the C. jejuni O:41 GBS isolates to have a tetrasaccharide structure consistent with GM1 mimicry.
lipopolysaccharides, Campylobacter, Campylobacter jejuni, ganglioside, Guillain-Barre syndrome, GM1
NCBI PubMed ID: 9673245Journal NLM ID: 0246127Publisher: American Society for Microbiology
Correspondence: anthony.moran@ucg.ie
Institutions: Department of Microbiology, National University of Ireland, Galway, Ireland, Department of Medical Microbiology, Red Cross Children's Hospital, Rondebosch, Cape Town, South Africa
Methods: GLC-MS, NMR, GLC, electrophoresis, TLC-immunostaining, colorimetry
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11. Compound ID: 1177
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)-Kdo
|
b-D-Glcp-(1-4)-+ |
Show graphically |
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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12. Compound ID: 1178
a-Neup5Ac-(2-3)-+ EtN-(1--P--6)--+
| |
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: 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_8,SB_84,SB_88,SB_96
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
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13. 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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14. Compound ID: 1501
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-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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15. Compound ID: 1546
a-Neup5Ac-(2-3)-+ EtN-(1--P--6)--+
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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)-a-Kdo
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b-D-Glcp-(1-4)-+ |
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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_8,SB_84,SB_88,SB_96
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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