Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Campylobacter jejuni [ICD11:
XN4Q5 
]
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
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
Structure type: oligomer
Location inside paper: Fig. 1
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
Biological activity: binds to TT-peroxydaze, MAb Ha1rbc, MAb EG1, MAb CGM3
Biosynthesis and genetic data: serological data
Comments, role: two unspecified α-heptoses were assumed to be a-LDmanHepp by annotator
Related record ID(s): 294, 295
NCBI Taxonomy refs (TaxIDs): 197Reference(s) to other database(s): GTC:G93064IM
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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