Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Host organism: Homo sapiens
Associated disease: meningitis [ICD11:
1D01 
];
septicemia [ICD11:
MA15.Y ];
pneumonia [ICD11:
CA40 ];
infection due to Neisseria meningitidis [ICD11:
XN1DV ]
NCBI PubMed ID: 29940397Publication DOI: 10.1016/j.carres.2018.06.007Journal NLM ID: 0043535Publisher: Elsevier
Correspondence: neil.ravenscroft
uct.ac.za
Institutions: Department of Chemistry, University of Cape Town, Rondebosch, 7701, South Africa, Department of Computer Science, University of Cape Town, Rondebosch, 7701, South Africa
Neisseria meningitidis is a major cause of bacterial meningitis worldwide especially in Africa. The capsular polysaccharide (CPS) is the main virulence factor and the target antigen for polysaccharide and conjugate vaccines. The high burden of serogroup A disease in the Meningitis Belt of sub-Saharan Africa led to the introduction of MenAfriVac®, which has successfully reduced the number of cases of group A disease. However, several outbreaks caused by other serogroups have been reported, including those due to serogroup X. The capsular polysaccharides of serogroups A and X are both homopolymers of amino sugars (?-D-ManNAc and ?-D-GlcNAc) containing phosphodiester linkages at C-6 and C-4, respectively. The similarity of the primary structures of the two polysaccharides suggests that serogroup A vaccination may provide cross-protection against serogroup X disease. Molecular dynamics simulations of a series of serogroup A and X oligosaccharides reveal that the MenA CPS behaves as a flexible random coil which becomes less conformationally defined as the length increases, whereas serogroup X forms a more stable regular helical structure. The presence of the MenX helix is supported by NMR analysis; it has four residues per turn and becomes more stable as the chain length increases. Licensed MenA vaccines are largely O-acetylated at C-3: simulations show that these O-acetyl groups are highly solvent exposed and their presence favors more extended conformations compared to the more compact conformations of MenA without O-acetylation. These findings may have implications for the design of optimal conjugate vaccines.
Neisseria meningitidis, capsular polysaccharide, molecular modeling, Antigen conformation
Structure type: homopolymer
Location inside paper: p.44, A
Compound class: CPS
Contained glycoepitopes: IEDB_1330666,IEDB_1330667,IEDB_1330668,IEDB_1330669,IEDB_1330670,IEDB_1330671,IEDB_149549,IEDB_149550,IEDB_149551,IEDB_149552
Methods: conformation analysis, MD simulations, post-simulation analysis
3D data: 3D data, molecular modeling
Related record ID(s): 12611, 12612, 12613, 12614, 12615
NCBI Taxonomy refs (TaxIDs): 65699Reference(s) to other database(s): GTC:G04962CQ
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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