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Taxonomic group: bacteria / Proteobacteria (Phylum: Proteobacteria)
Host organism: Homo sapiens
Associated disease: respiratory diseases [ICD11: 12

]; pertussis (whooping cough) [ICD11: 1C12.Z

, ICD11: XN9W3

]; infection due to Bordetella pertussis [ICD11: XN23B

]; infection due to Bordetella bronchiseptica [ICD11: XN173

]

The structure was elucidated in this paper
NCBI PubMed ID: 21367691
Publication DOI: 10.1073/pnas.1100782108
Journal NLM ID: 7505876
Publisher: National Academy of Sciences
Correspondence: kielbj

mail.nih.gov
Institutions: Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, USA.

Pertussis is a highly contagious respiratory disease that is especially dangerous for infants and children. Despite mass vaccination, reported pertussis cases have increased in the United States and other parts of the world, probably because of increased awareness, improved diagnostic means, and waning vaccine-induced immunity among adolescents and adults. Licensed vaccines do not kill the organism directly; the addition of a component inducing bactericidal antibodies would improve vaccine efficacy. We investigated Bordetella pertussis and Bordetella bronchiseptica LPS-derived core oligosaccharide (OS) protein conjugates for their immunogenicity in mice. B. pertussis and B. bronchiseptica core OS were bound to aminooxylated BSA via their terminal Kdo residues. The two conjugates induced similar anti-B. pertussis LPS IgG levels in mice. B. bronchiseptica was investigated because it is easier to grow than B. pertussis. Using B. bronchiseptica genetically modified strains deficient in the O-specific polysaccharide, we isolated fractions of core OS with one to five repeats of the terminal trisaccharide, having at the nonreducing end a GlcNAc or GalNAc, and bound them to BSA at different densities. The highest antibody levels in mice were elicited by conjugates containing an average of 8-17 OS chains per protein and with one repeat of the terminal trisaccharide. Conjugate-induced antisera were bactericidal against B. pertussis, and the titers correlated with ELISA-measured antibody levels (r = 0.74). Such conjugates are easy to prepare and standardize; added to a recombinant pertussis toxoid, they may induce antibacterial and antitoxin immunity.

Gram-negative, hydroxylamine

Structure type: oligomer
Location inside paper: p.4088, fig.1, band A
Aglycon: lipid A
Compound class: core oligosaccharide with O-unit
Contained glycoepitopes: IEDB_115136,IEDB_130650,IEDB_137340,IEDB_137777,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_140630,IEDB_141807,IEDB_142345,IEDB_142488,IEDB_146664,IEDB_151531,IEDB_2189047,IEDB_2275071,IEDB_983931,SB_192

Methods: NMR, SDS-PAGE, ESI-MS, Western blotting, MALDI-TOF MS, serological methods, conjugation
Biological activity: serological data,immunological data
Comments, role: In B. bronchiseptica RB50, 50% of N-4 of FucNAc4N were methylated and 30% of O-4 of the Hep substituted with GlcA was phosphorylated.

NCBI Taxonomy refs (TaxIDs): 520, 257310
Reference(s) to other database(s): GTC:G24502SK
Show glycosyltransferases

There is only one chemically distinct structure:

CN[C@@H]1[C@H](O[C@@H]2O[C@H](C(=O)O)[C@@H](O[C@H]3O[C@H](CO)[C@@H](O)[C@H](O)[C@H]3NC(C)=O)[C@H](NC(C)=O)[C@@H]2NC(C)=O)[C@@H](NC(C)=O)[C@@H](OC[C@H]2O[C@H](O[C@@H]3[C@@H](CO[C@H]4O[C@H](C(=O)O)[C@H](O)[C@H](O)[C@H]4N)O[C@@H](O[C@@H]4[C@@H]([C@@H](O)CO)O[C@H](O[C@@H]5[C@H](OP(=O)(O)O)C[C@](O)(C(=O)O)O[C@@H]5[C@H](O)CO)[C@@H](O)[C@H]4O[C@H]4O[C@H]([C@@H](O)CO[C@H]5O[C@H](CO)[C@@H](O)[C@H](O)[C@H]5N)[C@@H](OP(=O)(O)O)[C@H](O)[C@@H]4O[C@H]4O[C@H](C(=O)O)[C@@H](O)[C@H](O)[C@H]4O)[C@H](O)[C@H]3O)[C@H](N)[C@@H](O)[C@@H]2O[C@H]2O[C@H]([C@@H](O)CO)[C@@H](O)[C@H](O)[C@@H]2O)O[C@@H]1C

SVG MW SMILES 3D mol Ionize