Gremyakova TA, Vinogradov EV, Lindner B, Kocharova NA, Senchenkova SN, Shashkov AS, Knirel YA, Holst O, Shaikhutdinova RZ, Anisimov AP The core structure of the lipopolysaccharide of Yersinia pestis strain KM218. Influence of growth temperature Advances in Experimental Medicine and Biology529 (2003)
229-232
core structure, Yersinia enterocolitica, Growth Temperature, Yersinia pestis, Full Structure
NCBI PubMed ID:12756762 Journal NLM ID:0121103 Publisher: Kluwer Academic/Plenum Publishers Institutions: State Research Center for Applied Microbiology, Obolensk, Moscow Region, Russia, N.D. Zelinsky Institute of Organic Chemistry, Russian Academy od Sciences, Moscow, Russia, Research Center Borstel, Center for Medicine und Biosciences, Borstel, Germany Methods: methylation, NMR-2D, NMR, ESI-MS, ESI-ICR-MS
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Griffiss JM, Brandt BL, Saunders NB, Zollinger W Structural relationships and sialylation among meningococcal L1, L8, and L3,7 lipooligosaccharide serotypes Journal of Biological Chemistry275(13) (2000)
9716-9724
Eighteen of 34 endemic meningococcal case strains were of the L8 lipooligosaccharide (LOS) type; four of these were both L3 and L7 (L3,7), and seven were L1. L1 structures arose by alternative terminal Gal substitutions of lactosyl diheptoside L8 structures, as determined by electrospray ionization and other mass spectrometric techniques, and enzymatic and chemical degradations (Structures L1 and L1a). [see text for structure] The more abundant molecule, designated L1, had a trihexose globosyl alpha chain; the less abundant one, designated L1a, had a β-lactosyl alpha chain and a parallel α-lactosaminyl gamma chain. A P(k) globoside (Gal α1→4 Gal β1→4 Glc-R) monoclonal antibody bound 9/10 L1 strains, but a P(1) globoside (Gal α1→4 Gal β1→4 GlcNAc-R) mAb bound none of them. α-Galactosidase caused loss of both L1 structures and creation of L8 structures; β-galactosidase caused loss of the L8 determinant. The L1/P(k) glycose was partially sialylated. Some LOS also had unsubstituted basal β-GlcNAc additions. These structural relationships explain co-expression of L8, L1, and L3,7 serotypes.
NCBI PubMed ID:10734124 Journal NLM ID:2985121R Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology Correspondence: crapaudvacom.ucsf.edu Institutions: Centre for Immunochemistry and Department of Laboratory Medicine, University of California, San Francisco, California 94121, Department of Bacterial Diseases, Walter Reed Army Institute of Research, Washington, D. C. 20307 Methods: dephosphorylation, ESI-MS, MS/MS, enzymatic degradation, LSI-MS
The publication contains the following compound(s):
Michael FS, Szymanski CM, Li J, Chan KH, Khieu NH, Larocque S, Wakarchuk WW, Brisson JR, Monteiro MA The structures of the lipooligosaccharide and capsule polysaccharide of Campylobacter jejuni genome sequenced strain NCTC11168 European Journal of Biochemistry269(21) (2002)
5119-5136
Campylobacter jejuni infections are one of the leading causes of human gastroenteritis and are suspected of being a precursor to Guillain- Barre and Miller-Fisher syndromes. Recently, the complete genome sequence of C. jejuni NCTC11168 was described. In this study, the molecular structure of the lipooligosaccharide and capsular polysaccharide of C. jejuni NCTC11168 was investigated. The lipooligosaccharide was shown to exhibit carbohydrate structures analogous to the GM1a and GM2 carbohydrate epitopes of human gangliosides (shown below): The high Mr capsule polysaccharide was composed of β-D-Ribp, β-D-GalfNAc, α-D-GlcpA6(NGro), a uronic acid amidated with 2-amino-2-deoxyglycerol at C-6, and 6-O-methyl-d-glycero-α-l-gluco-heptopyranose as a side-branch (shown below): . The structural information presented here will aid in the identification and characterization of specific enzymes that are involved in the biosynthesis of these structures and may lead to the discovery of potential therapeutic targets. In addition, the correlation of carbohydrate structure with gene complement will aid in the elucidation of the role of these surface carbohydrates in C. jejuni pathogenesis.
NCBI PubMed ID:12392544 Publication DOI:10.1046/j.1432-1033.2002.03201.x Journal NLM ID:0107600 Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies Correspondence: jean-robert.brissonnrc.ca; Monteimwyeth.com Institutions: Institute for Biological Sciences, National Research Council of Canada, Ottawa, Canada, Wyeth Vaccines Research, 211 Bailey Road, West Henrietta, NY, 14586, USA Methods: NMR, Smith degradation
The publication contains the following compound(s):
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