Found 4 structures.
Displayed structures from 1 to 4
Expand all compounds
Collapse all compounds
Show all as text (SweetDB notation)
Show all graphically (SNFG notation)
1. Compound ID: 4341
|
{{{-a-D-Manp-(1-2)-}}}/n=0-2/-a-D-Manp-(1-5)-a-D-Araf-(1-2)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-+
|
{{{-a-D-Manp-(1-2)-}}}/n=0-2/-a-D-Manp-(1-5)-b-D-Araf-(1-2)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-{{{-a-D-Araf-(1-5)-}}}a-D-Araf-(1-3)-{{{-a-D-Araf-(1-5)-}}}+
|
{{{-a-D-Manp-(1-2)-}}}/n=0-2/-a-D-Manp-(1-5)-b-D-Araf-(1-2)-a-D-Araf-(1-5)-+ |
| |
{{{-a-D-Manp-(1-2)-}}}/n=0-2/-a-D-Manp-(1-5)-b-D-Araf-(1-2)-a-D-Araf-(1-3)-a-D-Araf-(1-5)-{{{-a-D-Araf-(1-5)-}}}a-D-Araf-(1-3)-{{{-a-D-Araf-(1-5)-}}}{{{-a-D-Araf-(1-5)-}}}D-Araf-(1--/mannan core ID 10733/ |
Show graphically |
Structure type: oligomer
Aglycon: mannan core ID 10733
Trivial name: arabinan
Contained glycoepitopes: IEDB_130701,IEDB_136104,IEDB_140116,IEDB_141795,IEDB_141830,IEDB_141834,IEDB_143632,IEDB_144983,IEDB_152206,IEDB_164480,IEDB_1855257,IEDB_76933,IEDB_983930,SB_136,SB_196,SB_44,SB_67,SB_72
The structure is contained in the following publication(s):
- Article ID: 1628
Li W, Chatterjee D, Lee RE "Rapid structural characterization of the arabinogalactan and lipoarabinomannan in live mycobacterial cells using 2D and 3D HR-MAS NMR: structural changes in the arabinan due to ethambutol treatment and gene mutation are observed" -
Glycobiology 15(2) (2005) 139-151
Mycobacteria possess a unique, highly evolved, carbohydrate- and lipid-rich cell wall that is believed to be important for their survival in hostile environments. Until now, our understanding of mycobacterial cell wall structure has been based upon destructive isolation and fragmentation of individual cell wall components. This study describes the observation of the major cell wall structures in live, intact mycobacteria using 2D and 3D high-resolution magic-angle spinning (HR-MAS) nuclear magnetic resonance (NMR). As little as 20 mg (wet weight) of [13C]-enriched cells were required to produce a whole-cell spectra in which discrete cross-peaks corresponding to specific cell wall components could be identified. The most abundant signals of the arabinogalactan (AG) and lipoarabinomannan (LAM) were assigned in the HR-MAS NMR spectra by comparing the 2D and 3D NMR whole-cell spectra with the spectra of purified cellular components. This study confirmed that the structures of the AG and LAM moieties in the cell wall of live mycobacteria are consistent with structural reports in the literature, which were obtained via degradative analysis. Most important, by using intact cells it was possible to directly demonstrate the effects of ethambutol on the mycobacterial cell wall polysaccharides, characterize the effects of embB gene knockout in the M. smegmatis ∆embB mutant, and observe differences in the cell wall structures of two mycobacterial species (M. bovis BCG and M. smegmatis.) Herein, we show that HR-MAS NMR is a powerful, rapid, nondestructive technique to monitor changes in the complex, carbohydrate-rich cell wall of live mycobacterial cells.
Mycobacteria, arabinogalactan, lipoarabinomannan, Mycobacterium smegmatis, HR-MAS NMR, HCCH-TOCSY, Mycobacterium bovis, mycolyl arabinogalactanstructure
NCBI PubMed ID: 15371346Publication DOI: 10.1093/glycob/cwh150Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Correspondence: relee@utmem.edu
Institutions: Department of Pharmaceutical Sciences, University of Tennessee Health Science Center, 847 Monroe Ave. Rm. 327, Memphis, TN 38163, USA
Methods: NMR
Expand this compound
Collapse this compound
2. Compound ID: 6673
|
a-D-Manp-(1-2)-a-D-Manp-(1-5)-a-D-Araf-(1-2)-a-D-Araf-(1-3)-+
|
?%a-D-Manp-(1-2)-?%a-D-Manp-(1-2)-a-D-Manp-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-3)-+
|
b-D-Araf-(1-2)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-3)-+ | a-D-Manp-(1-2)-+ a-D-Manp-(1-2)-+
| | | |
b-D-Araf-(1-2)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-{{{-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-}}}/n=5/-a-D-Araf-(1-5)-a-D-Araf-(1-?)-a-D-Manp-(1-6)-{{{-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-}}}/n=5/-a-D-Manp |
Show graphically |
Structure type: structural motif or average structure
Trivial name: arabinomannan
Contained glycoepitopes: IEDB_130701,IEDB_1309625,IEDB_136104,IEDB_140116,IEDB_141793,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_143632,IEDB_144983,IEDB_152206,IEDB_153220,IEDB_153762,IEDB_153763,IEDB_1855257,IEDB_76933,IEDB_857718,IEDB_857732,IEDB_857735,IEDB_983930,SB_136,SB_191,SB_196,SB_198,SB_44,SB_67,SB_72
The structure is contained in the following publication(s):
- Article ID: 2663
Venisse A, Berjeaud JM, Chaurand P, Gilleron M, Puzo G "Structural features of lipoarabinomannan from Mycobacterium bovis BCG. Determination of molecular mass by laser desorption mass spectrometry" -
Journal of Biological Chemistry 268 (1993) 12401-12411
It was recently shown that mycobacterial lipoarabinomannan (LAM) can be classified into two types (Chatterjee, D., Lowell, K., Rivoire B., McNeil M. R., and Brennan, P. J. (1992) J. Biol. Chem. 267, 6234-6239) according to the presence or absence of mannosyl residues (Manp) located at the nonreducing end of the oligoarabinosyl side chains. These two types of LAM were found in a pathogenic Mycobacterium tuberculosis strain and in an avirulent M. tuberculosis strain, respectively, suggesting that LAM with Manp characterizes virulent and "disease-inducing strains." We now report the structure of the LAM from Mycobacterium bovis Bacille Calmette-Guérin (BCG) strain Pasteur, largely used throughout the world as vaccine against tuberculosis. Using an up-to-date analytical approach, we found that the LAM of M. bovis BCG belongs to the class of LAMs capped with Manp. By means of two-dimensional homonuclear and heteronuclear scalar coupling NMR analysis and methylation data, the sugar spin system assignments were partially established, revealing that the LAM contained two types of terminal Manp and 2-O-linked Manp. From the following four-step process: (i) partial hydrolysis of deacylated LAM (dLAM), (ii) oligosaccharide derivatization with aminobenzoic ethyl ester, (iii) HPLC purification, (iv) FAB/MS-MS analysis; it was shown that the dimannosyl unit α-D-Manp-(1→2)-α-D-Manp is the major residue capping the termini of the arabinan of the LAM. In this report, LAM molecular mass determination was established using matrix-assisted UV-laser desorption/ionization mass spectrometry which reveals that the LAM molecular mass is around 17.4 kDa. The similarity of the LAM structures between M. bovis BCG and M. tuberculosis H37Rv is discussed in regard to their function in the immunopathology of mycobacterial infection.
NCBI PubMed ID: 8509380Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Institutions: Centre National de la Recherche Scientifique, Département Glycoconjugués et Biomembranes, Toulouse, France
Methods: 1H NMR, FAB-MS/MS, LD-MS
- Article ID: 3114
Venisse A, Fournié JJ, Puzo G "Mannosylated lipoarabinomannan interacts with phagocytes" -
European Journal of Biochemistry 231 (1995) 440-447
Infection by Mycobacterium tuberculosis first involves its adhesion to mononuclear host phagocytes. Various macrophage opsonic and non-opsonic receptors are known to mediate this adhesion, with some specificity of mannosyl receptors for the more virulent strains. Mannosylated lipoarabinomannan, a major component of cell walls from M. tuberculosis and Mycobacterium bovis BCG, is endowed with mannooligosaccharide units that could mediate its binding to these latter receptors. To explore its interaction with murine immune cells by flow cytometry, we report a new procedure to fluorescently tag the polysaccharide molecules. We covalently labeled mannosylated lipoarabinomannan from M. bovis BCG with biotin, allowing formation of stable complexes with streptavidin coupled to a fluorochrome. In this work, we demonstrated that this major carbohydrate antigen interacts selectively with murine phagocytes, i.e. granulocytes and macrophages. This binding was affected by temperature and was serum- and divalent-cation-dependent. It also appears to involve a metabolically recycling protein receptor on the phagocyte surface and mannosyl aggretopes on the mannosylated lipoarabinomannan molecule. Thus, the latter may provide a means for mycobacteria to bind to and invade their host phagocytes. This molecule could constitute one of the early factors of mycobacterial virulence.
NCBI PubMed ID: 7635156Publication DOI: 10.1111/j.1432-1033.1995.tb20717.xJournal NLM ID: 0107600Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
Institutions: Departement des Glycoconjugues et Biomembranes, Laboratoire de Pharmacologie et Toxicologie Fondamentales du CNRS, Toulouse, France
Expand this compound
Collapse this compound
3. Compound ID: 7322
|
a-D-Manp-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-3)-+
|
a-D-Araf-(1-2)-a-D-Araf-(1-5)-+ |
| |
a-D-Araf-(1-2)-a-D-Araf-(1-3)-a-D-Araf-(1-5)-a-D-Araf-(1-3)-+ |
| |
a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Araf-(1-5)-+ | |
| | |
a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Araf-(1-3)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-3)-+ | |
| | |
a-D-Araf-(1-2)-a-D-Araf-(1-5)-+ | | |
| | | |
a-D-Araf-(1-2)-a-D-Araf-(1-3)-a-D-Araf-(1-5)-a-D-Araf-(1-3)-+ | | |
| | | |
a-D-Araf-(1-2)-a-D-Araf-(1-5)-+ | | | |
| | | | |
a-D-Araf-(1-2)-a-D-Araf-(1-3)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-3)-+ | | | |
| | | | |
a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Araf-(1-5)-+ | | | | |
| | | | | |
a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Araf-(1-3)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-3)-+ | | | | |
| | | | | |
a-D-Manp-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-3)-+ | | | | | |
| | | | | | |
-5)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-a-D-Araf-(1- |
Show graphically |
Structure type: polymer chemical repeating unit
Trivial name: arabinomannan
Contained glycoepitopes: IEDB_130701,IEDB_136104,IEDB_143632,IEDB_144983,IEDB_152206,IEDB_1855257,IEDB_983930,SB_136,SB_196,SB_44,SB_67,SB_72
The structure is contained in the following publication(s):
- Article ID: 3318
Wittkowski M, Mittelstadt J, Brandau S, Reiling N, Lindner B, Torrelles J, Brennan PJ, Holst O "Capsular arabinomannans from Mycobacterium avium with morphotype specific structural differences but identical biological activity" -
Journal of Biological Chemistry 282(26) (2007) 19103-19112
The capsules of two colony-morphotypes of Mycobacterium avium strain 2151 were investigated, i.e. of the virulent smooth-transparent (SmT) and the non-virulent smooth-opaque (SmO) type. From both morphotypes we separated a non-acylated arabinomannan (AM) from an acylated polysaccharide fraction by affinity chromatography, of which the AMs were structurally characterised. The AMs from the virulent morphotype in contrast to that from the non-virulent form possessed a larger mannan chain and a shorter arabinan chain. Incubation of murine bone marrow derived macrophages and human dendritic cells showed that the acylated polysaccharide fractions were potent inducers of TNF , IL 12 and IL-10, compared to non-acylated AMs which only led to a marginal cytokine release. Further in vitro experiments showed that both, the acylated polysaccharide fractions as well as the non-acylated AMs were able to induce in vitro anti-tumor cytotoxicity of human peripheral blood mononuclear cells. Thus, morphotype specific structural differences in capsular AMs of M. avium do not correlate with biological activity, however, their acylation is a prerequisite for effective stimulation of murine macrophages and human dendritic cells
biological activity, Mycobacterium avium, cells, virulent, macrophages, capsules, arabinomannan
NCBI PubMed ID: 17459879Publication DOI: 10.1042/BJ20070017Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: oholst@fz-borstel.de
Institutions: Immunochemistry and Biochemical Microbiology, Research Center Borstel, Borstel D-23845
Methods: 13C NMR, 1H NMR, NMR-2D, methylation, SDS-PAGE, chemical analysis, ESI-FTICR-MS, NMR-1D, serological methods
Expand this compound
Collapse this compound
4. Compound ID: 14427
|
{{{-a-D-Araf-(1-5)-+ a-D-Manp-(1-2)-+
| |
{{{-a-D-Araf-(1-5)-}}}a-D-Araf-(1-3)-a-D-Araf-(1-5)-a-D-Araf-(1-5)-}}}a-D-Araf-(1-2)-{{{-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-}}}a-D-Manp |
Show graphically |
Structure type: oligomer
Trivial name: lipoarabinomannan
Compound class: glycolipid
Contained glycoepitopes: IEDB_130701,IEDB_136104,IEDB_140116,IEDB_141793,IEDB_141828,IEDB_141829,IEDB_141831,IEDB_143632,IEDB_144983,IEDB_152206,IEDB_153220,IEDB_153762,IEDB_153763,IEDB_1855257,IEDB_76933,IEDB_857735,IEDB_983930,SB_136,SB_191,SB_196,SB_198,SB_44,SB_67,SB_72
The structure is contained in the following publication(s):
- Article ID: 5740
Campanero-Rhodes MA, Palma AS, Menendez M, Solis D "Microarray Strategies for Exploring Bacterial Surface Glycans and Their Interactions With Glycan-Binding Proteins" -
Frontiers in Microbiology 10 (2020) 2909
Bacterial surfaces are decorated with distinct carbohydrate structures that may substantially differ among species and strains. These structures can be recognized by a variety of glycan-binding proteins, playing an important role in the bacteria cross-talk with the host and invading bacteriophages, and also in the formation of bacterial microcolonies and biofilms. In recent years, different microarray approaches for exploring bacterial surface glycans and their recognition by proteins have been developed. A main advantage of the microarray format is the inherent miniaturization of the method, which allows sensitive and high-throughput analyses with very small amounts of sample. Antibody and lectin microarrays have been used for examining bacterial glycosignatures, enabling bacteria identification and differentiation among strains. In addition, microarrays incorporating bacterial carbohydrate structures have served to evaluate their recognition by diverse host/phage/bacterial glycan-binding proteins, such as lectins, effectors of the immune system, or bacterial and phagic cell wall lysins, and to identify antigenic determinants for vaccine development. The list of samples printed in the arrays includes polysaccharides, lipopoly/lipooligosaccharides, (lipo)teichoic acids, and peptidoglycans, as well as sequence-defined oligosaccharide fragments. Moreover, microarrays of cell wall fragments and entire bacterial cells have been developed, which also allow to study bacterial glycosylation patterns. In this review, examples of the different microarray platforms and applications are presented with a view to give the current state-of-the-art and future prospects in this field.
antibodies, immune system, lectins, vaccine development, microarrays, bacterial glycans, bacterial interactions
NCBI PubMed ID: 32010066Publication DOI: 10.3389/fmicb.2019.02909Journal NLM ID: 101548977Publisher: Lausanne: Frontiers Research Foundation
Correspondence: Dolores Solis
Institutions: Instituto de Quimica Fisica Rocasolano, Consejo Superior de Investigaciones Cientificas, Madrid, Spain, Centro de Investigacion Biomedica en Red de Enfermedades Respiratorias, Instituto de Salud Carlos III, Madrid, Spain, UCIBIO, Department of Chemistry, Faculty of Science and Technology, NOVA University of Lisbon, Lisbon, Portuga
Expand this compound
Collapse this compound
Total list of structure IDs on all result pages of the current query:
Total list of corresponding CSDB IDs (record IDs):
Execution: 2 sec