InChI=1S/C6H12O6/c7-1-2-3(8)4(9)5(10)6(11)12-2/h2-11H,1H2/t2-,3-,4+,5+,6-/m1/s1 |
WQZGKKKJIJFFOK-RWOPYEJCSA-N |
OC[C@H]1O[C@@H](O)[C@@H](O)[C@@H](O)[C@@H]1O |
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epitope
The biological role played by a material entity when bound by a receptor of the adaptive immune system. Specific site on an antigen to which an antibody binds.
metabolite
Any intermediate or product resulting from metabolism. The term 'metabolite' subsumes the classes commonly known as primary and secondary metabolites.
(via D-mannopyranose )
Saccharomyces cerevisiae metabolite
Any fungal metabolite produced during a metabolic reaction in Baker's yeast (Saccharomyces cerevisiae ).
(via D-mannose )
fundamental metabolite
Any metabolite produced by all living cells.
(via mannose )
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View more via ChEBI Ontology
BETA-D-MANNOSE
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PDBeChem
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beta-D-Mannose
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KEGG COMPOUND
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β-D-mannose
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UniProt
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WURCS=2.0/1,1,0/[a1122h-1b_1-5]/1/
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GlyTouCan
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1680742
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Reaxys Registry Number
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Reaxys
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648640
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Gmelin Registry Number
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Gmelin
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7322-31-8
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CAS Registry Number
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ChemIDplus
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Jandus P, Boligan KF, Smith DF, de Graauw E, Grimbacher B, Jandus C, Abdelhafez MM, Despont A, Bovin N, Simon D, Rieben R, Simon HU, Cummings RD, von Gunten S (2019) The architecture of the IgG anti-carbohydrate repertoire in primary antibody deficiencies. Blood 134, 1941-1950 [PubMed:31537530] [show Abstract] Immune system failure in primary antibody deficiencies (PADs) has been linked to recurrent infections, autoimmunity, and cancer, yet clinical judgment is often based on the reactivity to a restricted panel of antigens. Previously, we demonstrated that the human repertoire of carbohydrate-specific immunoglobulin G (IgG) exhibits modular organization related to glycan epitope structure. The current study compares the glycan-specific IgG repertoires between different PAD entities. Distinct repertoire profiles with extensive qualitative glycan-recognition defects were observed, which are characterized by the common loss of Galα and GalNAc reactivity and disease-specific recognition of microbial antigens, self-antigens, and tumor-associated carbohydrate antigens. Antibody repertoire analysis may provide a useful tool to elucidate the degree and the clinical implications of immune system failure in individual patients. | Schneider C, Smith DF, Cummings RD, Boligan KF, Hamilton RG, Bochner BS, Miescher S, Simon HU, Pashov A, Vassilev T, von Gunten S (2015) The human IgG anti-carbohydrate repertoire exhibits a universal architecture and contains specificity for microbial attachment sites. Science translational medicine 7, 269ra1 [PubMed:25568069] [show Abstract] Despite the paradigm that carbohydrates are T cell-independent antigens, isotype-switched glycan-specific immunoglobulin G (IgG) antibodies and polysaccharide-specific T cells are found in humans. We used a systems-level approach combined with glycan array technology to decipher the repertoire of carbohydrate-specific IgG antibodies in intravenous and subcutaneous immunoglobulin preparations. A strikingly universal architecture of this repertoire with modular organization among different donor populations revealed an association between immunogenicity or tolerance and particular structural features of glycans. Antibodies were identified with specificity not only for microbial antigens but also for a broad spectrum of host glycans that serve as attachment sites for viral and bacterial pathogens and/or exotoxins. Tumor-associated carbohydrate antigens were differentially detected by IgG antibodies, whereas non-IgG2 reactivity was predominantly absent. Our study highlights the power of systems biology approaches to analyze immune responses and reveals potential glycan antigen determinants that are relevant to vaccine design, diagnostic assays, and antibody-based therapies. | Mulakala C, Nerinckx W, Reilly PJ (2007) The fate of beta-D-mannopyranose after its formation by endoplasmic reticulum alpha-(1-->2)-mannosidase I catalysis. Carbohydrate research 342, 163-169 [PubMed:17157281] [show Abstract] The automated docking program AutoDock was used to dock all 38 characteristic beta-D-mannopyranose ring conformers into the active site of the yeast endoplasmic reticulum alpha-(1-->2)-mannosidase I, a Family 47 glycoside hydrolase that converts Man9GlcNAc2 to Man8GlcNAc2. The subject of this work is to establish the conformational pathway that allows the cleaved glycon product to leave the enzyme active site and eventually reach the ground-state conformation. Twelve of the 38 conformers optimally dock in the active site where the inhibitors 1-deoxymannonojirimycin and kifunensine are found in enzyme crystal structures. A further 23 optimally dock in a second site on the side of the active-site well, while three dock outside the active-site cavity. It appears, through analysis of the internal energies of different ring conformations, of intermolecular energies between the ligands and enzyme, and of forces exerted on the ligands by the enzyme, that beta-D-mannopyranose follows the path 3E-->1C4-->1H2-->B2,5 before being expelled by the enzyme. The highly conserved second site that strongly binds beta-D-mannopyranose-4C1 may exist to prevent competitive inhibition by the product, and is worthy of further investigation. |
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