InChI=1S/C8H15NO6/c1- 3(11) 9- 5- 7(13) 6(12) 4(2- 10) 15- 8(5) 14/h4- 8,10,12- 14H,2H2,1H3,(H,9,11) /t4- ,5- ,6+,7- ,8- /m1/s1 |
OVRNDRQMDRJTHS-JAJWTYFOSA-N |
CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[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.
Escherichia coli metabolite
Any bacterial metabolite produced during a metabolic reaction in Escherichia coli.
(via N-acetyl-D-galactosamine )
human metabolite
Any mammalian metabolite produced during a metabolic reaction in humans (Homo sapiens).
(via N-acetyl-D-galactosamine )
mouse metabolite
Any mammalian metabolite produced during a metabolic reaction in a mouse (Mus musculus).
(via N-acetyl-D-galactosamine )
(via N-acetylgalactosamine )
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View more via ChEBI Ontology
2-acetamido-2-deoxy-β-D-galactopyranose
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2-(acetylamino)-2-deoxy-β-D-galactopyranose
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ChEBI
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2-acetamido-2-deoxy-β-D-galactopyranoside
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ChEBI
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β-D-galactopyranose, 2-(acetylamino)-2-deoxy-
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ChEBI
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β-GalNAc
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ChEBI
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bGalNAc
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ChEBI
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N-acetyl-beta-D-galactosamine
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ChEBI
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N-Acetyl-beta-D-galactosamine
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KEGG COMPOUND
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N-acetyl-β-D-galactosamine
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UniProt
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WURCS=2.0/1,1,0/[a2112h-1b_1-5_2*NCC/3=O]/1/
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GlyTouCan
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1728373
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Reaxys Registry Number
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Reaxys
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1811-31-0
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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. | von Gunten S, Smith DF, Cummings RD, Riedel S, Miescher S, Schaub A, Hamilton RG, Bochner BS (2009) Intravenous immunoglobulin contains a broad repertoire of anticarbohydrate antibodies that is not restricted to the IgG2 subclass. The Journal of allergy and clinical immunology 123, 1268-76.e15 [PubMed:19443021] [show Abstract]
BackgroundSpecificities for carbohydrate IgG antibodies, thought to be predominantly of the IgG2 subclass, have never been broadly examined in healthy human subjects.ObjectiveTo examine commercial intravenous immunoglobulin (IVIG) preparations for their ability to recognize a wide range of glycans and to determine the contribution of IgG2 to the binding pattern observed.MethodsWe used a glycan microarray to evaluate IVIG preparations and a control mix of similar proportions of human myeloma IgG1 and IgG2 for binding to 377 glycans, courtesy of the Consortium for Functional Glycomics Core H. Glycans recognized were categorized using public databases for their likely cellular sources. IgG2 was depleted from IVIG by using immunoaffinity chromatography, and depletion was confirmed by using nephelometry and surface plasmon resonance.ResultsNearly half of the glycans bound IgG. Some of the glycans with the greatest antibody binding can be found in structures of human pathogenic bacteria (eg, Streptococcus pneumoniae, Mycobacterium tuberculosis, Vibrio cholera) and nonpathogenic bacteria, including LPS and lipoteichoic acid, capsular polysaccharides, and exopolysaccharides. Surprisingly, depletion of IgG2 had only a modest effect on anticarbohydrate recognition patterns compared with the starting IVIG preparation. Little to no binding activity was detected to human endogenous glycans, including tumor-associated antigens.ConclusionsThis novel, comprehensive analysis provides evidence that IVIG contains a much wider range than previously appreciated of anticarbohydrate IgG antibodies, including those recognizing both pathogenic and non-pathogen-associated prokaryotic glycans. |
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