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1. Compound ID: 4316
|
a-L-Fucp-(1-2)-+
|
-2)-a-D-Galp-(1-3)-b-D-Galp-(1-3)-a-D-GalpNAc-(1-3)-a-D-GalpNAc-(1- |
Show graphically |
Structure type: suggested polymer biological repeating unit
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_115013,IEDB_130645,IEDB_130648,IEDB_134627,IEDB_136044,IEDB_136045,IEDB_136906,IEDB_137472,IEDB_137473,IEDB_1391961,IEDB_1391963,IEDB_140125,IEDB_141582,IEDB_141584,IEDB_141794,IEDB_142489,IEDB_143260,IEDB_144562,IEDB_149558,IEDB_150766,IEDB_150948,IEDB_150952,IEDB_151528,IEDB_152212,IEDB_152214,IEDB_153553,IEDB_174333,IEDB_190606,IEDB_241096,IEDB_461710,IEDB_461718,IEDB_461719,IEDB_549285,IEDB_885822,IEDB_918314,SB_148,SB_154,SB_165,SB_166,SB_187,SB_195,SB_23,SB_24,SB_7,SB_8,SB_86,SB_87,SB_88
The structure is contained in the following publication(s):
- Article ID: 1617
Guo H, Yi W, Shao J, Lu Y, Zhang W, Song J, Wang PG "Molecular Analysis of the O-Antigen Gene Cluster of Escherichia coli O86:B7 and Characterization of the Chain Length Determinant Gene (wzz)" -
Applied and Environmental Microbiology 71(12) (2005) 7995-8001
Escherichia coli O86:B7 has long been used as a model bacterial strain to study the generation of natural blood group antibody in humans, and it has been shown to possess high human blood B activity. The O-antigen structure of O86:B7 was solved recently in our laboratory. Comparison with the published structure of O86:H2 showed that both O86 subtypes shared the same O unit, yet each of the O antigens is polymerized from a different terminal sugar in a different glycosidic linkage. To determine the genetic basis for the O-antigen differences between the two O86 strains, we report the complete sequence of O86:B7 O-antigen gene cluster between galF and hisI, each gene was identified based on homology to other genes in the GenBank databases. Comparison of the two O86 O-antigen gene clusters revealed that the encoding regions between galF and gnd are identical, including wzy genes. However, deletion of the two wzy genes revealed that wzy in O86:B7 is responsible for the polymerization of the O antigen, while the deletion of wzy in O86:H2 has no effect on O-antigen biosynthesis. Therefore, we proposed that there must be another functional wzy gene outside the O86:H2 O-antigen gene cluster. Wzz proteins determine the degree of polymerization of the O antigen. When separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the lipopolysaccharide (LPS) of O86:B7 exhibited a modal distribution of LPS bands with relatively short O units attached to lipid A-core, which differs from the LPS pattern of O86:H2. We proved that the wzz genes are responsible for the different LPS patterns found in the two O86 subtypes, and we also showed that the very short type of LPS is responsible for the serum sensitivity of the O86:B7 strain
Lipopolysaccharide, O-antigen, Escherichia coli, gene cluster, Wzz
NCBI PubMed ID: 16332778Publication DOI: 10.1128/AEM.71.12.7995-8001.2005Journal NLM ID: 7605801Publisher: American Society for Microbiology
Correspondence: wang.892@osu.edu
Institutions: Department of Biochemistry and Chemistry, The Ohio State University, Columbus, OH 43210
Methods: genetic methods
- Article ID: 3199
Yi W, Bystricky P, Yao Q, Guo H, Zhu L, Li H, Shen J, Li M, Ganguly S, Bush CA, Wang PG "Two different O-polysaccharides from Escherichia coli O86 are produced by different polymerization of the same O-repeating unit." -
Carbohydrate Research 341 (2006) 100-108
The structure of a new O-polysaccharide from Escherichia coli O86:K62:B7 was determined using NMR and methylation analysis. The structure is as follows: [carbohydrate: see text]. Comparison with the previously published structure from E. coli O86:K2:H2 revealed that the O-polysaccharides from these two E. coli O86 serotypes share the same branched pentasaccharide repeating unit. However, they differ in the anomeric configuration of the linkage, the linkage position, and the identity of the residue through which polymerization occurs. The immunochemical activity of these two forms of LPS toward anti-B antibody was studied and compared. The results showed that LPS from E. coli O86:K2:H2 strain possesses higher blood group B reactivity. The immunoreactivity difference was explained by modeling of the O-repeating unit tetrasaccharide fragments. This finding provides a good system for the further study of O-polysaccharide biosynthesis especially the repeating unit polymerization mechanism.
Lipopolysaccharide, O-polysaccharide, molecular modeling, blood group antigens, polymerization, O-Repeating unit, Blood group antigens; Lipopolysaccharide; Molecular modeling; O-Polysaccharide; O-Repeating unit; Polymerization
NCBI PubMed ID: 16313893Publication DOI: 10.1016/j.carres.2005.11.001Journal NLM ID: 0043535Publisher: Elsevier
Correspondence: Peng G. Wang
Institutions: Department of Biochemistry, The Ohio State University, Columbus, OH 43210, USA, Department of Chemistry, University of Maryland, Baltimore County, MD 21250, USA
Methods: methylation, GC-MS, NMR, ELISA, composition analysis
- Article ID: 3400
Guo H, Yi W, Li L, Wang PG "Three UDP-hexose 4-epimerases with overlapping substrate specificity coexist in E. coli O86:B7" -
Biochemical and Biophysical Research Communications 356(3) (2007) 604-609
The O-antigen gene cluster of Escherichia coli O86:B7 was sequenced previously in our lab. One UDP-hexose 4-epimerase gene (named gne2 in this paper) was found and later characterized to be able to catalyze the interconversion between UDP-GlcNAc/GalNAc and UDP-Glc/Gal with almost equal efficiency. However, sequencing of the flanking gene region upstream of the traditional O-antigen gene cluster revealed an open reading frame (gne1), sharing 100% identity with Gne from E. coli O55, previously identified as UDP-GlcNAc 4-epimerase. Furthermore, we also located the traditional galE gene in the gal operon of O86:B7, which can catalyze the interconversion of UDP-Glc to UDP-Gal. Thus, for the first time, three UDP-hexose 4-epimerases with overlapping substrate specificity were found to coexist in one bacterium. Deletion of gne1 and gne2 in O86:B7 produced two different LPS phenotypes: the gne1 mutant exhibited rough LPS, while the gne2 mutant showed semi-rough LPS phenotype. These findings provide new clues for understanding the mechanism of O-antigen biosynthesis
O-antigen, rough LPS, UDP-hexose 4-epimerase, Semi-rough LPS
NCBI PubMed ID: 17368567Journal NLM ID: 0372516Publisher: Academic Press
Correspondence: wang.892@osu.edu
Institutions: Department of Biochemistry, The Ohio State University, Columbus, OH 43210, USA
Methods: GLC-MS, GLC, serological methods, genetic methods, CE-ESI-MS
- Article ID: 3504
Li M, Shen J, Liu X, Shao J, Yi W, Chow CS, Wang PG "Identification of a New α1,2-Fucosyltransferase Involved in O-Antigen Biosynthesis of Escherichia coli O86:B7 and Formation of H-Type 3 Blood Group Antigen" -
Biochemistry 47 (2008) 11590-11597
Escherichia coli O86 possesses high human blood group B activity because of its O-antigen structure, sharing the human blood group B epitope. In this study, the wbwK gene of E. coli O86:B7 was expressed and purified as the GST fusion protein. Thereafter, the wbwK gene was biochemically identified to encode an α1,2-fucosyltransferase through radioactivity assays, as well as mass spectrometry and NMR spectroscopy. WbwK shows strict substrate specificity and only recognizes Galβ1,3GalNAcα-OR (T-antigen and derivatives) as the acceptor to generate the H-type 3 blood group antigen. In contrast to other α1,2-fucosyltransferases, WbwK does not display activity toward the simple substrate Galβ-OMe. Comparison with another recently characterized α1,2-fucosyltransferase (WbsJ) of E. coli O128:B12 indicates a low level of amino acid identity between them; however, they share a common acceptor substrate, Galβ1,3GalNAcα-OR. Domain swapping between WbwK and WbsJ revealed that the smaller variable domains located in the C-terminus determine substrate specificity, whereas the larger variable domain in the N-terminus might play a role in forming the correct conformation for substrate binding or for localization of the α1,2-fucosyltransferase involved in O-antigen biosynthesis. In addition, milligram scale biosynthesis of the H-type 3 blood group antigen was explored using purified recombinant WbwK. WbwK may have potential applications in masking T-antigen, the tumor antigen, in vivo
biosynthesis, gene, O-antigen, Escherichia coli, epitope, Substrate Specificity, T-Antigen, human blood group B
NCBI PubMed ID: 18842005Publication DOI: 10.1021/bi801067sJournal NLM ID: 0370623Publisher: American Chemical Society
Correspondence: csc@chem.wayne.edu; wang.892@osu.edu
Institutions: Department of Chemistry, Wayne State UniVersity, Detroit, Michigan 48202, and Department of Biochemistry, The Ohio State UniVersity, Columbus, Ohio 43210
Methods: 13C NMR, 1H NMR, ESI-MS, NMR-1D, serological methods, genetic methods, biochemical methods
- Article ID: 4690
Knirel YA, Gabius H, Blixt O, Rapoport EM, Khasbiullina NR, Shilova NV, Bovin NV "Human tandem-repeat-type galectins bind bacterial non-bGal polysaccharides" -
Glycoconjugate Journal 31(1) (2014) 7-12
Galectins are multifunctional effectors, for example acting as regulators of cell growth via protein-glycan interactions. The observation of capacity to kill bacteria for two tandem-repeat-type galectins, which target histo-blood epitopes toward this end (Stowell et al. Nat. Med. 16:295-301, 2010), prompted us to establish an array with bacterial polysaccharides. We addressed the question whether sugar determinants other than ?-galactosides may be docking sites, using human galectins-4, -8, and -9. Positive controls with histo-blood group ABH-epitopes and the E. coli 086 polysaccharide ascertained the suitability of the set-up. Significant signal generation, depending on type of galectin and polysacchride, was obtained. Presence of cognate ?-galactoside-related epitopes within a polysaccharide chain or its branch will not automatically establish binding properties, and structural constellations lacking galactosides, like rhamnan, were found to be active. These data establish the array as valuable screening tool, giving direction to further functional and structural studies.
glycan, Bacterial polysaccharide, ABO, galectin, printed glycan array, rhamnoside
NCBI PubMed ID: 24065176Publication DOI: 10.1007/s10719-013-9497-3Journal NLM ID: 8603310WWW link: doi:10.1007/s10719-013-9497-3Publisher: Kluwer Academic Publishers
Correspondence: bovin@carb.ibch.ru
Institutions: N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Leninsky prosp., 47, Moscow, Russian Federation, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya 16/10
Methods: GPC, mild acid degradation, binding assays
- Article ID: 4926
Bhaumik I, Kar RK, Bhunia A, Misra AK "Expedient synthesis of the pentasaccharide repeating unit of the O-antigen of Escherichia coli O86 and its conformational analysis" -
Glycoconjugate Journal 33 (2016) 887-896
Synthesis of the pentasaccharide with a 2-aminoethyl linker attached to the reducing end corresponding to the cell wall O-antigen of Escherichia coli O86 strain is reported. The synthetic strategy involves sequential glycosylation of suitably protected monosaccharide intermediates under similar glycosylation reaction conditions. Thioglycosides have been used as glycosyl donor throughout the synthetic strategy. Conformational analysis of the synthesized pentasaccharide has been carried out using 2D ROESY NMR spectral analysis and all atom explicit molecular dynamics (MD) simulation technique. Graphical abstract Facile synthesis of the pentasaccharide with a 2-aminoethyl linker attached to the reducing end corresponding to the cell wall O-antigen of Escherichia coli O86 strain is reported. Conformational analysis of the synthesized pentasaccharide has been carried out using 2D ROESY NMR spectral analysis and all atom explicit molecular dynamics (MD) simulation technique.
lipopolysaccharides, Escherichia coli, antigens, Glycosylations, Molecular dynamics (MD) simulation
NCBI PubMed ID: 27263095Publication DOI: 10.1007/s10719-016-9687-xJournal NLM ID: 8603310Publisher: Kluwer Academic Publishers
Correspondence: akmisra69@gmail.com
Institutions: Department of Biophysics, Bose Institute, P-1/12, C.I.T. Scheme VII M, Kolkata, 700054, India, Division of Molecular Medicine, Bose Institute, P-1/12, C. I. T. Scheme VII M, Kolkata, 700054, India
Methods: 13C NMR, 1H NMR, NMR-2D, IR, TLC, conformation analysis, MALDI-MS, chemical synthesis, chemical methods, MD simulations, CD, glycosylations
- Article ID: 4957
Shang W, Zhai Y, Ma Z, Yang G, Ding Y, Han D, Li J, Zhang H, Liu J, Wang PG, Liu XW, Chen M "Production of human blood group B antigen epitope conjugated protein in Escherichia coli and utilization of the adsorption blood group B antibody" -
Microbial Cell Factories 15(1) (2016) 138
BACKGROUND: In the process of ABO-incompatible (ABOi) organ transplantation, removal of anti-A and/or B antibodies from blood plasma is a promising method to overcome hyperacute rejection and allograft loss caused by the immune response between anti-A and/or B antibodies and the A and/or B antigens in the recipient. Although there are commercial columns to do this work, the application is still limited because of the high production cost. RESULTS: In this study, the PglB glycosylation pathway from Campylobacter jejuni was exploited to produce glycoprotein conjugated with Escherichia coli O86:B7 O-antigen, which bears the blood group B antigen epitope to absorb blood group B antibody in blood. The titers of blood group B antibody were reduced to a safe level without changing the clotting function of plasma after glycoprotein absorption of B antibodies in the plasma. CONCLUSIONS: We developed a feasible strategy for the specific adsorption/removal of blood group antibodies. This method will be useful in ABOi organ transplantation and universal blood transfusion.
PglB, blood group B antigen, Conjugated glycoprotein, E.coli O-antigen, Immunoadsorption
Publication DOI: 10.1186/s12934-016-0538-zJournal NLM ID: 101139812Publisher: London: BioMed Central
Correspondence: chenmin@sdu.edu.cn; xianweiliu@sdu.edu.cn
Institutions: The Institute of Medical Molecular Genetics, Department of Biochemistry and Molecular Biology, Bin Zhou Medical University, No. 346, Guan Hai Road, Lai Shan District, Yan Tai City, Shan Dong Province, 264003, People's Republic of China, The State Key Laboratory of Microbial Technology, National Glycoengineering Research Center, School of Life Sciences and Shandong Provincial Key Laboratory of Carbohydrate Chemistry and Glycobiology, Shandong University, Jinan, Shandong, 250100, People's Republic of China
Methods: SDS-PAGE, ELISA, Western blotting, MALDI-TOF MS, serological methods, genetic methods, statistical analysis, binding assays, conjugation
- Article ID: 5472
Liu B, Furevi A, Perepelov AV, Guo X, Cao H, Wang Q, Reeves PR, Knirel YA, Wang L, Widmalm G "Structure and genetics of Escherichia coli O antigens" -
FEMS Microbiology Reviews 44(6) (2020) 655-683
Escherichia coli includes clonal groups of both commensal and pathogenic strains, with some of the latter causing serious infectious diseases. O antigen variation is current standard in defining strains for taxonomy and epidemiology, providing the basis for many serotyping schemes for Gram-negative bacteria. This review covers the diversity in E. coli O antigen structures and gene clusters, and the genetic basis for the structural diversity. Of the 187 formally defined O antigens, six (O31, O47, O67, O72, O94 and O122) have since been removed and four (O14, O34, O89 and O144) strains do not produce any O antigen. Therefore, structures are presented for 176 of the 181 E. coli O antigens, some of which include subgroups. Most (93%) of these O antigens are synthesized via the Wzx/Wzy pathway, 11 via the ABC transporter pathway, with O20, O57 and O60 still uncharacterized due to failure to find their O antigen gene clusters. Biosynthetic pathways are given for 38 of the 49 sugars found in E. coli O antigens, and several pairs or groups of the E. coli antigens that have related structures show close relationships of the O antigen gene clusters within clades, thereby highlighting the genetic basis of the evolution of diversity.
structure, O antigen, Escherichia coli, gene cluster, serogroup, diversity
NCBI PubMed ID: 31778182Publication DOI: 10.1093/femsre/fuz028Journal NLM ID: 8902526Publisher: Oxford University Press
Correspondence: G. Widmalm
; Lei Wang
Institutions: Department of Organic Chemistry, Arrhenius Laboratory, Stockholm University, Stockholm, Sweden, N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, Tianjin Key Laboratory of Microbial Functional Genomics, Tianjin, China, The Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, Tianjin, China, School of Molecular and Microbial Bioscience (G08), University of Sydney, Sydney, Australia, TEDA Institute of Biological Sciences and Biotechnology, Nankai University, TEDA, Tianjin, China, Department of Immunology, School of Basic Medical Sciences, Tianjin Medical University, Tianjin, China
- Article ID: 5760
Dobrochaeva K, Khasbiulina N, Shilova N, Antipova N, Obukhova P, Galanina O, Blixt O, Kunz H, Filatov A, Knirel Y, Le Pendu J, Khaidukov S, Bovin N "Specificity of human natural antibodies referred to as anti-Tn" -
Molecular Immunology 120 (2020) 74-82
To understand the role of human natural IgM known as antibodies against the carbohydrate epitope Tn, the antibodies were isolated using GalNAcα-Sepharose affinity chromatography, and their specificity was profiled using microarrays (a glycan array printed with oligosaccharides and bacterial polysaccharides, as well as a glycopeptide array), flow cytometry, and inhibition ELISA. The antibodies bound a restricted number of GalNAcα-terminated oligosaccharides better than the parent monosaccharide, e.g., 6-O-Su-GalNAcα and GalNAcα1-3Galβ1-3(4)GlcNAcβ. The binding with several bacterial polysaccharides that have no structural resemblance to the affinity ligand GalNAcα was quite unexpected. Given that GalNAcα is considered the key fragment of the Tn antigen, it is surprising that these antibodies bind weakly GalNAcα-OSer and do not bind a wide variety of GalNAcα-OSer/Thr-containing mucin glycopeptides. At the same time, we have observed specific binding to cells having Tn-positive glycoproteins containing similar glycopeptide motifs in a conformationally rigid macromolecule. Thus, specific recognition of the Tn antigen apparently requires that the naturally occurring "anti-Tn" IgM recognize a complex epitope comprising the GalNAcα as an essential component and a fairly long amino acid sequence where the amino acids adjacent to GalNAcα do not contact the antibody paratope; i.e., the antibodies recognize a spatial epitope or a molecular pattern rather than a classical continuous sequence. In addition, we have not found any increase in the binding of natural antibodies when GalNAcα residues were clustered. These results may help in further development of anticancer vaccines based on synthetic Tn constructs.
cancer, glycans, natural antibodies, anti-glycan antibodies, Tn antigen
NCBI PubMed ID: 32087569Publication DOI: 10.1016/j.molimm.2020.02.005Journal NLM ID: 7905289Publisher: Elsevier
Correspondence: professorbovin@yandex.ru
Institutions: Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 16/10 Miklukho-Maklaya, Moscow, Russian Federation, Semiotik LLC, 16/10 Miklukho-Maklaya, Moscow, Russian Federation, National Medical Research Center for Obstetrics, Gynecology and Perinatology Named after Academician V.I. Kulakov of the Ministry of Healthcare of Russian Federation, Moscow, Russian Federation, National Research University Higher School of Economics, Moscow, Russian Federation, Department of Chemistry, Chemical Biology, University of Copenhagen, Thorvaldsensvej 40, 1871 Frederiksberg C, Denmark, Institut Fur Organische Chemie, Johannes Gutenberg-Universitat Mainz, Duesbergweg 10-14, D-55128, Mainz, Germany, Institute of Immunology, Federal Medical-Biological Agency of Russia, Moscow, Russian Federation, University of Nantes, Inserm, U892 IRT UN, 8 Quai MonCousu, BP70721 Nantes, FR 44007, France
Methods: ELISA, affinity chromatography, flow cytometry analysis, printed glycan array (PGA) analysis, FACS assay
- Article ID: 6153
Tuzikov AB, Rapoport EM, Khaidukov SV, Nokel EA, Knirel YA, Bovin NV "Synthesis of bodipy-labeled bacterial polysaccharides and their interaction with human dendritic cells" -
Glycoconjugate Journal 38 (2021) 369-374
In this report, we describe the fluorescent labeling of bacterial polysaccharides (Escherichia coli O86:B7, Escherichia coli O19ab, Pseudomonas aeruginosa O10a10b, and Shigella flexneri 2b) at the 'natural' amino group of their phosphoethanolamine moiety. Two protocols for labeling are compared: 1) on a scale of a few mg of the polysaccharide, with a dialysis procedure for purification from excessive reagents; and 2) on a scale of 0.1 mg of the polysaccharide, with a simple precipitation procedure instead of dialysis. The microscale version is sufficient for comfortable cytofluorometric analysis. The resulting probes were found to specifically bind to human dendritic cells in a dose-dependent manner. The used limited set of polysaccharides did not allow us even to get close to understanding which dendritic cell-associated lectins and which cognate polysaccharide epitopes are involved in recognition, but the proposed microscale protocol allows to generate a library of fluorescent probes for further mapping of the polysaccharide specificity of the dendritic cells.
bacterial polysaccharides, dendritic cells, fluorescent labeling
NCBI PubMed ID: 33783715Publication DOI: 10.1007/s10719-021-09993-9Journal NLM ID: 8603310Publisher: Kluwer Academic Publishers
Correspondence: professorbovin@yandex.ru
Institutions: Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry RAS, 16/10 Miklukho-Maklaya str, Moscow, Russia, School of Engineering, Computer and Mathematical Sciences, Auckland University of Technology, Auckland, New Zealand
Methods: TLC, antibody binding, mild acid degradation, flow cytometry analysis, fluorescence labeling
- Article ID: 6201
Banahene N, Kavunja HW, Swarts BM "Chemical reporters for bacterial glycans: development and applications" -
Chemical Reviews 122(3) (2022) 3336-3413
Bacteria possess an extraordinary repertoire of cell envelope glycans that have critical physiological functions. Pathogenic bacteria have glycans that are essential for growth and virulence but are absent from humans, making them high-priority targets for antibiotic, vaccine, and diagnostic development. The advent of metabolic labeling with bioorthogonal chemical reporters and small-molecule fluorescent reporters has enabled the investigation and targeting of specific bacterial glycans in their native environments. These tools have opened the door to imaging glycan dynamics, assaying and inhibiting glycan biosynthesis, profiling glycoproteins and glycan-binding proteins, and targeting pathogens with diagnostic and therapeutic payload. These capabilities have been wielded in diverse commensal and pathogenic Gram-positive, Gram-negative, and mycobacterial species-including within live host organisms. Here, we review the development and applications of chemical reporters for bacterial glycans, including peptidoglycan, lipopolysaccharide, glycoproteins, teichoic acids, and capsular polysaccharides, as well as mycobacterial glycans, including trehalose glycolipids and arabinan-containing glycoconjugates. We cover in detail how bacteria-targeting chemical reporters are designed, synthesized, and evaluated, how they operate from a mechanistic standpoint, and how this information informs their judicious and innovative application. We also provide a perspective on the current state and future directions of the field, underscoring the need for interdisciplinary teams to create novel tools and extend existing tools to support fundamental and translational research on bacterial glycans.
biosynthesis, polysaccharides, glycoconjugates, glycan, Gram-negative bacteria, gram-positive bacteria
NCBI PubMed ID: 34905344Publication DOI: 10.1021/acs.chemrev.1c00729Journal NLM ID: 2985134RPublisher: Chem Rev
Correspondence: ben.swarts@cmich.edu
Institutions: Department of Chemistry and Biochemistry, Central Michigan University, Mount Pleasant, Michigan 48859, United States, Biochemistry, Cell, and Molecular Biology Program, Central Michigan University, Mount Pleasant, Michigan 48859, United States
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2. Compound ID: 14502
|
a-L-Fucp-(1-2)-+
|
-2)-a-D-Galp-(1-3)-b-D-Galp-(1-3)-a-D-GalpNAc-(1-3)-a-D-GalpNAc-(1- |
Show graphically |
Structure type: suggested polymer biological repeating unit
Aglycon: core-lipid A
Trivial name: O-unit
Compound class: O-polysaccharide, LPS
Contained glycoepitopes: IEDB_115013,IEDB_130645,IEDB_130648,IEDB_134627,IEDB_136044,IEDB_136045,IEDB_136906,IEDB_137472,IEDB_137473,IEDB_1391961,IEDB_1391963,IEDB_140125,IEDB_141582,IEDB_141584,IEDB_141794,IEDB_142489,IEDB_143260,IEDB_144562,IEDB_149558,IEDB_150766,IEDB_150948,IEDB_150952,IEDB_151528,IEDB_152212,IEDB_152214,IEDB_153553,IEDB_174333,IEDB_190606,IEDB_241096,IEDB_461710,IEDB_461718,IEDB_461719,IEDB_549285,IEDB_885822,IEDB_918314,SB_148,SB_154,SB_165,SB_166,SB_187,SB_195,SB_23,SB_24,SB_7,SB_8,SB_86,SB_87,SB_88
The structure is contained in the following publication(s):
- Article ID: 5760
Dobrochaeva K, Khasbiulina N, Shilova N, Antipova N, Obukhova P, Galanina O, Blixt O, Kunz H, Filatov A, Knirel Y, Le Pendu J, Khaidukov S, Bovin N "Specificity of human natural antibodies referred to as anti-Tn" -
Molecular Immunology 120 (2020) 74-82
To understand the role of human natural IgM known as antibodies against the carbohydrate epitope Tn, the antibodies were isolated using GalNAcα-Sepharose affinity chromatography, and their specificity was profiled using microarrays (a glycan array printed with oligosaccharides and bacterial polysaccharides, as well as a glycopeptide array), flow cytometry, and inhibition ELISA. The antibodies bound a restricted number of GalNAcα-terminated oligosaccharides better than the parent monosaccharide, e.g., 6-O-Su-GalNAcα and GalNAcα1-3Galβ1-3(4)GlcNAcβ. The binding with several bacterial polysaccharides that have no structural resemblance to the affinity ligand GalNAcα was quite unexpected. Given that GalNAcα is considered the key fragment of the Tn antigen, it is surprising that these antibodies bind weakly GalNAcα-OSer and do not bind a wide variety of GalNAcα-OSer/Thr-containing mucin glycopeptides. At the same time, we have observed specific binding to cells having Tn-positive glycoproteins containing similar glycopeptide motifs in a conformationally rigid macromolecule. Thus, specific recognition of the Tn antigen apparently requires that the naturally occurring "anti-Tn" IgM recognize a complex epitope comprising the GalNAcα as an essential component and a fairly long amino acid sequence where the amino acids adjacent to GalNAcα do not contact the antibody paratope; i.e., the antibodies recognize a spatial epitope or a molecular pattern rather than a classical continuous sequence. In addition, we have not found any increase in the binding of natural antibodies when GalNAcα residues were clustered. These results may help in further development of anticancer vaccines based on synthetic Tn constructs.
cancer, glycans, natural antibodies, anti-glycan antibodies, Tn antigen
NCBI PubMed ID: 32087569Publication DOI: 10.1016/j.molimm.2020.02.005Journal NLM ID: 7905289Publisher: Elsevier
Correspondence: professorbovin@yandex.ru
Institutions: Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 16/10 Miklukho-Maklaya, Moscow, Russian Federation, Semiotik LLC, 16/10 Miklukho-Maklaya, Moscow, Russian Federation, National Medical Research Center for Obstetrics, Gynecology and Perinatology Named after Academician V.I. Kulakov of the Ministry of Healthcare of Russian Federation, Moscow, Russian Federation, National Research University Higher School of Economics, Moscow, Russian Federation, Department of Chemistry, Chemical Biology, University of Copenhagen, Thorvaldsensvej 40, 1871 Frederiksberg C, Denmark, Institut Fur Organische Chemie, Johannes Gutenberg-Universitat Mainz, Duesbergweg 10-14, D-55128, Mainz, Germany, Institute of Immunology, Federal Medical-Biological Agency of Russia, Moscow, Russian Federation, University of Nantes, Inserm, U892 IRT UN, 8 Quai MonCousu, BP70721 Nantes, FR 44007, France
Methods: ELISA, affinity chromatography, flow cytometry analysis, printed glycan array (PGA) analysis, FACS assay
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