Found 9 structures.
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1. Compound ID: 809
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a-Neup5Ac-(2-3)-b-D-Galp-(1-3)-b-D-GlcpNAc-(1-3)-+
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-4)-b-D-Galp-(1-4)-b-D-Glcp-(1- |
Show graphically |
Structure type: polymer chemical repeating unit
Trivial name: PS-Ib
Compound class: O-antigen, CPS
Contained glycoepitopes: IEDB_117715,IEDB_135813,IEDB_136044,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_1391962,IEDB_1391966,IEDB_141589,IEDB_141794,IEDB_141807,IEDB_142076,IEDB_142078,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_143794,IEDB_146100,IEDB_146664,IEDB_149174,IEDB_150899,IEDB_150933,IEDB_151531,IEDB_157001,IEDB_190606,IEDB_241110,IEDB_983931,SB_116,SB_124,SB_127,SB_133,SB_137,SB_145,SB_156,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_174,SB_186,SB_187,SB_192,SB_195,SB_29,SB_39,SB_6,SB_68,SB_7,SB_84,SB_88
The structure is contained in the following publication(s):
- Article ID: 216
Watanabe M, Miyake K, Yanae K, Kataoka Y, Koizumi S, Endo T, Ozaki A, Iijima S "Molecular characterization of a novel b1,3-galactosyltransferase for capsular polysaccharide synthesis by Streptococcus agalactiae type Ib" -
Journal of Biochemistry 131(2) (2002) 183-191
A group B streptococcus, Streptococcus agalactiae type Ib, produces a high-molecular- weight polysaccharide consisting of the following pentasaccharide repeating unit: →4)-[α-D-NeupNAc-(2→3)-β-D-Galp-(1→3)-β-D-GlcpNAc-(1→3)]-β-D-Galp-(1→4)-β-D-Glcp-(1→. The type- specific capsular polysaccharide (CP) synthesis (cps) genes of this strain were cloned and analyzed. A cloned 10-kb DNA fragment contained cpsIbE to L and neu (neuraminic acid synthesis gene) B. Comparison of the gene products with those of S. agalactiae type Ia, which has a similar but distinct CP, showed that the translation products of cpsIa and cpsIb genes exhibited very high homology except for those of cpsJ and K. In the type Ia strain, cpsIaJ encodes β1,4- galactosyltransferase, which catalyzes the transfer of galactose as the fourth monosaccharide of the sugar repeating unit. In the type Ib CP, this galactose forms a β1,3-linkage to GlcNAc. The low homology between the type Ia and Ib CpsJs seems to reflect this difference. By enzymatic activity measurement, the cpsIbJ product was found to display β1,3-galactosyltransferase activity. Furthermore, hydrophobic cluster analysis clarified the similarities and differences of the structures in N-terminal regions, including the DXD motif, between the galactosyltransferases.
synthesis, transfer, structure, gene, DNA, strain, capsular, characterization, polysaccharide, Streptococcus, repeating unit, analysis, capsular polysaccharide, group, molecular, form, acid, type, high, group B Streptococcus, cluster, specific, neuraminic acid, activity, sugar, motif, region, translation, enzymatic, difference, fragment, pentasaccharide, galactose, comparison, biotechnology, cloned, Cluster Analysis, CPS, engineering, galactosyltransferase, Galactosyltransferases, homology, hydrophobic, Japan, measurement, monosaccharide, similarity, Streptococcus agalactiae
NCBI PubMed ID: 11820930Journal NLM ID: 0376600Publisher: Japanese Biochemical Society
Correspondence: miyake@proc.nubio.nagoya-u.ac.jp
Institutions: Department of Biotechnology, Graduate School of Engineering, Nagoya University, Furo-cho, Chikusa-ku, Nagoya 464-8603, Japan
Methods: genetic methods
- Article ID: 1337
Zou W, Jennings HJ "Chemical-enzymatic synthesis of a branched hexasaccharide fragment of type Ia group B Streptococcus capsular polysaccharide" -
Journal of Carbohydrate Chemistry 15 (1996) 925-937
A branched hexasaccharide fragment of type Ia group B streptococcal polysaccharide, aNeuAc(2-3)bDGalp(1-4)bDGlcpNAc(1-3)[bDGlcp(1-4)]bDGalp(1-4)bDGlcpOMe (13) has been synthesised by chemical-enzymatic procedures.
synthesis, branched, hexasaccharide, capsular, polysaccharide, Streptococcus, capsular polysaccharide, group, type, group B Streptococcus, chemical, enzymatic, fragment, enzymatic synthesis
Journal NLM ID: 8218151Publisher: Marcel Dekker
Institutions: Institute for Biological Sciences, National Research Council of Canada, Ottawa, Canada
- Article ID: 1500
Cieslewicz MJ, Chaffin D, Glusman G, Kasper D, Madan A, Rodrigues S, Fahey J, Wessels MR, Rubens CE "Structural and genetic diversity of group B streptococcus capsular polysaccharides" -
Infection and Immunity 73(5) (2005) 3096-3103
Group B Streptococcus (GBS) is an important pathogen of neonates, pregnant women, and immunocompromised individuals. GBS isolates associated with human infection produce one of nine antigenically distinct capsular polysaccharides which are thought to play a key role in virulence. A comparison of GBS polysaccharide structures of all nine known GBS serotypes together with the predicted amino acid sequences of the proteins that direct their synthesis suggests that the evolution of serotype-specific capsular polysaccharides has proceeded through en bloc replacement of individual glycosyltransferase genes with DNA sequences that encode enzymes with new linkage specificities. We found striking heterogeneity in amino acid sequences of synthetic enzymes with very similar functions, an observation that supports horizontal gene transfer rather than stepwise mutagenesis as a mechanism for capsule variation. Eight of the nine serotypes appear to be closely related both structurally and genetically, whereas serotype VIII is more distantly related. This similarity in polysaccharide structure strongly suggests that the evolutionary pressure toward antigenic variation exerted by acquired immunity is counterbalanced by a survival advantage conferred by conserved structural motifs of the GBS polysaccharides
Bacterial Proteins, Streptococcus agalactiae, Bacterial Capsules, Genetic Variation
NCBI PubMed ID: 15845517Journal NLM ID: 0246127Publisher: American Society for Microbiology
Correspondence: craig.rubens@seattlechildrens.org
Institutions: Division of Infectious Diseases, Children's Hospital, University of Washington, Seattle, WA 98109, USA, Channing Division of Infectious Diseases, Children's Hospital Boston, Department of Microbiology and Molecular Genetics, Harvard Medical School Boston, Massachusetts, Institute for Systems Biology and Division of Infectious Diseases, Children's Hospital, University of Washington, 3 Seattle, Washington
Methods: genetic methods, biosynthetic methods
- Article ID: 1751
Jennings HJ, Katzenellenbogen E, Lugowski C, Kasper DL "Structure of native polysaccharide antigens of type Ia and type Ib group B Streptococcus" -
Biochemistry 22 (1983) 1258-1264
NCBI PubMed ID: 6838851Publication DOI: 10.1021/bi00274a042Journal NLM ID: 0370623Publisher: American Chemical Society
Institutions: Division of Biological Sciences, National Research Council of Canada, Ottawa, Ontario, Canada K1A OR6
Methods: 13C NMR, GC-MS
- Article ID: 2712
Schifferle RE, Jennings HJ, Wessels MR, Katzenellenbogen E, Roy R, Kasper DL "Immunochemical analysis of the types Ia and Ib group B streptococcal polysaccharides" -
Journal of Immunology 135 (1985) 4164-4170
The types Ia and Ib group B streptococcal type-specific polysaccharides have remarkable immunologic differences despite a great deal of structural similarity. Although these two complex polysaccharides differ only by a single glycosidic linkage, they are antigenically distinct. Furthermore, terminal sialic acid residues appear to be critical to the immunodeterminant on the type Ia polysaccharide, whereas the antigenicity of the type Ib polysaccharide does not show this dependence on sialic acid. In the current investigation we defined better the immunodeterminant of these polysaccharides. With homologous rabbit antiserum, the type Ia native and core polysaccharides demonstrated partial serologic identity, whereas the type Ib native and core polysaccharides demonstrated complete serologic identity. Surprisingly, the type I degalactosylated polysaccharide, degraded structure, was capable of reacting with a population of antibodies present in type Ia antiserum similar to the complete type Ia native polysaccharide, although demonstrating a reduced level of immunodeterminant expression. Unlike the reactions of the type Ia polysaccharides with homologous rabbit antiserum, the Ib native and core polysaccharides were able to react with identical populations of antibodies in type Ib-specific antiserum. A minor population of antibodies was demonstrated in the type Ib antiserum, which was reactive with the degalactosylated polysaccharide. That a population of antibodies reactive toward the degalactosylated polysaccharide is present in both type Ia and type Ib antisera suggests that the Iabc cross-reacting determinant is due to the presence of serum antibodies reactive with this trisaccharide repeating unit, which is shared by both the type Ia and the type Ib native and core polysaccharides.
NCBI PubMed ID: 3934276Journal NLM ID: 2985117RPublisher: Bethesda, MD: American Association of Immunologists
Methods: serological methods
- Article ID: 4049
Knirel YA, Shevelev SD, Perepelov AV "Higher aldulosonic acids: components of bacterial glycans" -
Mendeleev Communications 21(4) (2011) 173-182
Recent data on the natural occurrence, chemistry, and biochemistry of C8 and C9 aldulosonic acids (3-deoxy-d-manno-oct-2-ulosonic acid, sialic acids, N-acyl derivatives of 5,7-diamino-3,5,7,9-tetradeoxynon-2-ulosonic acids, and some others) as well as on the structures and biological significance of bacterial glycans containing these higher acidic monosaccharides are summarized.
structure, Bacterial, glycan, aldulosonic acid, higher acidic monosaccharides, sialic acids
Publication DOI: 10.1016/j.mencom.2011.07.001Journal NLM ID: 9425965Publisher: Moscow: Academy of Sciences of the USSR; Cambridge,UK : Royal Society of Chemistry
Correspondence: knirel@ioc.ac.ru
Institutions: N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia
- Article ID: 4430
Ovodov YS "Bacterial capsular antigens. Structural patterns of capsular antigens" -
Biochemistry (Moscow) 71(9) (2006) 937-954
Structural patterns of bacterial capsular antigens including capsular polysaccharides and exoglycans are given in this review. In addition, the immunological activity of capsular antigens and their role in type specificity of bacteria are discussed.
structure, capsular polysaccharides, bacterial capsular antigens, bacterial exoglycans, immunological activity, type specificity
NCBI PubMed ID: 17009947Publication DOI: 10.1134/S000629790609001XJournal NLM ID: 0376536Publisher: Nauka/Interperiodica
Correspondence: ovoys@physiol.komisc.ru
Institutions: Institute of Physiology, Komi Science Center, Urals Branch of the Russian Academy of Sciences, Syktyvkar 167982, Russia
- Article ID: 4727
Stowell SR, Arthur CM, McBride R, Berger O, Razi N, Heimburg-Molinaro J, Rodrigues LC, Gourdine J, Noll AJ, von Gunten S, Smith DF, Knirel YA, Paulson JC, Cummings RD "Microbial glycan microarrays define key features of host-microbial interactions" -
Nature Chemical Biology 10(6) (2014) 470-476
Genomic approaches continue to provide unprecedented insight into the microbiome, yet host immune interactions with diverse microbiota can be difficult to study. We therefore generated a microbial microarray containing defined antigens isolated from a broad range of microbial flora to examine adaptive and innate immunity. Serological studies with this microarray show that immunoglobulins from multiple mammalian species have unique patterns of reactivity, whereas exposure of animals to distinct microbes induces specific serological recognition. Although adaptive immunity exhibited plasticity toward microbial antigens, immunological tolerance limits reactivity toward self. We discovered that several innate immune galectins show specific recognition of microbes that express self-like antigens, leading to direct killing of a broad range of Gram-negative and Gram-positive microbes. Thus, host protection against microbes seems to represent a balance between adaptive and innate immunity to defend against evolving antigenic determinants while protecting against molecular mimicry.
molecular mimicry, glycan, interaction, Gram-negative, galectins, Gram-positive, innate immunity, Glycomics
Publication DOI: 10.1038/nchembio.1525Journal NLM ID: 101231976Publisher: New York, NY: Nature Publishing Group
Correspondence: jpaulson@scripps.edu; rdcummi@emory.edu
Institutions: Department of Biochemistry and the Glycomics Center, Emory University School of Medicine, Atlanta, Georgia, USA, Department of Cell and Molecular Biology, The Scripps Research Institute, La Jolla, California, USA, Department of and Chemical Physiology, The Scripps Research Institute, La Jolla, California, USA
Methods: serological methods
- Article ID: 4835
Berti F, Ravenscroft N "Characterization of Carbohydrate Vaccines by NMR Spectroscopy" -
Methods in Molecular Biology 1331 (2015) 189-209
Physicochemical techniques are a powerful tool for the structural characterization of carbohydrate-based vaccines. High-field Nuclear Magnetic Resonance (NMR) spectroscopy has been established as an extremely useful and robust method for tracking the industrial manufacturing process of these vaccines from polysaccharide bulk antigen through to the final formulation. Here, we describe the use of proton NMR for structural identity and conformity testing of carbohydrate-based vaccines.
carbohydrates, capsular polysaccharide, antigens, nuclear magnetic resonance spectroscopy, vaccines
NCBI PubMed ID: 26169742Publication DOI: 10.1007/978-1-4939-2874-3_12Journal NLM ID: 9214969Publisher: Springer
Correspondence: francesco.x.berti@gsk.com
Institutions: Research, GSK Vaccines, Via Fiorentina 1, 53100, Siena, Italy
- Article ID: 5420
Del Bino L, Calloni I, Oldrini D, Raso MM, Cuffaro R, Arda A, Codee JDC, Jiménez-Barbero J, Adamo R "Regioselective Glycosylation Strategies for the Synthesis of Group Ia and Ib Streptococcus Related Glycans Enable Elucidating Unique Conformations of the Capsular Polysaccharides" -
Chemistry: a European Journal 25(71) (2019) 16277-16278
Group B Streptococcus serotypes Ia and Ib capsular polysaccharides are key targets for vaccine development. In spite of their immunospecifity these polysaccharides share high structural similarity. Both are composed of the same monosaccharide residues and differ only in the connection of the Neu5Ac α2-3 Gal side chain to the GlcNAc unit, which is a β1-4 linkage in serotype Ia and a β1-3 linkage in serotype Ib. The development of efficient regioselective routes for GlcNAc β1-3 [Glc β1-4]Gal synthons is described, which give access to different group B Streptococcus (GBS) Ia and Ib repeating unit frameshifts. These glycans were used to probe the conformation and molecular dynamics of the two polysaccharides, highlighting the different presentation of the protruding Neu5Ac α2-3 Gal moieties on the polysaccharide backbones and a higher flexibility of Ib polymer relative to Ia, which can impact epitope exposure.
conformation, synthesis, carbohydrates, Streptococcus, glycan, conformation analysis, glycosylation, regioselectivity, therapeutics
NCBI PubMed ID: 31506992Publication DOI: 10.1002/chem.201903527Journal NLM ID: 9513783Publisher: Weinheim: VCH Verlagsgesellschaft/Verlag I
Correspondence: roberto.x.adamo@gsk.com
Institutions: GSK, Via Fiorentina 1, 53100, Siena, Italy, CIC bioGUNE, Bizkaia Technology Park, Building 800, 48160, Derio, Spain, Department of Bioorganic Synthesis, Leiden University, 2333, Leiden, The Netherlands, Basque Foundation for Science IKERBASQUE, Bilbao, Spain, Department of Organic Chemistry II, Faculty of Science and Technology, University of the Basque Country, 48940, Leioa, Spain
Methods: 13C NMR, 1H NMR, NMR-2D, TLC, chemical synthesis, MD simulations, UV, optical rotation measurement, ESI-HR-MS, flash chromatography, conformational analysis
- Article ID: 5440
Goyette-Desjardins G, Vinogradov E, Okura M, Takamatsu D, Gottschalk M, Segura M "Structure determination of Streptococcus suis serotypes 7 and 8 capsular polysaccharides and assignment of functions of the cps locus genes involved in their biosynthesis" -
Carbohydrate Research 473 (2019) 36-45
Streptococcus suis serotypes 7 and 8 are counted among the top six S. suis serotypes causing clinical disease in pigs. Yet, limited information is available on these serotypes. Since S. suis serotyping system is based upon capsular polysaccharide (CPS) antigenicity and the CPS is considered a major virulence factor for encapsulated pathogens, here we determined for the first time the chemical compositions and structures of serotypes 7 and 8 CPSs. Chemical and spectroscopic data gave the following repeating unit sequences: [3)L-Rha(α1-P-2)D-Gal(α1-4)D-GlcA(β1-3)D-FucNAc4N(α1-]n for serotype 7 and [2)L-Rha(α1-P-4)D-ManNAc(β1-4)D-Glc(α1-]n for serotype 8. As serotype 8 CPS is identical to Streptococcus pneumoniae type 19F CPS, dot-blot analyses showed a strong reaction of the 19F polysaccharide with reference anti-S. suis serotype 8 rabbit serum. A correlation between S. suis serotypes 7 and 8 sequences and genes of those serotypes' loci encoding putative glycosyltransferases and polymerases responsible for the biosynthesis of the repeating units was tentatively established. Knowledge of CPS structure and composition will contribute to better dissect the role of this bacterial component in the pathogenesis of the disease caused by S. suis serotypes 7 and 8.
capsular polysaccharide, carbohydrate structure, Serotype 8, Streptococcus suis, Serotype 7
NCBI PubMed ID: 30605786Publication DOI: 10.1016/j.carres.2018.12.009Journal NLM ID: 0043535Publisher: Elsevier
Correspondence: M. Segura
Institutions: Swine and Poultry Infectious Diseases Research Center, Faculty of Veterinary Medicine, University of Montreal, 3200 Sicotte St., St-Hyacinthe, Quebec, J2S 2M2, Canada, Canadian Glycomics Network (GlycoNet), University of Alberta, 11227 Saskatchewan Dr., Edmonton, Alberta, T6G 2G2, Canada, National Research Council, 100 Sussex Dr., Ottawa, Ontario, K1A 0R6, Canada, Division of Bacterial and Parasitic Disease, National Institute of Animal Health, National Agriculture and Food Research Organization, 3-1-5 Kannondai, Tsukuba, Ibaraki, 305-0856, Japan, The United Graduate School of Veterinary Sciences, Gifu University, 1-1 Yanagido, Gifu, Gifu, 501-1193, Japan
Methods: gel filtration, 13C NMR, 1H NMR, NMR-2D, GLC-MS, sugar analysis, 31P NMR, acid hydrolysis, Western blotting, bioinformatic analysis
- Article ID: 5485
Paoletti LC, Kasper DL "Surface Structures of Group B Streptococcus Important in Human Immunity" -
Microbiology Spectrum 7(2) (2019) ID GPP3-0001-2017
The surface of the Gram-positive opportunistic pathogen Streptococcus agalactiae, or group B Streptococcus (GBS), harbors several carbohydrate and protein antigens with the potential to be effective vaccines. Capsular polysaccharides of all clinically-relevant GBS serotypes coupled to immunogenic proteins of both GBS and non-GBS origin have undergone extensive testing in animals that led to advanced clinical trials in healthy adult women. In addition, GBS proteins either alone or in combination have been tested in animals; a fusion protein construct has recently advanced to human clinical studies. Given our current understanding of the antigenicity and immunogenicity of the wide array of GBS surface antigens, formulations now exist for the generation of viable vaccines against diseases caused by GBS.
structure, capsular polysaccharides, group B Streptococcus, surface, vaccines, Streptococcus agalactiae, Gram-positive
NCBI PubMed ID: 30873933Publication DOI: 10.1128/microbiolspec.GPP3-0001-2017Journal NLM ID: 101634614Publisher: Washington, DC: ASM Press
Correspondence: Lawrence C. Paoletti
Institutions: Division of Immunology, Department of Microbiology and Immunobiology, Harvard Medical School, Boston, MA 02115
- Article ID: 5791
Knirel YA, Van Calsteren M "Bacterial exopolysaccharides" -
Book: Comprehensive Glycoscience: From Chemistry to Systems Biology. Reference Module in Chemistry, Molecular Sciences and Chemical Engineering (2021) 1-75
Bacterial extracellular polysaccharides are known as a cell-bound capsule, a sheath, or a slime, which is excreted into the environment. They play an important role in virulence of medical bacteria and plant-to-symbiont interaction and are used for serotyping of bacteria and production of vaccines. Some exopolysaccharides have commercial applications in industry, and claims of health benefits have been documented for an increasing number of them. Exopolysaccharides have diverse composition and structure, and some contain sugar and non-sugar components that are found in bacterial carbohydrates only. The present article provides an updated collection of the data on exopolysaccharides of various classes of gram-negative and gram-positive bacteria reported until the end of 2019. When known, biosynthesis pathways of exopolysaccharides are treated in a summary manner. References are made to structure and biosynthesis relatedness between exopolysaccharides of different bacterial taxa as well as between bacterial polysaccharides and mammalian glycosaminoglycans.
polysaccharide structure, Gram-negative bacteria, capsule, Biofilm, polysaccharide biosynthesis, gram-positive bacteria, Monosaccharide composition, Bacterial exopolysaccharide, non-sugar component
Publication DOI: 10.1016/B978-0-12-819475-1.00005-5Publisher: Elsevier
Correspondence: marie-rose.vancalsteren@canada.ca; yknirel@gmail.com
Editors: Barchi J, Kamerling H
Institutions: N. D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, Saint-Hyacinthe Research and Development Centre, Agriculture and Agri-Food Canada, Saint-Hyacinthe, QC, Canada
- Article ID: 6051
Duke JA, Paschall AV, Robinson LS, Knoot CJ, Vinogradov E, Scott NE, Feldman MF, Avci FY, Harding CM "Development and Immunogenicity of a Prototype Multivalent Group B Streptococcus Bioconjugate Vaccine" -
ACS Infectious Diseases 7(11) (2021) 3111-3123
Group B Streptococcus (GBS) is a leading cause of neonatal infections and invasive diseases in nonpregnant adults worldwide. Developing a protective conjugate vaccine targeting the capsule of GBS has been pursued for more than 30 years; however, it has yet to yield a licensed product. In this study, we present a novel bioconjugation platform for producing a prototype multivalent GBS conjugate vaccine and its subsequent analytical and immunological characterizations. Using a glycoengineering strategy, we generated strains of Escherichia coli that recombinantly express the type Ia, type Ib, and type III GBS capsular polysaccharides. We then combined the type Ia-, Ib-, and III-capsule-expressing E. coli strains with an engineered Pseudomonas aeruginosa exotoxin A (EPA) carrier protein and the PglS oligosaccharyltransferase. Coexpression of a GBS capsule, the engineered EPA protein, and PglS enabled the covalent attachment of the target GBS capsule to an engineered serine residue on EPA, all within the periplasm of E. coli. GBS bioconjugates were purified, analytically characterized, and evaluated for immunogenicity and functional antibody responses. This proof-of-concept study signifies the first step in the development of a next-generation multivalent GBS bioconjugate vaccine, which was validated by the production of conjugates that are able to elicit functional antibodies directed against the GBS capsule.
group B Streptococcus, capsule, conjugate vaccine, bioconjugation, bioconjugate, multivalent
NCBI PubMed ID: 34633812Publication DOI: 10.1021/acsinfecdis.1c00415Journal NLM ID: 101654580Publisher: Washington, DC: American Chemical Society
Correspondence: Fikri Y. Avci
; Christian M. Harding
Institutions: Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, USA, United States, Center for Molecular Medicine, University of Georgia, Athens, GA, USA, United States, VaxNewMo, St. Louis, Missouri 63110, United States, Human Health Therapeutics Centre, National Research Council Canada, Ottawa, ON K1A 0R6, Canada, Department of Microbiology and Immunology, University of Melbourne at the Peter Doherty Institute for Infection and Immunity, Parkville, Australia, Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, Missouri 63110, United States
Methods: 13C NMR, 1H NMR, NMR-2D, sugar analysis, ELISA, ESI-MS, Western blotting, HPLC, SEC, immunization, protein detection, opsonophagocytosis assay, glycoengineering, bioconjugation
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2. Compound ID: 836
Structure type: oligomer
Trivial name: 3'-sialyl-LeA
Contained glycoepitopes: IEDB_130653,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_1391962,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142353,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_146100,IEDB_149174,IEDB_149556,IEDB_150899,IEDB_150933,IEDB_151531,IEDB_152214,IEDB_153235,IEDB_174333,IEDB_190606,IEDB_241110,IEDB_423096,IEDB_461723,SB_116,SB_127,SB_137,SB_155,SB_165,SB_166,SB_170,SB_171,SB_172,SB_186,SB_187,SB_195,SB_29,SB_39,SB_68,SB_7,SB_84,SB_86,SB_88
The structure is contained in the following publication(s):
- Article ID: 230
Feizi T "Progress in deciphering the information content of the 'glycome' - a crescendo in the closing years of the millennium" -
Glycoconjugate Journal 17(7-9) (2000) 553-565
The closing years of the second millennium have been uplifting for carbohydrate biology. Optimism that oligosaccharide sequences are bearers of crucial biological information has been borne out by the constellation of efforts of carbohydrate chemists, biochemists, immunochemists, and cell- and molecular biologists. The direct involvement of specific oligosaccharide sequences in protein targeting and folding, and in mechanisms of infection, inflammation and immunity is now unquestioned. With the emergence of families of proteins with carbohydrate-binding activities, assignments of information content for defined oligosaccharide sequences will become more common, but the pinpointing and elucidation of the bioactive domains on oligosaccharides will continue to pose challenges even to the most experienced carbohydrate biologists. The neoglycolipid technology incorporates some of the key requirements for this challenge: namely the resolution of complex glycan mixtures, and ligand binding coupled with sequence determination by mass spectrometry.
monoclonal antibodies, mass spectrometry, blood group antigen, carbohydrate ligands, differentiation antigens, embryonic development, galectins, inflammation, leukocyte adhesion, neoglycolipids, oligosaccharide ligands, oligosaccharid probes, selectins
NCBI PubMed ID: 11421348Journal NLM ID: 8603310Publisher: Kluwer Academic Publishers
Correspondence: t.feizi@ic.ac.uk
Institutions: The Glycosciences Laboratory, Imperial College School of Medicine, Harrow, United Kingdom
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3. Compound ID: 4064
|
a-Neup5Ac-(2-3)-b-D-Galp-(1-3)-+
|
-6)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-Glcp-(1- |
Show graphically |
Structure type: polymer chemical repeating unit
Compound class: CPS
Contained glycoepitopes: IEDB_117715,IEDB_135813,IEDB_136044,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_1391962,IEDB_1391966,IEDB_141794,IEDB_141807,IEDB_142076,IEDB_142078,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_143794,IEDB_146100,IEDB_146664,IEDB_149138,IEDB_149139,IEDB_149141,IEDB_149174,IEDB_150899,IEDB_150933,IEDB_151531,IEDB_157001,IEDB_190606,IEDB_241110,IEDB_983931,SB_116,SB_124,SB_127,SB_133,SB_137,SB_145,SB_156,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_174,SB_186,SB_187,SB_192,SB_195,SB_29,SB_39,SB_6,SB_68,SB_7,SB_84,SB_88
The structure is contained in the following publication(s):
- Article ID: 1500
Cieslewicz MJ, Chaffin D, Glusman G, Kasper D, Madan A, Rodrigues S, Fahey J, Wessels MR, Rubens CE "Structural and genetic diversity of group B streptococcus capsular polysaccharides" -
Infection and Immunity 73(5) (2005) 3096-3103
Group B Streptococcus (GBS) is an important pathogen of neonates, pregnant women, and immunocompromised individuals. GBS isolates associated with human infection produce one of nine antigenically distinct capsular polysaccharides which are thought to play a key role in virulence. A comparison of GBS polysaccharide structures of all nine known GBS serotypes together with the predicted amino acid sequences of the proteins that direct their synthesis suggests that the evolution of serotype-specific capsular polysaccharides has proceeded through en bloc replacement of individual glycosyltransferase genes with DNA sequences that encode enzymes with new linkage specificities. We found striking heterogeneity in amino acid sequences of synthetic enzymes with very similar functions, an observation that supports horizontal gene transfer rather than stepwise mutagenesis as a mechanism for capsule variation. Eight of the nine serotypes appear to be closely related both structurally and genetically, whereas serotype VIII is more distantly related. This similarity in polysaccharide structure strongly suggests that the evolutionary pressure toward antigenic variation exerted by acquired immunity is counterbalanced by a survival advantage conferred by conserved structural motifs of the GBS polysaccharides
Bacterial Proteins, Streptococcus agalactiae, Bacterial Capsules, Genetic Variation
NCBI PubMed ID: 15845517Journal NLM ID: 0246127Publisher: American Society for Microbiology
Correspondence: craig.rubens@seattlechildrens.org
Institutions: Division of Infectious Diseases, Children's Hospital, University of Washington, Seattle, WA 98109, USA, Channing Division of Infectious Diseases, Children's Hospital Boston, Department of Microbiology and Molecular Genetics, Harvard Medical School Boston, Massachusetts, Institute for Systems Biology and Division of Infectious Diseases, Children's Hospital, University of Washington, 3 Seattle, Washington
Methods: genetic methods, biosynthetic methods
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4. Compound ID: 6262
|
a-Neup5Ac-(2-3)-b-D-Galp-(1-3)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-Glcp |
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Structure type: oligomer
Compound class: O-antigen
Contained glycoepitopes: IEDB_117715,IEDB_135813,IEDB_136044,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_1391962,IEDB_1391966,IEDB_141794,IEDB_141807,IEDB_142076,IEDB_142078,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_143794,IEDB_146100,IEDB_146664,IEDB_149174,IEDB_150899,IEDB_150933,IEDB_151531,IEDB_157001,IEDB_190606,IEDB_241110,IEDB_983931,SB_116,SB_124,SB_127,SB_133,SB_137,SB_145,SB_156,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_174,SB_186,SB_187,SB_192,SB_195,SB_29,SB_39,SB_6,SB_68,SB_7,SB_84,SB_88
The structure is contained in the following publication(s):
- Article ID: 2827
Hayrinen J, Pelkonen S, Finne J "Structural similarity of the type-specific group B streptococcal polysaccharides and the carbohydrate units of tissue glycoproteins: evaluation of possible cross-reactivity" -
Vaccine 7 (1989) 217-224
Journal NLM ID: 8406899Publisher: Elsevier
- Article ID: 5647
Wharton RE, Stefanov EK, King RG, Kearney JF "Antibodies generated against Streptococci protect in a mouse model of disseminated aspergillosis" -
Journal of Immunology 194(9) (2015) 4387-4396
Invasive aspergillosis (IA) resulting from infection by Aspergillus fumigatus is a leading cause of death in immunosuppressed populations. There are limited therapeutic options for this disease and currently no vaccine. There is evidence that some anti-A. fumigatus mAbs can provide protection against IA. However, vaccine development has been impeded by a paucity of immunological targets on this organism demonstrated to provide protective responses. Sialylated oligosaccharide epitopes found on a variety of pathogens, including fungi and group B streptococci (GBS), are thought to be major virulence factors of these organisms facilitating pathogen attachment to host cells and modulating complement activation and phagocytosis. Because some of these oligosaccharide structures are conserved across kingdoms, we screened a panel of mAbs raised against GBS serotypes for reactivity to A. fumigatus. This approach revealed that SMB19, a GBSIb type-specific mAb, reacts with A. fumigatus conidia and hyphae. The presence of this Ab in mice, as a result of passive or active immunization, or by enforced expression of the SMB19 H chain as a transgene, results in significant protection in both i.v. and airway-induced models of IA. This study demonstrates that some Abs generated against bacterial polysaccharides engage fungal pathogens and promote their clearance in vivo and thus provide rationale of alternative strategies for the development of vaccines or therapeutic mAbs against these organisms
immunization, vaccine, aspergillosis, Aspergillus fumigatus
NCBI PubMed ID: 25821219Publication DOI: 10.4049/jimmunol.1401940Journal NLM ID: 2985117RPublisher: Bethesda, MD: American Association of Immunologists
Correspondence: Kearney JF
Institutions: Department of Microbiology, University of Alabama at Birmingham, Birmingham, USA, Department of Pathology, University of Alabama at Birmingham, Birmingham, USA
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5. Compound ID: 12884
|
/Variants 0/-a-Neup5Ac-(2-3)-b-D-Galp-(1-3)-b-D-GlcpNAc-(1-3)-+
|
-4)-b-D-Glcp-(1-4)-b-D-Galp-(1-
/Variants 0/ is:
?%Ac-9)-
OR (exclusively)
?%Ac-8)-
OR (exclusively)
?%Ac-7)- |
Show graphically |
Structure type: polymer chemical repeating unit
Compound class: CPS
Contained glycoepitopes: IEDB_117715,IEDB_135813,IEDB_136044,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_1391962,IEDB_1391966,IEDB_141589,IEDB_141794,IEDB_141807,IEDB_142076,IEDB_142078,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_143794,IEDB_146100,IEDB_146664,IEDB_149174,IEDB_150899,IEDB_150933,IEDB_151531,IEDB_157001,IEDB_190606,IEDB_241110,IEDB_983931,SB_116,SB_124,SB_127,SB_133,SB_137,SB_145,SB_156,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_174,SB_186,SB_187,SB_192,SB_195,SB_29,SB_39,SB_6,SB_68,SB_7,SB_84,SB_88
The structure is contained in the following publication(s):
- Article ID: 5129
Berti F, De Ricco R, Rappuoli R "Role of O-Acetylation in the Immunogenicity of Bacterial Polysaccharide Vaccines" -
Molecules 23(6) (2018) 1340
The incidence of infectious diseases caused by several bacterial pathogens such as Haemophilus influenzae type b, Streptococcus pneumoniae, and Neisseria meningitidis, has been dramatically reduced over the last 25 years through the use of glycoconjugate vaccines. The structures of the bacterial capsular polysaccharide (CPS) antigens, extracted and purified from microbial cultures and obtained with very high purity, show that many of them are decorated by O-acetyl groups. While these groups are often considered important for the structural identity of the polysaccharides, they play a major role in the functional immune response to some vaccines such as meningococcal serogroup A and Salmonella typhi Vi, but do not seem to be important for many others, such as meningococcal serogroups C, W, Y, and type III Group B Streptococcus. This review discusses the O-acetylation status of CPSs and its role in the immunological responses of these antigens.
O-acetylation, Bacterial polysaccharide, conjugate vaccines, Bacterial Vaccines, carbohydrate antigens
NCBI PubMed ID: 29865239Publication DOI: 10.3390/molecules23061340Journal NLM ID: 100964009Publisher: Basel, Switzerland: MDPI
Correspondence: rino.x.rappuoli@gsk.com
Institutions: External R&D, GSK Vaccines, 53100 Siena, Italy, External R&D, GSK Vaccines, 53100 Siena, Ital
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6. Compound ID: 14028
|
a-Neup5Ac-(2-3)-b-D-Galp-(1-3)-b-D-GlcpNAc-(1-3)-+
|
-4)-b-D-Galp-(1-4)-b-D-Glcp-(1- |
Show graphically |
Structure type: polymer chemical repeating unit
Aglycon: carrier protein CRM197,TT
Compound class: CPS
Contained glycoepitopes: IEDB_117715,IEDB_135813,IEDB_136044,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_1391962,IEDB_1391966,IEDB_141589,IEDB_141794,IEDB_141807,IEDB_142076,IEDB_142078,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_143794,IEDB_146100,IEDB_146664,IEDB_149174,IEDB_150899,IEDB_150933,IEDB_151531,IEDB_157001,IEDB_190606,IEDB_241110,IEDB_983931,SB_116,SB_124,SB_127,SB_133,SB_137,SB_145,SB_156,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_174,SB_186,SB_187,SB_192,SB_195,SB_29,SB_39,SB_6,SB_68,SB_7,SB_84,SB_88
The structure is contained in the following publication(s):
- Article ID: 5541
Sun X, Stefanetti G, Berti F, Kasper DL "Polysaccharide structure dictates mechanism of adaptive immune response to glycoconjugate vaccines" -
Proceedings of the National Academy of Sciences of the USA 116(1) (2019) 193-198
Glycoconjugate vaccines are among the most effective interventions for preventing several serious infectious diseases. Covalent linkage of the bacterial capsular polysaccharide to a carrier protein provides CD4+ T cells with epitopes that facilitate a memory response to the polysaccharide. Classically, the mechanism responsible for antigen processing was thought to be similar to what was known for hapten-carrier conjugates: protease digestion of the carrier protein in the endosome and presentation of a resulting peptide to the T cell receptor on classical peptide-recognizing CD4+ T cells. Recently, an alternative mechanism has been shown to be responsible for the memory response to some glycoconjugates. Processing of both the protein and the polysaccharide creates glycopeptides in the endosome of antigen-presenting cells. For presentation, the peptide portion of the glycopeptide is bound to MHCII, allowing the covalently linked glycan to activate carbohydrate-specific helper CD4+ T cells (Tcarbs). Herein, we assessed whether this same mechanism applies to conjugates prepared from other capsular polysaccharides. All of the glycoconjugates tested induced Tcarb-dependent responses except that made with group C Neisseria meningitidis; in the latter case, only peptides generated from the carrier protein were critical for helper T cell recognition. Digestion of this acid-sensitive polysaccharide, a linear homopolymer of α(2 → 9)-linked sialic acid, to the size of the monomeric unit resulted in a dominant CD4+ T cell response to peptides in the context of MHCII. Our results show that different mechanisms of presentation, based on the structure of the carbohydrate, are operative in response to different glycoconjugate vaccines.
vaccine, glycoconjugate, Tcarb, antigen presentation, group C Neisseria meningitidis
NCBI PubMed ID: 30510007Publication DOI: 10.1073/pnas.1816401115Journal NLM ID: 7505876Publisher: National Academy of Sciences
Correspondence: D.L. Kasper
Institutions: Department of Microbiology and Immunobiology, Harvard Medical School, Boston, MA 02115, Graduate Program in Immunology, Harvard Medical School, Boston, MA 02115, Department of Chemistry, University of Milan, 20133 Milan, Italy, Technical R&D, GSK Vaccines, 53100 Siena, Italy
Methods: ELISA, biological assays, serological methods, HPSEC, statistical analysis, immunization, conjugation, flow cytometry analysis, antigen presentation by BMDCs
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7. Compound ID: 14432
|
a-Neup5Ac-(2-3)-b-D-Galp-(1-3)-+
|
-3)-b-D-Glcp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1- |
Show graphically |
Structure type: polymer chemical repeating unit
Compound class: CPS
Contained glycoepitopes: IEDB_135813,IEDB_136044,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_1391962,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142488,IEDB_143794,IEDB_146100,IEDB_146664,IEDB_149174,IEDB_150899,IEDB_150933,IEDB_151531,IEDB_157001,IEDB_190606,IEDB_241110,IEDB_983931,SB_116,SB_127,SB_137,SB_156,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_186,SB_187,SB_192,SB_195,SB_29,SB_39,SB_68,SB_7,SB_84,SB_88
The structure is contained in the following publication(s):
- Article ID: 5741
Carboni F, Adamo R "Structure-based glycoconjugate vaccine design: The example of Group B Streptococcus type III capsular polysaccharide" -
Drug Discovery Today: Technologies (2020) 23-33
Microbial surface polysaccharides are important virulence factors and targets for vaccine development. Glycoconjugate vaccines, obtained by covalently linking carbohydrates and proteins, are well established tools for prevention of bacterial infections. Elucidation of the minimal portion involved in the interactions with functional antibodies is of utmost importance for the understanding of their mechanism of induction of protective immune responses and the design of synthetic glycan based vaccines. Typically, this is achieved by combination of different techniques, which include ELISA, glycoarray, Surface Plasmon Resonance in conjunction with approaches for mapping at atomic level the position involved in binding, such as Saturation Transfer NMR and X-ray crystallography. This review provides an overview of the structural studies performed to map glycan epitopes (glycotopes), with focus on the highly complex structure of Group B Streptococcus type III (GBSIII) capsular polysaccharide. Furthermore, it describes the rational process followed to translate the obtained information into the design of a protective glycoconjugate vaccine based on a well-defined synthetic glycan epitope.
carbohydrates, glycoconjugates, group B Streptococcus, vaccines, Structural glycobiology
NCBI PubMed ID: 33388125Publication DOI: 10.1016/j.ddtec.2020.11.003Journal NLM ID: 101235076Publisher: Oxford: Elsevier
Correspondence: R. Adamo
Institutions: GSK, Via Fiorentina 1, 53100 Siena, Italy
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8. Compound ID: 15164
|
a-D-Manp-(1-3)-+
|
a-D-Manp-(1-6)-+ | ?%D-Galp-(1-3)-+
| | |
a-D-Manp-(1-3)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc-(1-?)-Subst-(1-2)-EtN-(1--P--6)--a-D-Manp-(1-2)-+
|
a-Neup5Ac-(2-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+ |
| |
a-Neup5Ac-(2-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+ | | /Variants 0/-+ Ste-(1-1)-+
| | | | |
a-Neup5Ac-(2-3)-b-D-Galp-(1-3)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-3)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-3)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-3)-a-D-Galp-(1-3)-a-D-Manp-(1-6)-a-D-Manp-(1-4)-a-D-GlcpN-(1-6)-myoIno-(1--P--3)--Gro
/Variants 0/ is:
Ste-(1-2)-
OR (inclusively)
Pam-(1-2)-
OR (inclusively)
C18={?}-(1-2)-
Subst = protein |
Show graphically |
Structure type: oligomer
Trivial name: procyclin glycoprotein
Compound class: GPI-anchor, GPI-anchored polypeptides
Contained glycoepitopes: IEDB_120354,IEDB_123886,IEDB_123890,IEDB_130646,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_136104,IEDB_136794,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_1391962,IEDB_140108,IEDB_140116,IEDB_140122,IEDB_141181,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_142078,IEDB_143242,IEDB_143632,IEDB_143794,IEDB_144983,IEDB_144993,IEDB_146100,IEDB_149174,IEDB_150899,IEDB_150933,IEDB_151079,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153220,IEDB_153529,IEDB_157001,IEDB_158533,IEDB_164174,IEDB_187201,IEDB_190606,IEDB_241110,IEDB_241112,IEDB_423120,IEDB_429156,IEDB_474450,IEDB_534865,IEDB_548907,IEDB_857734,IEDB_983930,SB_115,SB_116,SB_127,SB_131,SB_136,SB_137,SB_156,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_186,SB_187,SB_191,SB_195,SB_196,SB_197,SB_198,SB_29,SB_30,SB_33,SB_39,SB_44,SB_67,SB_68,SB_7,SB_72,SB_73,SB_74,SB_77,SB_84,SB_85,SB_88
The structure is contained in the following publication(s):
- Article ID: 5910
Cummings RD, Van Die I "Parasitic Infections" -
Book: In: Essentials of Glycobiology [Internet]. 3rd edition. (2017)
Parasitic protozoans and helminths (worms) synthesize glycans with structures often different from those typically found in vertebrates and are typically antigenic. Parasites also express glycan-binding proteins (GBPs) involved in host invasion and parasitism. As part of the disease process, parasite glycans can trigger the host's innate immune system, which can lead to the induction of adaptive immune responses. This chapter discusses the major roles of glycoconjugates in parasitic infections.
NCBI PubMed ID: 28876851Publication DOI: 10.1101/glycobiology.3e.043Publisher: Cold Spring Harbor (NY), Cold Spring Harbor Laboratory Press, 2015-2017
Correspondence: Richard D. Cummings
; Irma van Die
Editors: Varki A, Cummings RD, Esko JD
Institutions: Department of Surgery, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA, USA, Department of Molecular Cell Biology & Immunology, VU University Center, Amsterdam, The Netherlands
- Article ID: 6349
Cummings RD, Hokke CH, Haslam SM "Parasitic Infections" -
Book: Essentials of Glycobiology [Internet]. 4rd edition (2022)
Parasitic protozoans and helminths (worms) synthesize glycans with structures often different from those typically found in vertebrates, and are thus often antigenic. Parasites also express glycan-binding proteins (GBPs) involved in host invasion and parasitism. As part of the disease process, parasite glycans can trigger the host's innate immune system, which can lead to the induction of adaptive immune responses. This chapter discusses the major roles of glycoconjugates in parasitic infections.
NCBI PubMed ID: 35536961Publication DOI: 10.1101/glycobiology.4e.43Publisher: Cold Spring Harbor (NY): Cold Spring Harbor Laboratory Press
Correspondence: R.D. Cummings
Editors: Varki A, Cummings RD, Esko JD, Stanley P, Hart GW, Aebi M, Mohnen D, Kinoshita T, Packer NH, Prestegard JH, Schnaar RL, Seeberger RH
Institutions: Department of Surgery, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA, USA, Department of Molecular Cell Biology & Immunology, VU University Center, Amsterdam, The Netherlands
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9. Compound ID: 16051
|
b-D-Glcp-(1-6)-+
|
a-Neup5Ac-(2-3)-b-D-Galp-(1-3)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1--/(1->1)3-aminopropyl/ |
Show graphically |
Structure type: oligomer
Aglycon: (1->1)3-aminopropyl
Compound class: CPS
Contained glycoepitopes: IEDB_135813,IEDB_136044,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_1391962,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142488,IEDB_143794,IEDB_146100,IEDB_146664,IEDB_149139,IEDB_149174,IEDB_150899,IEDB_150933,IEDB_151531,IEDB_157001,IEDB_190606,IEDB_241110,IEDB_983931,SB_116,SB_127,SB_137,SB_156,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_186,SB_187,SB_192,SB_195,SB_29,SB_39,SB_68,SB_7,SB_84,SB_88
The structure is contained in the following publication(s):
- Article ID: 6211
Del Bino L, Osterlid KE, Wu DY, Nonne F, Romano MR, Codée J, Adamo R "Synthetic Glycans to Improve Current Glycoconjugate Vaccines and Fight Antimicrobial Resistance" -
Chemical Reviews 122(20) (2022) 15672-15716
Antimicrobial resistance (AMR) is emerging as the next potential pandemic. Different microorganisms, including the bacteria Acinetobacter baumannii, Clostridioides difficile, Escherichia coli, Enterococcus faecium, Klebsiella pneumoniae, Neisseria gonorrhoeae, Pseudomonas aeruginosa, non-typhoidal Salmonella, and Staphylococcus aureus, and the fungus Candida auris, have been identified by the WHO and CDC as urgent or serious AMR threats. Others, such as group A and B Streptococci, are classified as concerning threats. Glycoconjugate vaccines have been demonstrated to be an efficacious and cost-effective measure to combat infections against Haemophilus influenzae, Neisseria meningitis, Streptococcus pneumoniae, and, more recently, Salmonella typhi. Recent times have seen enormous progress in methodologies for the assembly of complex glycans and glycoconjugates, with developments in synthetic, chemoenzymatic, and glycoengineering methodologies. This review analyzes the advancement of glycoconjugate vaccines based on synthetic carbohydrates to improve existing vaccines and identify novel candidates to combat AMR. Through this literature survey we built an overview of structure-immunogenicity relationships from available data and identify gaps and areas for further research to better exploit the peculiar role of carbohydrates as vaccine targets and create the next generation of synthetic carbohydrate-based vaccines.
carbohydrates, glycan, glycoconjugate vaccine
NCBI PubMed ID: 35608633Publication DOI: 10.1021/acs.chemrev.2c00021Journal NLM ID: 2985134RPublisher: Chem Rev
Correspondence: J. Codée
; R. Adamo
Institutions: GSK, R&D, 53100 Siena, Italy, Leiden Institute of Chemistry, Leiden University, 2300 RA Leiden, The Netherlands
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Total list of structure IDs on all result pages of the current query:
Total list of corresponding CSDB IDs (record IDs):
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