Show legend Show as text

Structure type: oligomer
Aglycon: core
Trivial name: polymannan
Compound class: O-polysaccharide
Contained glycoepitopes: IEDB_115576,IEDB_130701,IEDB_136104,IEDB_140116,IEDB_141111,IEDB_141795,IEDB_141807,IEDB_141830,IEDB_143632,IEDB_144983,IEDB_145662,IEDB_151531,IEDB_152206,IEDB_153756,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_164480,IEDB_174840,IEDB_241100,IEDB_76933,IEDB_983930,SB_136,SB_196,SB_197,SB_44,SB_67,SB_72

• Article ID: 3832
  Clarke BR, Cuthbertson L, Whitfield C "Nonreducing terminal modifications determine the chain length of polymannose O antigens of Escherichia coli and couple chain termination to polymer export via an ATP-binding cassette transporter" - Journal of Biological Chemistry 279(34) (2004) 35709-35718
  

  The chain length of bacterial lipopolysaccharide O antigens is regulated to give a modal distribution that is critical for pathogenesis. This paper describes the process of chain length determination in the ATP-binding cassette (ABC) transporter-dependent pathway, a pathway that is widespread among Gram-negative bacteria. Escherichia coli O8 and O9/O9a polymannans are synthesized in the cytoplasm, and an ABC transporter exports the nascent polymer across the inner membrane prior to completion of the LPS molecule. The polymannan O antigens have nonreducing terminal methyl groups. The 3-O-methyl group in serotype O8 is transferred from S-adenosylmethionine by the WbdD(O8) enzyme, and this modification terminates polymerization. Methyl groups are added to the O9a polymannan in a reaction dependent on preceding phosphorylation. The bifunctional WbdD(O9a) catalyzes both reactions, but only the kinase activity controls chain length. Chain termination occurs in a mutant lacking the ABC transporter, indicating that it precedes export. An E. coli wbdD(O9a) mutant accumulated O9a polymannan in the cytoplasm, indicating that WbdD activity coordinates polymannan chain termination with export across the inner membrane.

  serotype, Escherichia coli, O-antigens, structure-activity relationship, ABC transporter, chain length

  NCBI PubMed ID: 15184370
  Publication DOI: 10.1074/jbc.M404738200
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: cwhitfie@uoguelph.ca
  Institutions: Department of Microbiology, University of Guelph, Guelph, Ontario N1G 2W1, Canada
  Methods: serological methods, genetic methods, biochemical methods, immunofluorescence microscopy
  
   
  
  Escherichia coli O9, Klebsiella pneumoniae O3
  CSDB ID 25215 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: core
Trivial name: polymannan
Compound class: O-polysaccharide
Contained glycoepitopes: IEDB_115576,IEDB_130701,IEDB_136104,IEDB_140116,IEDB_141111,IEDB_141807,IEDB_141830,IEDB_143632,IEDB_144983,IEDB_145662,IEDB_151531,IEDB_152206,IEDB_164174,IEDB_164175,IEDB_164176,IEDB_174840,IEDB_241100,IEDB_76933,IEDB_983930,SB_136,SB_196,SB_197,SB_44,SB_67,SB_72

• Article ID: 3832
  Clarke BR, Cuthbertson L, Whitfield C "Nonreducing terminal modifications determine the chain length of polymannose O antigens of Escherichia coli and couple chain termination to polymer export via an ATP-binding cassette transporter" - Journal of Biological Chemistry 279(34) (2004) 35709-35718
  

  The chain length of bacterial lipopolysaccharide O antigens is regulated to give a modal distribution that is critical for pathogenesis. This paper describes the process of chain length determination in the ATP-binding cassette (ABC) transporter-dependent pathway, a pathway that is widespread among Gram-negative bacteria. Escherichia coli O8 and O9/O9a polymannans are synthesized in the cytoplasm, and an ABC transporter exports the nascent polymer across the inner membrane prior to completion of the LPS molecule. The polymannan O antigens have nonreducing terminal methyl groups. The 3-O-methyl group in serotype O8 is transferred from S-adenosylmethionine by the WbdD(O8) enzyme, and this modification terminates polymerization. Methyl groups are added to the O9a polymannan in a reaction dependent on preceding phosphorylation. The bifunctional WbdD(O9a) catalyzes both reactions, but only the kinase activity controls chain length. Chain termination occurs in a mutant lacking the ABC transporter, indicating that it precedes export. An E. coli wbdD(O9a) mutant accumulated O9a polymannan in the cytoplasm, indicating that WbdD activity coordinates polymannan chain termination with export across the inner membrane.

  serotype, Escherichia coli, O-antigens, structure-activity relationship, ABC transporter, chain length

  NCBI PubMed ID: 15184370
  Publication DOI: 10.1074/jbc.M404738200
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: cwhitfie@uoguelph.ca
  Institutions: Department of Microbiology, University of Guelph, Guelph, Ontario N1G 2W1, Canada
  Methods: serological methods, genetic methods, biochemical methods, immunofluorescence microscopy
  
   
  
  Escherichia coli O9a
  CSDB ID 25286 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: methylmannose polysaccharides (MMPs)
Contained glycoepitopes: IEDB_130701,IEDB_140116,IEDB_144983,IEDB_145662,IEDB_152206,IEDB_76933,IEDB_983930,SB_44,SB_67,SB_72

• Article ID: 4352
  Mendes V, Maranha A, Alarico S, Empadinhas N "Biosynthesis of mycobacterial methylglucose lipopolysaccharides" - Natural Product Reports 29(8) (2012) 834-844
  

  Mycobacterial pathogenesis is closely associated with a unique cell envelope rich in complex carbohydrates and unique lipids, among which are the mycolic acids. Mycobacteria also synthesize unique intracellular polymethylated polysaccharides (PMPSs), namely methylglucose lipopolysaccharides (MGLPs), which are acylated with short-chain fatty acids, and methylmannose polysaccharides (MMPs). Since PMPSs modulate the synthesis of long-chain fatty acids in vitro, the possibility of a similar role in vivo and the regulation of mycolic acids assembly have been anticipated. Unlike MGLPs, MMPs have been identified in M. smegmatis and other fast-growing mycobacteria but not in M. tuberculosis, implying an essential role for MGLPs in this pathogen and turning the biosynthetic enzymes into attractive drug targets. The genome of M. tuberculosis was decoded 14 years ago but only recently has the identity of the genes involved in MGLPs biosynthesis been investigated. Two gene clusters (Rv1208-Rv1213 and Rv3030-Rv3037c) containing a few genes considered to be essential for M. tuberculosis growth, have initially been proposed to coordinate MGLPs biosynthesis. Among these genes, only the product of Rv1208 for the first step in the MGLPs pathway has, so far, been crystallized and its three-dimensional structure been determined. However, recent results indicate that at least three additional clusters may be involved in this pathway. The functional assignment of authentic roles to some of these M. tuberculosis H37Rv genes sheds new light on the intricacy of MGLPs biogenesis and renewed interest on their biological role.

  biosynthesis, synthesis, structure, Pathogenesis, regulation, gene cluster, Mycobacteria, cell envelope, mycolic acid, polymethylated polysaccharides (PMPSs)

  NCBI PubMed ID: 22678749
  Publication DOI: 10.1039/c2np20014g
  Journal NLM ID: 8502408
  Publisher: London: Royal Society of Chemistry
  Correspondence: numenius@cnc.uc.pt
  Institutions: CNC-Center for Neuroscience and Cell Biology, University of Coimbra, 3004-517 Coimbra, Portugal
  
   
  
  Mycobacterium smegmatis
  CSDB ID 28457 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_115576,IEDB_130701,IEDB_136104,IEDB_137485,IEDB_140116,IEDB_142357,IEDB_143632,IEDB_144983,IEDB_144995,IEDB_145662,IEDB_152206,IEDB_164174,IEDB_164479,IEDB_983930,SB_136,SB_196,SB_197,SB_44,SB_67,SB_72

• Article ID: 5142
  Clarke BR, Ovchinnikova OG, Kelly SD, Williamson ML, Butler JE, Liu B, Wang L, Gou X, Follador R, Lowary TL, Whitfield C "Molecular basis for the structural diversity in serogroup O2-antigen polysaccharides in Klebsiella pneumoniae" - Journal of Biological Chemistry 293(13) (2018) 4666-4679
  

  Klebsiella pneumoniae is a major health threat. Vaccination and passive immunization are considered as alternative therapeutic strategies for managing Klebsiella infections. Lipopolysaccharide O antigens are attractive candidates because of the relatively small range of known O-antigen polysaccharide structures, but immunotherapeutic applications require a complete understanding of the structures found in clinical settings. Currently, the precise number of Klebsiella O antigens is unknown because available serological tests have limited resolution, and their association with defined chemical structures is sometimes uncertain. Molecular serotyping methods can evaluate clinical prevalence of O serotypes but require a full understanding of the genetic determinants for each O-antigen structure. This is problematic with Klebsiella pneumoniae because genes outside the main rfb (O-antigen biosynthesis) locus can have profound effects on the final structure. Here, we report two new loci encoding enzymes that modify a conserved polysaccharide backbone comprising disaccharide repeat units [→3)-α-d-Galp-(1→3)-β-d-Galf-(1→] (O2a antigen). We identified in serotype O2aeh a three-component system that modifies completed O2a glycan in the periplasm by adding 1,2-linked α-Galp side-group residues. In serotype O2ac, a polysaccharide comprising disaccharide repeat units [→5)-β-d-Galf-(1→3)-β-d-GlcpNAc-(1→] (O2c antigen) is attached to the non-reducing termini of O2a-antigen chains. O2c-polysaccharide synthesis is dependent on a locus encoding three glycosyltransferase enzymes. The authentic O2aeh and O2c antigens were recapitulated in recombinant Escherichia coli hosts to establish the essential gene set for their synthesis. These findings now provide a complete understanding of the molecular genetic basis for the known variations in Klebsiella O-antigen carbohydrate structures based on the O2a backbone.

  polysaccharide, O antigen, polysaccharide structure, Gram-negative bacteria, glycosyltransferase, serotyping, lipopolysaccharide (LPS), carbohydrate structure, nuclear magnetic resonance (NMR), Klebsiella pneumonia

  NCBI PubMed ID: 29602878
  Publication DOI: 10.1074/jbc.RA117.000646
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: cwhitfie@uoguelph.ca
  Institutions: TEDA Institute of Biological Sciences and Biotechnology, Nankai University, 23 Hongda St. TEDA, Tianjin, China, LimmaTech Biologics AG, 8952 Schlieren, Switzerland, and the Department of Chemistry and Alberta Glycomics Centre, University of Alberta, Edmonton, AB, Canada, the Department of Molecular and Cellular Biology, University of Guelph, Guelph, Ontario, Canada N1G 2W1
  Methods: gel filtration, 13C NMR, 1H NMR, NMR-2D, PCR, DNA sequencing, SDS-PAGE, DNA techniques, bioinformatic analysis, mmunoblotting
  
   
  
  Klebsiella pneumoniae O5
  CSDB ID 12468 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure ; 1988.7 [M+Na]+
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_130701,IEDB_135813,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141831,IEDB_143632,IEDB_144983,IEDB_145662,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153220,IEDB_164174,IEDB_187201,IEDB_429156,IEDB_548907,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_33,SB_44,SB_53,SB_67,SB_72,SB_73,SB_74,SB_77,SB_85

• Article ID: 5923
  Feasley C, van der Wel H, West CM "Evolutionary diversity of social amoebae N-glycomes may support interspecific autonomy" - Glycoconjugate Journal 32(6) (2015) 345-359
  

  Multiple species of cellular slime mold (CSM) amoebae share overlapping subterranean environments near the soil surface. Despite similar life-styles, individual species form independent starvation-induced fruiting bodies whose spores can renew the life cycle. N-glycans associated with the cell surface glycocalyx have been predicted to contribute to interspecific avoidance, resistance to pathogens, and prey preference. N-glycans from five CSM species that diverged 300-600 million years ago and whose genomes have been sequenced were fractionated into neutral and acidic pools and profiled by MALDI-TOF-MS. Glycan structure models were refined using linkage specific antibodies, exoglycosidase digestions, MALDI-MS/MS, and chromatographic studies. Amoebae of the type species Dictyostelium discoideum express modestly trimmed high mannose N-glycans variably modified with core α3-linked Fuc and peripherally decorated with 0-2 residues each of β-GlcNAc, Fuc, methylphosphate and/or sulfate, as reported previously. Comparative analyses of D. purpureum, D. fasciculatum, Polysphondylium pallidum, and Actyostelium subglobosum revealed that each displays a distinctive spectrum of high-mannose species with quantitative variations in the extent of these modifications, and qualitative differences including retention of Glc, mannose methylation, and absence of a peripheral GlcNAc, fucosylation, or sulfation. Starvation-induced development modifies the pattern in all species but, except for universally observed increased mannose-trimming, the N-glycans do not converge to a common profile. Correlations with glycogene repertoires will enable future reverse genetic studies to eliminate N-glycomic differences to test their functions in interspecific relations and pathogen evasion.

  evolution, N-glycan, Dictyostelium, Cellular slime molds, Social amoebae

  NCBI PubMed ID: 25987342
  Publication DOI: 10.1007/s10719-015-9592-8
  Journal NLM ID: 8603310
  Publisher: Kluwer Academic Publishers
  Correspondence: Christopher M. West ; Christopher M. West
  Institutions: Department of Biochemistry & Molecular Biology, Oklahoma Center for Medical Glycobiology, University of Oklahoma Health Sciences Center, 975 NE 10th St., BRC-415, OUHSC, Oklahoma City, OK, 73104, USA
  Methods: SDS-PAGE, Western blotting, MALDI-TOF MS, enzymatic digestion, permethylation, column chromatography, MALDI-TOF/TOF MS, bioinformatic analysis (BLASTp)
  
   
  
  Polysphondylium pallidum
  CSDB ID 4490 (all data & tools)

Show legend Show as text

Structure type: oligomer ; 1255.52 [M+Na]+
Compound class: N-glycan
Contained glycoepitopes: IEDB_115015,IEDB_130701,IEDB_135813,IEDB_136045,IEDB_136104,IEDB_137340,IEDB_137485,IEDB_141793,IEDB_141807,IEDB_142489,IEDB_143632,IEDB_144562,IEDB_144983,IEDB_145662,IEDB_149135,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_153220,IEDB_164174,IEDB_174333,IEDB_983930,SB_136,SB_196,SB_197,SB_198,SB_44,SB_67,SB_72,SB_74,SB_85,SB_86

• Article ID: 7315
  Moshtanska V, Kujumdzieva A, Petrova V, Beeumen JV, Voelter W, Devreese B, Dolashka-Angelova P "Glycosylated Cu/Zn-superoxide dismutase from Kluyveromyces yeast, determined by mass spectrometry" - Biotechnology and Biotechnological Equipment 23 (2009) 718-721
  

  The primary structure of Cu/Zn SOD from Kluyveromyces marxianus NBIMCC 1984 (Cu/Zn-KmSOD) was elucidated by N-terminal sequencing of the intact protein and by determination of the amino acid sequences of the tryptic peptides through MALDI-TOF-TOF. The molecular mass of the SOD homodimer subunit, containing 152 amino acid residues, was calculated to be 15858,3 Da while by MALDI-TOF 17096,63 Da were determined. Only one tryptophan residue at position 33 and one linkage site—Asn-Ile/Leu-Thr- were identified in the polypeptide chain of Cu/Zn-KmSOD. The full oligosaccharide structure of the naturally glycosylated superoxide dismutase was determined by mass spectrometry. Enzymatialyc liberated N-glycan from the enzyme was analysed using MALDI-TOF and tandem mass spectrometry on a Q- Trap mass spectrometer. One methylated hexose and an external fucose, linked to the hexoses were identified in the glycan.

  MALDI-TOF, glycoprotein, yeast, Cu/Zn superoxide dismutase, Q-Trap, Kluyveromyces marxianus

  Publication DOI: 10.1080/13102818.2009.10818525
  Journal NLM ID: 101128940
  Publisher: Abingdon, UK: Taylor & Francis
  Correspondence: dolashka@orgchm.bas.bg
  Institutions: Institute of Organic Chemistry with Centre of Phytohemistry, Bulgarian Academy of Sciences, Sofia, Bulgaria, Sofia University, Biological Faculty, Department of General and Industrial Microbiology, Sofia, Bulgaria, Laboratory of Protein Biochemistry and Biomolecular Engineering, Ghent University, Ghent, Belgium, Institute of Biochemistry, University of Tübingen, Tübingen, Germany
  Methods: MALDI-MS, HPLC, enzymatic digestion, extraction, column chromatography, Lowry method
  
   
  
  Kluyveromyces marxianus NBIMCC 1984
  CSDB ID 44062 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: galactomannan
Contained glycoepitopes: IEDB_130701,IEDB_134623,IEDB_136044,IEDB_137472,IEDB_137485,IEDB_141794,IEDB_144983,IEDB_145662,IEDB_152206,IEDB_190606,IEDB_221845,IEDB_433717,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_44,SB_67,SB_7,SB_72,SB_88

• Article ID: 9509
  Bose S, Srivastava HC "Structure of a polysaccharide from the seeds of Cassia grandis L.F.: Part I. Hydrolytic studies" - Indian Journal of Chemistry 16 (1978) 966-969
  
  Journal NLM ID: 7613423
  
   
  
  Cassia grandis
  CSDB ID 130119 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: galactomannan
Contained glycoepitopes: IEDB_130701,IEDB_134623,IEDB_136044,IEDB_137472,IEDB_137485,IEDB_141794,IEDB_144983,IEDB_145662,IEDB_152206,IEDB_190606,IEDB_221845,IEDB_433717,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_44,SB_67,SB_7,SB_72,SB_88

• Article ID: 9509
  Bose S, Srivastava HC "Structure of a polysaccharide from the seeds of Cassia grandis L.F.: Part I. Hydrolytic studies" - Indian Journal of Chemistry 16 (1978) 966-969
  
  Journal NLM ID: 7613423
  
   
  
  Cassia grandis
  CSDB ID 130117 (all data & tools)