Show legend Show as text

Structure type: polymer chemical repeating unit
Compound class: CPS
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_150900,IEDB_151531,IEDB_225177,IEDB_885823

• Article ID: 671
  Gunawardena S, Reddy GP, Wang YH, Kolli VSK, Orlando R, Morris JG, Bush CA "Structure of a muramic acid containing capsular polysaccharide from the pathogenic strain of Vibrio vulnificus ATCC27562" - Carbohydrate Research 309(1) (1998) 65-76
  

  Vibrio vulnificus strains isolated from septicemia cases and from the environment show a wide variety of capsular types. In an attempt to find common structural features which can be correlated with pathogenicity and toxicity, we have determined structures of the capsular polysaccharides (CPS) from several pathogenic strains. We report the complete structure of the polysaccharide from the pathogenic V. vulnificus strain ATCC27562 using a combination of homonuclear and heteronuclear one-dimensional and two dimensional NMR experiments. The 13C and 1H NMR spectra, including the exchangeable amide proton resonances, have been completely assigned. The amide linkage between Ser and C6 of GalA has been unambiguously determined by water-suppressed 2D NOESY. To verify the structure established by NMR, we have fragmented the polymer employing the Smith degradation procedure. The Smith product identified by NMR and matrix-assisted laser desorption mass spectrometry is consistent with the proposed structure for the CPS, which is composed of D-GlcNAc, MurNAc, D-GalA, L-Rha and is serine-linked as shown: [formula: see text]

  structure, mass spectrometry, Vibrio, Capsular polysaccaride, NMR spectrometry

  NCBI PubMed ID: 9720237
  Publication DOI: 10.1016/s0008-6215(98)00115-3
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: bush@umbc.edu
  Institutions: Department of Chemistry and Biochemistry, University of Maryland Baltimore County 21250, USA, Complex carbohydrate Research Center and Department of Biochemistry and Molecular Biology, The University of Georgia, 220 Riverbend Road, Athens, GA 30602-4712, USA, Departments of Medicine and Pathology, University of Maryland School of Medicine and Veterans Affairs Medical Center, Baltimore, MD 21201, USA
  Methods: NMR-2D, NMR, Smith degradation
  
   
  
  Vibrio vulnificus ATCC 27562
  CSDB ID 466 (all data & tools)
• 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/B978-0-12-819475-1.00005-5
  Publisher: 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
  
   
  
  Vibrio vulnificus ATCC 27562
  CSDB ID 6665 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: CPS
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_150900,IEDB_151531

• Article ID: 671
  Gunawardena S, Reddy GP, Wang YH, Kolli VSK, Orlando R, Morris JG, Bush CA "Structure of a muramic acid containing capsular polysaccharide from the pathogenic strain of Vibrio vulnificus ATCC27562" - Carbohydrate Research 309(1) (1998) 65-76
  

  Vibrio vulnificus strains isolated from septicemia cases and from the environment show a wide variety of capsular types. In an attempt to find common structural features which can be correlated with pathogenicity and toxicity, we have determined structures of the capsular polysaccharides (CPS) from several pathogenic strains. We report the complete structure of the polysaccharide from the pathogenic V. vulnificus strain ATCC27562 using a combination of homonuclear and heteronuclear one-dimensional and two dimensional NMR experiments. The 13C and 1H NMR spectra, including the exchangeable amide proton resonances, have been completely assigned. The amide linkage between Ser and C6 of GalA has been unambiguously determined by water-suppressed 2D NOESY. To verify the structure established by NMR, we have fragmented the polymer employing the Smith degradation procedure. The Smith product identified by NMR and matrix-assisted laser desorption mass spectrometry is consistent with the proposed structure for the CPS, which is composed of D-GlcNAc, MurNAc, D-GalA, L-Rha and is serine-linked as shown: [formula: see text]

  structure, mass spectrometry, Vibrio, Capsular polysaccaride, NMR spectrometry

  NCBI PubMed ID: 9720237
  Publication DOI: 10.1016/s0008-6215(98)00115-3
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: bush@umbc.edu
  Institutions: Department of Chemistry and Biochemistry, University of Maryland Baltimore County 21250, USA, Complex carbohydrate Research Center and Department of Biochemistry and Molecular Biology, The University of Georgia, 220 Riverbend Road, Athens, GA 30602-4712, USA, Departments of Medicine and Pathology, University of Maryland School of Medicine and Veterans Affairs Medical Center, Baltimore, MD 21201, USA
  Methods: NMR-2D, NMR, Smith degradation
  
   
  
  Vibrio vulnificus ATCC 27562
  CSDB ID 575 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: peptidoglycan
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_1635957,IEDB_241115,IEDB_423183,IEDB_885814

• Article ID: 1112
  Popham DL, Helin J, Costello CE, Setlow P "Analysis of the peptidoglycan structure of Bacillus subtilis endospores" - Journal of Bacteriology 178(22) (1996) 6451-6458
  

  Peptidoglycan was prepared from purified Bacillus subtilis spores of wild-type and several mutant strains. Digestion with muramidase resulted in cleavage of the glycosidic bonds adjacent to muramic acid replaced by peptide or alanine side chains but not the bonds adjacent to muramic lactam. Reduction of the resulting muropeptides allowed their separation by reversed-phase high-pressure liquid chromatography. The structures of 20 muropeptides were determined by amino acid and amino sugar analysis and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. In wild-type spores, 50% of the muramic acid had been converted to the lactam and 75% of these lactam residues were spaced regularly at every second muramic acid position in the glycan chains. Single L-alanine side chains were found on 25% of the muramic acid residues. The remaining 25% of the muramic acid had tetrapeptide or tripeptide side chains, and 11% of the diaminopimelic acid in these side chains was involved in peptide cross-links. Analysis of spore peptidoglycan produced by a number of mutants lacking proteins involved in cell wall metabolism revealed structural changes. The most significant changes were in the spores of a dacB mutant which lacks the sporulation-specific penicillin-binding protein 5*. In these spores, only 46% of the muramic acid was in the lactam form, 12% had L-alanine side chains, and 42% had peptide side chains containing diaminopimelic acid, 29% of which was involved in cross-links.

  structure, structural, analysis, peptidoglycan, Bacillus, Bacillus subtilis

  NCBI PubMed ID: 8932300
  Journal NLM ID: 2985120R
  Publisher: American Society for Microbiology
  Correspondence: setlow@sun.uchc.edu
  Institutions: Department of Biochemistry, University of Connecticut Health Center, Farmington, Connecticut 06030-3305, Mass Spectrometry Resource, Department of Biophysics, Boston University School of Medicine, Boston, Massachusetts 02118-2394
  Methods: carboxyl reduction, amino acid analysis, MALDI-TOF MS, HPLC, enzymatic digestion, amino sugar analysis
  
   
  
  Bacillus subtilis
  CSDB ID 4065 (all data & tools)

Show legend Show as text

Structure type: monomer
C₉H₁₇N₁O₇
Trivial name: muramic acid

• Article ID: 1125
  Ragousis V, Leondiadis L, Livaniou E, Evangelatos GP "A simple approach to the synthesis of muramic acid and isomuramic acid: 1H and 13C NMR characterisation" - Carbohydrate Research 297(3) (1997) 289-295
  

  A simple and efficient synthesis of 2-amino-3-O-[(R)-1-carboxyethyl]-2-deoxy-D-glucose (muramic acid, 6) and its stereoisomer 2-amino-3-O-[(S)-1-carboxyethyl]-2-deoxy-D-glucose (isomuramic acid, 7) from methyl 2-acetamido-4,6-O-benzylidene-2-deoxy-a-D-glucopyranoside (1) is described. Condensation of the O-3 oxyanion of 1 with an excess of methyl (R,S)-2-bromopropionate, followed by alkaline hydrolysis of the crude product and subsequent acidification, afforded crystalline methyl 2-acetamido-4,6-O-benzylidene-3-O-[(R,S)-1-carboxyethyl]-2-deoxy-a-D-glucopyranoside (2), in 72% yeld, as a mixture of diastereomers. Esterification of 2 with an excess of diazomethane afforded quantitatively the corresponding mixture of epimeric esters, which were very easily separated by column chromatography on silica gel, giving pure (R) and (S) epimeric esters. Removal of the benzylidene and acetyl groups by acid hydrolysis gave, respectively, muramic acid (6), in 95% yield and isomuramic acid (7), in 93% yield. 1H and 13C NMR data are given.

  NMR, synthesis, acid, 13C NMR, characterisation, 1H NMR, approach, isomuramic acid, muramic acid, 2-acetamido-2-deoxyglucosides

  Publication DOI: 10.1016/S0008-6215(96)00271-6
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: Department of Chemistry, Laboratory of Organic Chemistry, University of Athens, Panepistimiopolis, Zographou, 15771 Athens, Greece, Immunochemistry Laboratory, Institute of Radioisotopes and Radiodiagnostic Products, National Centre for Scientific Research ''Demokritos'', Ag. Paraskeui, 153 IOAthens, Greece
  Methods: 13C NMR, 1H NMR
  
   
  
  (bacteria)
  CSDB ID 4301 (all data & tools)

Show legend Show as text

Structure type: polymer chemical repeating unit
Contained glycoepitopes: IEDB_137340,IEDB_141807,IEDB_150900,IEDB_151531,IEDB_225177,IEDB_885823

• Article ID: 1136
  Reddy GP, Hayat U, Xu QW, Reddy KV, Wang YH, Chiu KW, Morris JG, Bush CA "Structure determination of the capsular polysaccharide from Vibrio vulnificus strain 6353" - European Journal of Biochemistry 255(1) (1998) 279-288
  

  Vibrio vulnificus is a pathogenic gram-negative bacterium, endemic to brackish waters, which is often isolated from sediments, from the water column or from shellfish. It is associated with wound infections and septicemia in humans and the virulence of V. vulnificus has been strongly associated with encapsulation. The capsular polysaccharide purified from a virulent strain of V. vulnificus 6353 did not show cross reactivity with antibodies to the capsular polysaccharide of a related pathogenic strain of V. vulnificus (MO6-24) the structure of which was recently reported. NMR spectroscopic analysis of the purified polysaccharide from strain 6353 showed that the polymer is composed of four sugar residues per repeating subunit including 2,6-dideoxy-2-N-acetylamino-α-D-glucose (QuiNAc), 2-deoxy-2-N-acetylamino-α-D-galactose (α-D-GalNAc), 2-deoxy-2-N-acetylamino-α-D-galcturonic acid (α-D-GalNAcA) and 2-N-acetylamino-α-D-glucuronamide (α-D-GlcNAcANH2). The 1H- and 13C NMR spectra were completely assigned by homonuclear and heteronuclear NMR spectroscopy. Sugar types and anomeric configurations were determined from proton homonuclear coupling constants and glycosidic linkages were determined from 1H-13C heteronuclear multiple bond correlation spectra. Sugar identities were confirmed by high performance anion-exchange chromatography and absolute configurations were determined by gas chromatography in combination with molecular modeling and NMR spectroscopy. The structure of the polysaccharide repeating unit is: [→4)-α-D-GalpNAc-(1→3)-α-D-GalpNAcA-(1→3)-α-D-QuipNAc-(1→]n α-D-GlcpNAcANH2(1→4)-→. While there are some common features shared among the structures of the capsular polysaccharides of pathogenic strains of V. vulnificus, there are distinct differences in the detailed structures.

  NMR, structure, polysaccharide, bacteria, Vibrio, Vibrio vulnificus

  NCBI PubMed ID: 9692929
  Publication DOI: 10.1046/j.1432-1327.1998.2550279.x
  Journal NLM ID: 0107600
  Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
  Correspondence: bush@umbc.edu
  Institutions: Department of Chemistry and Biochemistry, University of Maryland Baltimore County, Baltimore MD, USA, Departments of Medicine and Pathology, University of Maryland School of Medicine and Veterans Affairs Medical Center, Baltimore MD, USA
  Methods: 13C NMR, 1H NMR, NMR-2D, HPLC
  
   
  
  Vibrio vulnificus ATCC 27562
  CSDB ID 4414 (all data & tools)

Show legend Show as text

Structure type: polymer chemical repeating unit
Compound class: CPS
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_150900,IEDB_151531,IEDB_225177,IEDB_885823

• Article ID: 1136
  Reddy GP, Hayat U, Xu QW, Reddy KV, Wang YH, Chiu KW, Morris JG, Bush CA "Structure determination of the capsular polysaccharide from Vibrio vulnificus strain 6353" - European Journal of Biochemistry 255(1) (1998) 279-288
  

  Vibrio vulnificus is a pathogenic gram-negative bacterium, endemic to brackish waters, which is often isolated from sediments, from the water column or from shellfish. It is associated with wound infections and septicemia in humans and the virulence of V. vulnificus has been strongly associated with encapsulation. The capsular polysaccharide purified from a virulent strain of V. vulnificus 6353 did not show cross reactivity with antibodies to the capsular polysaccharide of a related pathogenic strain of V. vulnificus (MO6-24) the structure of which was recently reported. NMR spectroscopic analysis of the purified polysaccharide from strain 6353 showed that the polymer is composed of four sugar residues per repeating subunit including 2,6-dideoxy-2-N-acetylamino-α-D-glucose (QuiNAc), 2-deoxy-2-N-acetylamino-α-D-galactose (α-D-GalNAc), 2-deoxy-2-N-acetylamino-α-D-galcturonic acid (α-D-GalNAcA) and 2-N-acetylamino-α-D-glucuronamide (α-D-GlcNAcANH2). The 1H- and 13C NMR spectra were completely assigned by homonuclear and heteronuclear NMR spectroscopy. Sugar types and anomeric configurations were determined from proton homonuclear coupling constants and glycosidic linkages were determined from 1H-13C heteronuclear multiple bond correlation spectra. Sugar identities were confirmed by high performance anion-exchange chromatography and absolute configurations were determined by gas chromatography in combination with molecular modeling and NMR spectroscopy. The structure of the polysaccharide repeating unit is: [→4)-α-D-GalpNAc-(1→3)-α-D-GalpNAcA-(1→3)-α-D-QuipNAc-(1→]n α-D-GlcpNAcANH2(1→4)-→. While there are some common features shared among the structures of the capsular polysaccharides of pathogenic strains of V. vulnificus, there are distinct differences in the detailed structures.

  NMR, structure, polysaccharide, bacteria, Vibrio, Vibrio vulnificus

  NCBI PubMed ID: 9692929
  Publication DOI: 10.1046/j.1432-1327.1998.2550279.x
  Journal NLM ID: 0107600
  Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
  Correspondence: bush@umbc.edu
  Institutions: Department of Chemistry and Biochemistry, University of Maryland Baltimore County, Baltimore MD, USA, Departments of Medicine and Pathology, University of Maryland School of Medicine and Veterans Affairs Medical Center, Baltimore MD, USA
  Methods: 13C NMR, 1H NMR, NMR-2D, HPLC
  
   
  
  Vibrio vulnificus ATCC 27562
  CSDB ID 4414 (all data & tools)

Show legend Show as text

Structure type: polymer chemical repeating unit
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_1635957,IEDB_885814

• Article ID: 1367
  Bateman KP, Banoub JH, Thibault P "Probing the microheterogeneity of O-specific chains from Yersinia ruckeri using capillary zone electrophoresis/electrospray mass spectrometry" - Electrophoresis 17(12) (1996) 1818-1828
  

  Lipopolysaccharide, LPS, chain, O-specific, spectrometry, mass spectrometry, Yersinia, Capillary zone electrophoresis, electrospray mass spectrometry, microheterogeneity, Yersinia ruckeri

  Journal NLM ID: 8204476
  Publisher: Wiley-VCH
  Correspondence: pierre.thibault@nec.ca
  Institutions: Institute for Marine Biosciences, Nova Scotia, Canada
  Methods: CE-ESI-MS
  
   
  
  Yersinia ruckeri
  CSDB ID 6244 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: undecaprenol-Z8E3
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_1635957,IEDB_885814

• Article ID: 1616
  Guan Z, Breazeale SD, Raetz CR "Extraction and identification by mass spectrometry of undecaprenyl diphosphate-MurNAc-pentapeptide-GlcNAc from Escherichia coli" - Analytical Biochemistry 345(2) (2005) 336-339
  

  Undecaprenyl diphosphate-MurNAc-pentapeptide-GlcNAc (lipid II) is extracted from Escherichia coli cells by utilizing its unusual pH-dependent solubility property in a Bligh-Dyer system, and identified by electrospray ionization mass spectrometry in conjunction with a novel 15N mass shift analysis. The described approach will facilitate the structural characterization of lipid II variants from diverse bacteria, including antibiotic-resistant mutants, as well as the numerous minor uncharacterized lipids present in all biological systems

  Escherichia coli, mass spectrometry, Lipid II, 15N mass shift analysis

  NCBI PubMed ID: 16118008
  Publication DOI: 10.1016/j.ab.2005.07.002
  Journal NLM ID: 0370535
  Publisher: Academic Press
  Correspondence: zguan@biochem.duke.edu
  Institutions: Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA
  Methods: ESI-MS
  
   
  
  Escherichia coli
  CSDB ID 10546 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: S-layer glycan
Contained glycoepitopes: IEDB_115015,IEDB_135813,IEDB_136105,IEDB_137340,IEDB_141807,IEDB_142489,IEDB_143253,IEDB_149135,IEDB_151531,IEDB_225177,IEDB_885823,SB_86

• Article ID: 1623
  Kahlig H, Kolarich D, Zayni S, Scheberl A, Kosma P, Schäffer C, Messner P "N-Acetylmuramic acid as capping element of a-D-fucose-containing S-layer glycoprotein glycans from Geobacillus tepidamans GS5-97T" - Journal of Biological Chemistry 280(21) (2005) 20292-20299
  

  Geobacillus tepidamans GS5-97(T) is a novel Gram-positive, moderately thermophilic bacterial species that is covered by a glycosylated surface layer (S-layer) protein. The isolated and purified S-layer glycoprotein SgtA was ultrastructurally and chemically investigated and showed several novel properties. By SDS-PAGE, SgtA was separated into four distinct bands in an apparent molecular mass range of 106-166 kDa. The three high molecular mass bands gave a positive periodic acid-Schiff staining reaction, whereas the 106-kDa band was nonglycosylated. Glycosylation of SgtA was investigated by means of chemical analyses, 600-MHz nuclear magnetic resonance spectroscopy, and electrospray ionization quadrupole time-of-fight mass spectrometry. Glycopeptides obtained after Pronase digestion revealed the glycan structure [→2)-α-L-Rhap-(1→3)-α-D-Fucp-(1→](n=approximately 20), with D-fucopyranose having never been identified before as a constituent of S-layer glycans. The rhamnose residue at the nonreducing end of the terminal repeating unit of the glycan chain was di-substituted. For the first time, (R)-N-acetylmuramic acid, the key component of prokaryotic peptidoglycan, was found in an α-linkage to carbon 3 of the terminal rhamnose residue, serving as capping motif of an S-layer glycan. In addition, that rhamnose was substituted at position 2 with a β-N-acetylglucosamine residue. The S-layer glycan chains were bound via the trisaccharide core →2)-α-L-Rhap-(1→3)-α-L-Rhap-(1→3)-α-L-Rhap-(1→ to carbon 3 of β-D-galactose, which was attached in O-glycosidic linkage to serine and threonine residues of SgtA of G. tepidamans GS5-97(T).

  structure, mass spectrometry, glycosylation, Gram-positive, glycoprotein, D-fucose, Geobacillus, SgtA, S-layer glycan

  NCBI PubMed ID: 15781455
  Publication DOI: 10.1074/jbc.M501724200
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Institutions: Department of Organic Chemistry, University of Vienna, Austria
  Methods: NMR, sugar analysis, amino acid analysis, MS
  
   
  
  Geobacillus tepidamans GS5-97T
  CSDB ID 10723 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: peptidoglycan
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_1635957,IEDB_885814

• Article ID: 1693
  Welzel P "Transglycosylase inhibition" - Book: Antibiotics and antiviral compounds: chemical synthesis and modification (1993) 373-378
  
  Publisher: Weinheim, New York: VCH
  Editors: Krohn K, Kirst HA, Maag H
  
   
  
  Escherichia coli
  CSDB ID 103840 (all data & tools)

Show legend Show as text

Structure type: polymer chemical repeating unit
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_1635957,IEDB_885814

• Article ID: 1778
  Knirel YA, Kochetkov NK "The structure of lipopolysaccharides of gram-negative bacteria. III. The structure of O-antigens: A review" - Biochemistry (Moscow) 59(12) (1994) 1325-1383
  

  This review summarizes data on the composition and structure of the O-antigens, the polysaccharide chains of the outer-membrane lipopolysaccharides (LPS) of Gram-negative bacteria defining the immunospecificity of these microbial cells. Special reference is given to some structural features of the O-antigens, such as the presence of unique monosaccharides and noncarbohydrate components, masked regularity, and the occurrence in one microorganism of LPS with structurally different polysaccharide chains. Antigenic relationships between microorganisms belonging to different taxonomic groups are discussed.

  structure, O-antigen, chemical composition, bacterial lipopolysaccharides, Salmonella livingstone C1

  NCBI PubMed ID: 7533007
  Journal NLM ID: 0376536
  Publisher: Nauka/Interperiodica
  Institutions: Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia
  
   
  
  Yersinia ruckeri II
  CSDB ID 108436 (all data & tools)
• Article ID: 1798
  Banoub JH, Shaw DH, Pang H, Krepinsky JJ, Nakhla NA, Patel T "Structural elucidation of the O-specific antigen of Yersinia ruckeri by fast atom bombardment mass spectrometry (FAB-MS)" - Biomedical and Environmental Mass Spectrometry 19 (1990) 787-790
  
  NCBI PubMed ID: 2088577
  Journal NLM ID: 8603224
  Publisher: Wiley
  Institutions: Northwest Atlantic Fisheries Centre, St. John's, Newfoundland, Canada
  Methods: FAB-MS
  
   
  
  Yersinia ruckeri
  CSDB ID 110300 (all data & tools)

Show legend Show as text

Structure type: oligomer ; 910.36
Trivial name: muramyl peptide
Compound class: peptidoglycan
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_1635957,IEDB_885814

• Article ID: 2538
  Johannsen L, Rosenthal RS, MArtin SA, Cady AB, Obal F (Jr), Guinand M, Krueger JM "Somnogenic activity of O-acetylated and dimeric muramyl peptides" - Infection and Immunity 57 (1989) 2726-2732
  

  Slow-wave sleep-promoting factors in brain and urine were identified as muramyl peptides (MPs), the building blocks of bacterial cell wall peptidoglycan. In this study, structural variations of MPs that occur naturally in bacterial peptidoglycan were investigated for somnogenic activity. Monomeric and dimeric MPs were isolated and purified from Neisseria gonorrhoeae and Actinomadura sp. strain R39. The structures of these MPs were verified by fast atom bombardment mass spectroscopy and tandem mass spectroscopy. After intracerebroventricular administration of MPs, electroencephalograms and brain temperatures of rabbits were recorded for 6 h and were analyzed to determine durations of slow-wave sleep, rapid-eye-movement sleep, and wakefulness. The 6-O acetylation of muramic acid enhanced the somnogenic effects of certain monomeric MPs relative to their non-O-acetylated (but otherwise identical) counterparts. Two monomeric MPs containing an unsubstituted amide (i.e., Iso-Gln) were inactive, thus confirming previous results showing that amidation of a variety of MPs can block somnogenic activity. Two peptide-cross-linked MP dimers tested had no effect on slow-wave sleep, although a third peptide-cross-linked MP containing a 1,6-anhydro muramyl end on one of its monomeric subunits, a structure that enhances somnogenic potency of un-cross-linked monomers, was somnogenic. Two dimers connected by glycosidic bonds and containing an Iso-Gln moiety were inactive. Two other glycosidically linked dimers that also contained an Iso-Gln moiety, but were of lower molecular weight, were somnogenic. In summary, 6-O acetylation of muramic acid in somnogenic MPs enhances activity, and as a class, peptide-linked dimeric MPs tend to be less active than their constituent monomers.

  NCBI PubMed ID: 2759708
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Institutions: Department of Physiology and Biophysics, University of Tennessee, Memphis 38163
  Methods: FAB-MS, MS/MS, biological assays, HPLC
  
   
  
  Neisseria gonorrhoeae
  CSDB ID 130238 (all data & tools)

Show legend Show as text

Structure type: oligomer ; 868.35
Trivial name: muramyl peptide
Compound class: peptidoglycan
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_1635957,IEDB_885814

• Article ID: 2538
  Johannsen L, Rosenthal RS, MArtin SA, Cady AB, Obal F (Jr), Guinand M, Krueger JM "Somnogenic activity of O-acetylated and dimeric muramyl peptides" - Infection and Immunity 57 (1989) 2726-2732
  

  Slow-wave sleep-promoting factors in brain and urine were identified as muramyl peptides (MPs), the building blocks of bacterial cell wall peptidoglycan. In this study, structural variations of MPs that occur naturally in bacterial peptidoglycan were investigated for somnogenic activity. Monomeric and dimeric MPs were isolated and purified from Neisseria gonorrhoeae and Actinomadura sp. strain R39. The structures of these MPs were verified by fast atom bombardment mass spectroscopy and tandem mass spectroscopy. After intracerebroventricular administration of MPs, electroencephalograms and brain temperatures of rabbits were recorded for 6 h and were analyzed to determine durations of slow-wave sleep, rapid-eye-movement sleep, and wakefulness. The 6-O acetylation of muramic acid enhanced the somnogenic effects of certain monomeric MPs relative to their non-O-acetylated (but otherwise identical) counterparts. Two monomeric MPs containing an unsubstituted amide (i.e., Iso-Gln) were inactive, thus confirming previous results showing that amidation of a variety of MPs can block somnogenic activity. Two peptide-cross-linked MP dimers tested had no effect on slow-wave sleep, although a third peptide-cross-linked MP containing a 1,6-anhydro muramyl end on one of its monomeric subunits, a structure that enhances somnogenic potency of un-cross-linked monomers, was somnogenic. Two dimers connected by glycosidic bonds and containing an Iso-Gln moiety were inactive. Two other glycosidically linked dimers that also contained an Iso-Gln moiety, but were of lower molecular weight, were somnogenic. In summary, 6-O acetylation of muramic acid in somnogenic MPs enhances activity, and as a class, peptide-linked dimeric MPs tend to be less active than their constituent monomers.

  NCBI PubMed ID: 2759708
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Institutions: Department of Physiology and Biophysics, University of Tennessee, Memphis 38163
  Methods: FAB-MS, MS/MS, biological assays, HPLC
  
   
  
  Neisseria gonorrhoeae
  CSDB ID 130239 (all data & tools)

Show legend Show as text

Structure type: oligomer ; 1860.77
Trivial name: muramyl peptide
Compound class: peptidoglycan
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_1635957,IEDB_885814

• Article ID: 2538
  Johannsen L, Rosenthal RS, MArtin SA, Cady AB, Obal F (Jr), Guinand M, Krueger JM "Somnogenic activity of O-acetylated and dimeric muramyl peptides" - Infection and Immunity 57 (1989) 2726-2732
  

  Slow-wave sleep-promoting factors in brain and urine were identified as muramyl peptides (MPs), the building blocks of bacterial cell wall peptidoglycan. In this study, structural variations of MPs that occur naturally in bacterial peptidoglycan were investigated for somnogenic activity. Monomeric and dimeric MPs were isolated and purified from Neisseria gonorrhoeae and Actinomadura sp. strain R39. The structures of these MPs were verified by fast atom bombardment mass spectroscopy and tandem mass spectroscopy. After intracerebroventricular administration of MPs, electroencephalograms and brain temperatures of rabbits were recorded for 6 h and were analyzed to determine durations of slow-wave sleep, rapid-eye-movement sleep, and wakefulness. The 6-O acetylation of muramic acid enhanced the somnogenic effects of certain monomeric MPs relative to their non-O-acetylated (but otherwise identical) counterparts. Two monomeric MPs containing an unsubstituted amide (i.e., Iso-Gln) were inactive, thus confirming previous results showing that amidation of a variety of MPs can block somnogenic activity. Two peptide-cross-linked MP dimers tested had no effect on slow-wave sleep, although a third peptide-cross-linked MP containing a 1,6-anhydro muramyl end on one of its monomeric subunits, a structure that enhances somnogenic potency of un-cross-linked monomers, was somnogenic. Two dimers connected by glycosidic bonds and containing an Iso-Gln moiety were inactive. Two other glycosidically linked dimers that also contained an Iso-Gln moiety, but were of lower molecular weight, were somnogenic. In summary, 6-O acetylation of muramic acid in somnogenic MPs enhances activity, and as a class, peptide-linked dimeric MPs tend to be less active than their constituent monomers.

  NCBI PubMed ID: 2759708
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Institutions: Department of Physiology and Biophysics, University of Tennessee, Memphis 38163
  Methods: FAB-MS, MS/MS, biological assays, HPLC
  
   
  
  Neisseria gonorrhoeae
  CSDB ID 130246 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: muramyl peptide
Compound class: peptidoglycan
Contained glycoepitopes: IEDB_135813,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_1635957,IEDB_241115,IEDB_423183,IEDB_885814

• Article ID: 2594
  Kohlrausch U, Holtje JV "Analysis of murein and murein precursors during antibiotic-induced lysis of Escherichia coli" - Journal of Bacteriology 173 (1991) 3425-3431
  

  Lysis of Escherichia coli induced by either D-cycloserine, moenomycin, or penicillin G was monitored by studying murein metabolism. The levels of the soluble murein precursor UDP-N-acetylmuramyl-L-alanyl-D-glutamyl-m-diaminopimelyl-D-alanyl- D-alanine (UDP-MurNAc-pentapeptide) and the carrier-linked MurNAc-(pentapeptide)-pyrophosphoryl-undecaprenol as well as N-acetylglucosamine-β-1,4-MurNAc-(pentapeptide)-pyrophosphoryl- undecaprenol varied in a specific way. In the presence of penicillin, which is known to interfere with the cross-linking of murein, the concentration of the lipid-linked precursors unexpectedly decreased before the onset of lysis, although the level of UDP-MurNAc-pentapeptide remained normal. In the case of moenomycin, which specifically blocks the formation of the murein polysaccharide strands, the lipid-linked precursors as well as UDP-MurNAc-pentapeptide accumulated as was expected. D-Cycloserine, which inhibits the biosynthesis of UDP-MurNAc-pentapeptide, consequently caused a decrease in all three precursors. The muropeptide composition of the murein showed general changes such as an increase in the unusual DL-cross bridge between two neighboring meso-diaminopimelic acid residues and, as a result of uncontrolled DL- and DD-carboxypeptidase activity, an increase in tripeptidyl and a decrease in tetrapeptidyl and pentapeptidyl moieties. The average length of the glycan strands decreased. When the glycan strands were fractionated according to length, a dramatic increase in the amount of single disaccharide units was observed not only in the presence of penicillin but also in the presence of moenomycin. This result is explained by the action of an exo-muramidase, such as the lytic transglycosylases present in E. coli. It is proposed that antibiotic-induced bacteriolysis is the result of a zipperlike splitting of the murein net by exo-muramidases locally restricted to the equatorial zone of the cell.

  NCBI PubMed ID: 2045364
  Journal NLM ID: 2985120R
  Publisher: American Society for Microbiology
  Institutions: Abteilung Biochemie, Max-Planck-Institut für Entwicklungsbiologie, Munich, Germany
  
   
  
  Escherichia coli W7
  CSDB ID 131775 (all data & tools)