Show legend Show as text

Structure type: oligomer
Compound class: lipid A
Contained glycoepitopes: IEDB_135394,IEDB_135515,IEDB_141807,IEDB_151531,IEDB_176772

• Article ID: 37
  Caroff M, Karibian D "Structure of bacterial lipopolysaccharides" - Carbohydrate Research 338(23) (2003) 2431-2447
  

  Bacterial lipopolysaccharides are the major components of the outer surface of Gram-negative bacteria They are often of interest in medicine for their immunomodulatory properties. In small amounts they can be beneficial, but in larger amounts they may cause endotoxic shock. Although they share a common architecture, their structural details exert a strong influence on their activity. These molecules comprise: a lipid moiety, called lipid A, which is considered to be the endotoxic component, a glycosidic part consisting of a core of approximately 10 monosaccharides and, in 'smooth-type' lipopolysaccharides, a third region, named O-chain, consisting of repetitive subunits of one to eight monosaccharides responsible for much of the immunospecificity of the bacterial cell.

  Lipopolysaccharide, structure, core, lipid A, endotoxin, O-chains

  NCBI PubMed ID: 14670707
  Publication DOI: 10.1016/j.carres.2003.07.010
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: martine.carloff@bbmpc.u-psud.fr
  Institutions: Equipe Endotoxines, UMR 8619 du Centre National de la Recherche Scientifique, IBBMC, Université de Paris-Sud, F-Orsay, France
  
   
  
  Burkholderia caryophylli
  CSDB ID 31474 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: lipid A
Contained glycoepitopes: IEDB_135394,IEDB_135515,IEDB_141181,IEDB_141807,IEDB_151531

• Article ID: 37
  Caroff M, Karibian D "Structure of bacterial lipopolysaccharides" - Carbohydrate Research 338(23) (2003) 2431-2447
  

  Bacterial lipopolysaccharides are the major components of the outer surface of Gram-negative bacteria They are often of interest in medicine for their immunomodulatory properties. In small amounts they can be beneficial, but in larger amounts they may cause endotoxic shock. Although they share a common architecture, their structural details exert a strong influence on their activity. These molecules comprise: a lipid moiety, called lipid A, which is considered to be the endotoxic component, a glycosidic part consisting of a core of approximately 10 monosaccharides and, in 'smooth-type' lipopolysaccharides, a third region, named O-chain, consisting of repetitive subunits of one to eight monosaccharides responsible for much of the immunospecificity of the bacterial cell.

  Lipopolysaccharide, structure, core, lipid A, endotoxin, O-chains

  NCBI PubMed ID: 14670707
  Publication DOI: 10.1016/j.carres.2003.07.010
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: martine.carloff@bbmpc.u-psud.fr
  Institutions: Equipe Endotoxines, UMR 8619 du Centre National de la Recherche Scientifique, IBBMC, Université de Paris-Sud, F-Orsay, France
  
   
  
  Yersinia pseudotuberculosis
  CSDB ID 31476 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: lipid A

• Article ID: 119
  Trent MS, Ribeiro AA, Doerrler WT, Lin S, Cotter RJ, Raetz CRH "Accumulation of a polyisoprene-linked amino sugar in polymyxin resistant Salmonella typhimurium and Escherichia coli. Structural characterization and transfer to lipid A in the periplasm" - Journal of Biological Chemistry 276(46) (2001) 43132-43144
  

  Polymyxin-resistant mutants of Escherichia coli and Salmonella typhimurium accumulate a novel minor lipid that can donate 4-amino-4-deoxy-l-arabinose units (l-Ara4N) to lipid A. We now report the purification of this lipid from a pss(-) pmrA(C) mutant of E. coli and assign its structure as undecaprenyl phosphate-α-L-Ara4N. Approximately 0.2 mg of homogeneous material was isolated from an 8-liter culture by solvent extraction, followed by chromatography on DEAE-cellulose, C18 reverse phase resin, and silicic acid. Matrix-assisted laser desorption ionization/time of flight mass spectrometry in the negative mode yielded a single species [M - H](-) at m/z 977.5, consistent with undecaprenyl phosphate-α-L-Ara4N (M(r) = 978.41). (31)P NMR spectroscopy showed a single phosphorus atom at -0.44 ppm characteristic of a phosphodiester linkage. Selective inverse decoupling difference spectroscopy demonstrated that the undecaprenyl phosphate group is attached to the anomeric carbon of the l-Ara4N unit. One- and two-dimensional (1)H NMR studies confirmed the presence of a polyisoprene chain and a sugar moiety with chemical shifts and coupling constants expected for an equatorially substituted arabinopyranoside. Heteronuclear multiple-quantum coherence spectroscopy analysis demonstrated that a nitrogen atom is attached to C-4 of the sugar residue. The purified donor supports in vitro conversion of lipid IV(A) to lipid II(A), which is substituted with a single l-Ara4N moiety. The identification of undecaprenyl phosphate-α-L-Ara4N implies that l-Ara4N transfer to lipid A occurs in the periplasm of polymyxin-resistant strains, and establishes a new enzymatic pathway by which Gram-negative bacteria acquire antibiotic resistance.

  Escherichia coli, lipid A, polymyxin-resistant mutants, Salmonella typhimurium

  NCBI PubMed ID: 11535605
  Publication DOI: 10.1074/jbc.M106962200
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: raetz@biochem.duke.edu
  Institutions: Department of Biochemistry and the Duke NMR Spectroscopy Center and Department of Radiology, Duke University Medical Center, Durham, North Carolina 27710, Middle Atlantic Mass Spectrometry Laboratory, Department of Pharmacology and Molecular Sciences, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205-2185, USA
  Methods: 13C NMR, 1H NMR, NMR-2D, DNA techniques, TLC, 31P NMR, MALDI-TOF MS, radiolabeling, NMR-1D, genetic methods, biochemical methods, radioactivity measurement
  
   
  
  Salmonella typhimurium, Escherichia coli
  CSDB ID 5231 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure
Compound class: lipid A
Contained glycoepitopes: IEDB_135394,IEDB_135515,IEDB_141807,IEDB_151531,IEDB_176772,IEDB_534864

• Article ID: 119
  Trent MS, Ribeiro AA, Doerrler WT, Lin S, Cotter RJ, Raetz CRH "Accumulation of a polyisoprene-linked amino sugar in polymyxin resistant Salmonella typhimurium and Escherichia coli. Structural characterization and transfer to lipid A in the periplasm" - Journal of Biological Chemistry 276(46) (2001) 43132-43144
  

  Polymyxin-resistant mutants of Escherichia coli and Salmonella typhimurium accumulate a novel minor lipid that can donate 4-amino-4-deoxy-l-arabinose units (l-Ara4N) to lipid A. We now report the purification of this lipid from a pss(-) pmrA(C) mutant of E. coli and assign its structure as undecaprenyl phosphate-α-L-Ara4N. Approximately 0.2 mg of homogeneous material was isolated from an 8-liter culture by solvent extraction, followed by chromatography on DEAE-cellulose, C18 reverse phase resin, and silicic acid. Matrix-assisted laser desorption ionization/time of flight mass spectrometry in the negative mode yielded a single species [M - H](-) at m/z 977.5, consistent with undecaprenyl phosphate-α-L-Ara4N (M(r) = 978.41). (31)P NMR spectroscopy showed a single phosphorus atom at -0.44 ppm characteristic of a phosphodiester linkage. Selective inverse decoupling difference spectroscopy demonstrated that the undecaprenyl phosphate group is attached to the anomeric carbon of the l-Ara4N unit. One- and two-dimensional (1)H NMR studies confirmed the presence of a polyisoprene chain and a sugar moiety with chemical shifts and coupling constants expected for an equatorially substituted arabinopyranoside. Heteronuclear multiple-quantum coherence spectroscopy analysis demonstrated that a nitrogen atom is attached to C-4 of the sugar residue. The purified donor supports in vitro conversion of lipid IV(A) to lipid II(A), which is substituted with a single l-Ara4N moiety. The identification of undecaprenyl phosphate-α-L-Ara4N implies that l-Ara4N transfer to lipid A occurs in the periplasm of polymyxin-resistant strains, and establishes a new enzymatic pathway by which Gram-negative bacteria acquire antibiotic resistance.

  Escherichia coli, lipid A, polymyxin-resistant mutants, Salmonella typhimurium

  NCBI PubMed ID: 11535605
  Publication DOI: 10.1074/jbc.M106962200
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: raetz@biochem.duke.edu
  Institutions: Department of Biochemistry and the Duke NMR Spectroscopy Center and Department of Radiology, Duke University Medical Center, Durham, North Carolina 27710, Middle Atlantic Mass Spectrometry Laboratory, Department of Pharmacology and Molecular Sciences, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205-2185, USA
  Methods: 13C NMR, 1H NMR, NMR-2D, DNA techniques, TLC, 31P NMR, MALDI-TOF MS, radiolabeling, NMR-1D, genetic methods, biochemical methods, radioactivity measurement
  
   
  
  Salmonella typhimurium, Escherichia coli
  CSDB ID 31381 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: lipid A
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130659,IEDB_135394,IEDB_135515,IEDB_141181,IEDB_141807,IEDB_150908,IEDB_151531,IEDB_176772,IEDB_534864

• Article ID: 120
  Trent MS, Ribeiro AA, Lin S, Cotter RJ, Raetz CR "An inner membrane enzyme in Salmonella and Escherichia coli that transfers 4-amino-4-deoxy-L-arabinose to lipid A. Induction in polymyxin-resistant mutants and role of a novel lipid-linked donor" - Journal of Biological Chemistry 276(46) (2001) 43122-43131
  

  Attachment of the cationic sugar 4-amino-4-deoxy-l-arabinose (l-Ara4N) to lipid A is required for the maintenance of polymyxin resistance in Escherichia coli and Salmonella typhimurium. The enzymes that synthesize l-Ara4N and transfer it to lipid A have not been identified. We now report an inner membrane enzyme, expressed in polymyxin-resistant mutants, that adds one or two l-Ara4N moieties to lipid A or its immediate precursors. No soluble factors are required. A gene located near minute 51 on the S. typhimurium and E. coli chromosomes (previously termed orf5, pmrK, or yfbI) encodes the l-Ara4N transferase. The enzyme, renamed ArnT, consists of 548 amino acid residues in S. typhimurium with 12 possible membrane-spanning regions. ArnT displays distant similarity to yeast protein mannosyltransferases. ArnT adds two l-Ara4N units to lipid A precursors containing a Kdo disaccharide. However, as shown by mass spectrometry and NMR spectroscopy, it transfers only a single l-Ara4N residue to the 1-phosphate moiety of lipid IV(A), a precursor lacking Kdo. Proteins with full-length sequence similarity to ArnT are present in genomes of other bacteria thought to synthesize l-Ara4N-modified lipid A, including Pseudomonas aeruginosa and Yersinia pestis. As shown in the following article (Trent, M. S., Ribeiro, A. A., Doerrler, W. T., Lin, S., Cotter, R. J., and Raetz, C. R. H. (2001) J. Biol. Chem. 276, 43132-43144), ArnT utilizes the novel lipid undecaprenyl phosphate-α-l-Ara4N as its sugar donor, suggesting that l-Ara4N transfer to lipid A occurs on the periplasmic side of the inner membrane.

  Escherichia coli, acid, lipid A, NMR spectroscopy, MALDI, Salmonella typhimurium, 4-amino-4-deoxy-L-arabinose

  NCBI PubMed ID: 11535604
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: raetz@biochem.duke.edu
  Institutions: Department of Biochemistry, Duke NMR Spectroscopy Center, Duke University Medical Center, Durham, North Carolina 27710, USA
  Methods: 1H NMR, DNA techniques, kinetics assays, TLC, 31P NMR, MALDI-MS, radiolabeling, genetic methods, biochemical methods, radioactivity measurement
  
   
  
  Salmonella typhimurium
  CSDB ID 5232 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: lipid A
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130659,IEDB_141181,IEDB_141807,IEDB_151531,IEDB_176772,IEDB_534864

• Article ID: 120
  Trent MS, Ribeiro AA, Lin S, Cotter RJ, Raetz CR "An inner membrane enzyme in Salmonella and Escherichia coli that transfers 4-amino-4-deoxy-L-arabinose to lipid A. Induction in polymyxin-resistant mutants and role of a novel lipid-linked donor" - Journal of Biological Chemistry 276(46) (2001) 43122-43131
  

  Attachment of the cationic sugar 4-amino-4-deoxy-l-arabinose (l-Ara4N) to lipid A is required for the maintenance of polymyxin resistance in Escherichia coli and Salmonella typhimurium. The enzymes that synthesize l-Ara4N and transfer it to lipid A have not been identified. We now report an inner membrane enzyme, expressed in polymyxin-resistant mutants, that adds one or two l-Ara4N moieties to lipid A or its immediate precursors. No soluble factors are required. A gene located near minute 51 on the S. typhimurium and E. coli chromosomes (previously termed orf5, pmrK, or yfbI) encodes the l-Ara4N transferase. The enzyme, renamed ArnT, consists of 548 amino acid residues in S. typhimurium with 12 possible membrane-spanning regions. ArnT displays distant similarity to yeast protein mannosyltransferases. ArnT adds two l-Ara4N units to lipid A precursors containing a Kdo disaccharide. However, as shown by mass spectrometry and NMR spectroscopy, it transfers only a single l-Ara4N residue to the 1-phosphate moiety of lipid IV(A), a precursor lacking Kdo. Proteins with full-length sequence similarity to ArnT are present in genomes of other bacteria thought to synthesize l-Ara4N-modified lipid A, including Pseudomonas aeruginosa and Yersinia pestis. As shown in the following article (Trent, M. S., Ribeiro, A. A., Doerrler, W. T., Lin, S., Cotter, R. J., and Raetz, C. R. H. (2001) J. Biol. Chem. 276, 43132-43144), ArnT utilizes the novel lipid undecaprenyl phosphate-α-l-Ara4N as its sugar donor, suggesting that l-Ara4N transfer to lipid A occurs on the periplasmic side of the inner membrane.

  Escherichia coli, acid, lipid A, NMR spectroscopy, MALDI, Salmonella typhimurium, 4-amino-4-deoxy-L-arabinose

  NCBI PubMed ID: 11535604
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: raetz@biochem.duke.edu
  Institutions: Department of Biochemistry, Duke NMR Spectroscopy Center, Duke University Medical Center, Durham, North Carolina 27710, USA
  Methods: 1H NMR, DNA techniques, kinetics assays, TLC, 31P NMR, MALDI-MS, radiolabeling, genetic methods, biochemical methods, radioactivity measurement
  
   
  
  Salmonella typhimurium
  CSDB ID 31376 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: lipid A
Contained glycoepitopes: IEDB_135394,IEDB_135515,IEDB_141807,IEDB_151531

• Article ID: 120
  Trent MS, Ribeiro AA, Lin S, Cotter RJ, Raetz CR "An inner membrane enzyme in Salmonella and Escherichia coli that transfers 4-amino-4-deoxy-L-arabinose to lipid A. Induction in polymyxin-resistant mutants and role of a novel lipid-linked donor" - Journal of Biological Chemistry 276(46) (2001) 43122-43131
  

  Attachment of the cationic sugar 4-amino-4-deoxy-l-arabinose (l-Ara4N) to lipid A is required for the maintenance of polymyxin resistance in Escherichia coli and Salmonella typhimurium. The enzymes that synthesize l-Ara4N and transfer it to lipid A have not been identified. We now report an inner membrane enzyme, expressed in polymyxin-resistant mutants, that adds one or two l-Ara4N moieties to lipid A or its immediate precursors. No soluble factors are required. A gene located near minute 51 on the S. typhimurium and E. coli chromosomes (previously termed orf5, pmrK, or yfbI) encodes the l-Ara4N transferase. The enzyme, renamed ArnT, consists of 548 amino acid residues in S. typhimurium with 12 possible membrane-spanning regions. ArnT displays distant similarity to yeast protein mannosyltransferases. ArnT adds two l-Ara4N units to lipid A precursors containing a Kdo disaccharide. However, as shown by mass spectrometry and NMR spectroscopy, it transfers only a single l-Ara4N residue to the 1-phosphate moiety of lipid IV(A), a precursor lacking Kdo. Proteins with full-length sequence similarity to ArnT are present in genomes of other bacteria thought to synthesize l-Ara4N-modified lipid A, including Pseudomonas aeruginosa and Yersinia pestis. As shown in the following article (Trent, M. S., Ribeiro, A. A., Doerrler, W. T., Lin, S., Cotter, R. J., and Raetz, C. R. H. (2001) J. Biol. Chem. 276, 43132-43144), ArnT utilizes the novel lipid undecaprenyl phosphate-α-l-Ara4N as its sugar donor, suggesting that l-Ara4N transfer to lipid A occurs on the periplasmic side of the inner membrane.

  Escherichia coli, acid, lipid A, NMR spectroscopy, MALDI, Salmonella typhimurium, 4-amino-4-deoxy-L-arabinose

  NCBI PubMed ID: 11535604
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: raetz@biochem.duke.edu
  Institutions: Department of Biochemistry, Duke NMR Spectroscopy Center, Duke University Medical Center, Durham, North Carolina 27710, USA
  Methods: 1H NMR, DNA techniques, kinetics assays, TLC, 31P NMR, MALDI-MS, radiolabeling, genetic methods, biochemical methods, radioactivity measurement
  
   
  
  Salmonella typhimurium
  CSDB ID 31378 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: lipid A
Contained glycoepitopes: IEDB_135394,IEDB_135515,IEDB_141181,IEDB_141807,IEDB_151531

• Article ID: 120
  Trent MS, Ribeiro AA, Lin S, Cotter RJ, Raetz CR "An inner membrane enzyme in Salmonella and Escherichia coli that transfers 4-amino-4-deoxy-L-arabinose to lipid A. Induction in polymyxin-resistant mutants and role of a novel lipid-linked donor" - Journal of Biological Chemistry 276(46) (2001) 43122-43131
  

  Attachment of the cationic sugar 4-amino-4-deoxy-l-arabinose (l-Ara4N) to lipid A is required for the maintenance of polymyxin resistance in Escherichia coli and Salmonella typhimurium. The enzymes that synthesize l-Ara4N and transfer it to lipid A have not been identified. We now report an inner membrane enzyme, expressed in polymyxin-resistant mutants, that adds one or two l-Ara4N moieties to lipid A or its immediate precursors. No soluble factors are required. A gene located near minute 51 on the S. typhimurium and E. coli chromosomes (previously termed orf5, pmrK, or yfbI) encodes the l-Ara4N transferase. The enzyme, renamed ArnT, consists of 548 amino acid residues in S. typhimurium with 12 possible membrane-spanning regions. ArnT displays distant similarity to yeast protein mannosyltransferases. ArnT adds two l-Ara4N units to lipid A precursors containing a Kdo disaccharide. However, as shown by mass spectrometry and NMR spectroscopy, it transfers only a single l-Ara4N residue to the 1-phosphate moiety of lipid IV(A), a precursor lacking Kdo. Proteins with full-length sequence similarity to ArnT are present in genomes of other bacteria thought to synthesize l-Ara4N-modified lipid A, including Pseudomonas aeruginosa and Yersinia pestis. As shown in the following article (Trent, M. S., Ribeiro, A. A., Doerrler, W. T., Lin, S., Cotter, R. J., and Raetz, C. R. H. (2001) J. Biol. Chem. 276, 43132-43144), ArnT utilizes the novel lipid undecaprenyl phosphate-α-l-Ara4N as its sugar donor, suggesting that l-Ara4N transfer to lipid A occurs on the periplasmic side of the inner membrane.

  Escherichia coli, acid, lipid A, NMR spectroscopy, MALDI, Salmonella typhimurium, 4-amino-4-deoxy-L-arabinose

  NCBI PubMed ID: 11535604
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: raetz@biochem.duke.edu
  Institutions: Department of Biochemistry, Duke NMR Spectroscopy Center, Duke University Medical Center, Durham, North Carolina 27710, USA
  Methods: 1H NMR, DNA techniques, kinetics assays, TLC, 31P NMR, MALDI-MS, radiolabeling, genetic methods, biochemical methods, radioactivity measurement
  
   
  
  Salmonella typhimurium
  CSDB ID 31380 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: phosphate
Trivial name: core-lipid A backbone
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130659,IEDB_130670,IEDB_135394,IEDB_136044,IEDB_137472,IEDB_137473,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_150908,IEDB_151531,IEDB_190606,IEDB_2189046,IEDB_2189047,IEDB_226811,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_7,SB_88

• Article ID: 168
  Vinogradov E, Bock K "The structure of the core part of Proteus vulgaris OX2 lipopolysaccharide" - Carbohydrate Research 320(3-4) (1999) 239-243
  

  The identity of a novel structural component, an open-chain acetalic linkage, in the core part of the lipopolysac-charide (LPS) from Proteus vulgar is serotype OX2 has been determined by extensive NMR spectroscopic analysis of fragments isolated after mild acid hydrolysis of the intact LPS. The open-chain A^-acetylgalactosamine fragment is substituted in the 4-position by non-stoichiometric amounts of a p-galactopyranose residue and the overall structure of the core is as follows: [formula: see text]. All sugars except the TV-acetylgalactosamine are in the pyranose form, a-Hep refers to L-glycero-a-D-manno-heptopyranose and a-DDHep to D-glycero-a-D-manno-heptopyranose. Bold italics indicate non-stoichiometric substituents.

  Lipopolysaccharide, oligosaccharide, core, Proteus, Proteus vulgaris OX2, core structure

  NCBI PubMed ID: 10573861
  Publication DOI: 10.1016/S0008-6215(99)00181-0
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: kbo@crc.dk
  Institutions: Department of Chemistry, Carlsberg Laboratory, Gamle Carlsberg Vej 10, DK-2500 Valby, Copenhagen, Denmark
  Methods: NMR-2D, NMR
  
   
  
  Proteus vulgaris OX2
  CSDB ID 5298 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: phosphate
Trivial name: core-lipid A backbone
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130659,IEDB_130670,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137473,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_2189046,IEDB_2189047,IEDB_226811,IEDB_983931,SB_192,SB_7

• Article ID: 169
  Vinogradov E, Perry MB "Structural analysis of the core region of lipopolysaccharides from Proteus mirabilis serotypes O6, O48 and O57" - European Journal of Biochemistry 267(8) (2000) 2439-2446
  

  The structure of lipid A core region of the lipopolysaccharides (LPS) from Proteus mirabilis serotypes O6, O57 and O48 was determined using NMR, MS and chemical analysis of the oligosaccharides, obtained by mild acid hydrolysis, alkaline deacylation, and deamination of LPS: [see text for structure]. Incomplete substitutions are indicated by bold italic type. All sugars are present in pyranose form, α-Hep is the residue of L-glycero-α-D-manno-Hep, α-DD-Hep is the residue of D-glycero-α-D-manno-Hep, L-Ara4N is 4-amino-4-deoxy-L-arabinose, Qui4NAlaAla is the residue of 4-N-(L-alanyl-L-alanyl)-4-amino-4,6-dideoxyglucose. All sugars except L-Ara4N have D-configuration. β-GalA* is partially present in the form of amide with 1,4-diaminobutane (putrescine)-HN(CH2)4NH2 or spermidine-HN(CH2)3NH(CH2)4NH2.

  Lipopolysaccharide, lipopolysaccharides, LPS, core, structural, serotype, analysis, Proteus, Proteus mirabilis, structural analysis, core region, region, Serotypes

  NCBI PubMed ID: 10759870
  Publication DOI: 10.1046/j.1432-1327.2000.01262.x
  Journal NLM ID: 0107600
  Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
  Institutions: Institute for Biological Sciences, National Research Council, Ottawa, ON, Canada, Institute for Biological Sciences, National Research Council, Ottawa, ON, Canada.
  Methods: NMR-2D, NMR, mild acid hydrolysis, MS, alkaline deacylation, alkaline deamination
  
   
  
  Proteus mirabilis O6
  CSDB ID 5299 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: phosphate
Trivial name: core-lipid A backbone
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130659,IEDB_130670,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_151531,IEDB_2189046,IEDB_2189047,IEDB_226811,IEDB_983931,SB_192

• Article ID: 170
  Vinogradov E, Radziejewska-Lebrecht J, Kaca W "The structure of the carbohydrate backbone of core-lipid A region of the lipopolysaccharide from Proteus mirabilis wild-type strain S1959 (serotype O3) and its Ra mutant R110/1959" - European Journal of Biochemistry 267 (2000) 262-269
  

  The following structure of core-lipid A region of the lipopolysaccharide (LPS) from Proteus mirabilis strain 1959 (serotype O3) and its rough mutant Rl 10/1959 (Proteus type II core) was determined using NMR and chemical analysis of the core oligosaccharide, obtained by mild acid hydrolysis of LPS, and of the products of alkaline deacylation of the LPS: [formula: see text]. Incomplete substitutions are indicated by italics. All sugars are in pyranose form, a-Hep is the residue L-glycero-a-D-manno-Hep, a-DD-Hep is the residue D-gfycero-a-D-manno-Hep. The differences with the previously reported structures are discussed.

  Lipopolysaccharide, structure, strain, serotype, Proteus, Proteus mirabilis, structural analysis, region, core-lipid A region

  NCBI PubMed ID: 10601875
  Journal NLM ID: 0107600
  Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
  Correspondence: evv@crc.dk
  Institutions: Department of Chemistry, Carlsberg Laboratory, Copenhagen, Denmark, Department of Microbiology, University of Silesia, Katowice, Poland, Center of Microbiology and Virology, Polish Academy of Science, Lodz, Poland
  Methods: NMR-2D, NMR, ESI-MS, mild acid hydrolysis, deamination, de-N-O-acetylation
  
   
  
  Proteus mirabilis S1959
  CSDB ID 5300 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: core oligosaccharide, LPS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130670,IEDB_136044,IEDB_137472,IEDB_137473,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141794,IEDB_142488,IEDB_146664,IEDB_190606,IEDB_2189046,IEDB_2189047,IEDB_226811,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_7,SB_88

• Article ID: 168
  Vinogradov E, Bock K "The structure of the core part of Proteus vulgaris OX2 lipopolysaccharide" - Carbohydrate Research 320(3-4) (1999) 239-243
  

  The identity of a novel structural component, an open-chain acetalic linkage, in the core part of the lipopolysac-charide (LPS) from Proteus vulgar is serotype OX2 has been determined by extensive NMR spectroscopic analysis of fragments isolated after mild acid hydrolysis of the intact LPS. The open-chain A^-acetylgalactosamine fragment is substituted in the 4-position by non-stoichiometric amounts of a p-galactopyranose residue and the overall structure of the core is as follows: [formula: see text]. All sugars except the TV-acetylgalactosamine are in the pyranose form, a-Hep refers to L-glycero-a-D-manno-heptopyranose and a-DDHep to D-glycero-a-D-manno-heptopyranose. Bold italics indicate non-stoichiometric substituents.

  Lipopolysaccharide, oligosaccharide, core, Proteus, Proteus vulgaris OX2, core structure

  NCBI PubMed ID: 10573861
  Publication DOI: 10.1016/S0008-6215(99)00181-0
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: kbo@crc.dk
  Institutions: Department of Chemistry, Carlsberg Laboratory, Gamle Carlsberg Vej 10, DK-2500 Valby, Copenhagen, Denmark
  Methods: NMR-2D, NMR
  
   
  
  Proteus vulgaris OX2
  CSDB ID 5329 (all data & tools)
• Article ID: 178
  Vinogradov E, Sidorczyk Z "The structure of the carbohydrate backbone of the core-lipid A region of the lipopolysaccharide from Proteus penneri strain 40: new Proteus strains containing open-chain acetal-linked N-acetylgalactosamine in the core part of the LPS" - Carbohydrate Research 330(3) (2001) 537-540
  

  Analysis of the core part of the LPS from several strains of Proteus revealed that P. penneri strains 2, 11, 19, 107, and P. vulgaris serotypes 04 and 08 have the same structure with a new type of linkage between monosaccharidesan open-chain acetal--that was previously determined for P. vulgaris OX2 and P. penneri 17. The LPS from P. penneri strain 40 contains the same structure substituted with one additional monosaccharide: [molecular structure: see text] where (1S)-GalaNAc1 is a residue of N-acetyl-D-galactosamine in the open-chain form. It is connected as a cyclic acetal to positions 4 and 6 of the galactosamine residue having a free amino group. All other sugars are in the pyranose form.

  Lipopolysaccharide, LPS, structure, core, strain, carbohydrate, Proteus, Proteus penneri, region, backbone, N-acetylgalactosamine, open-chain

  NCBI PubMed ID: 11269407
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: evguenii.vinogradov@nrc.ca
  Institutions: Institute for Biological Sciences, National Research Council, 100 Sussex Drive, Ottawa, Ont., Canada K 1A 0R 6, Institute of Microbiology and Immunology, University of Lodz, 90- 237 Lodz, Banacha 12: 16, Poland
  Methods: NMR-2D, NMR, chemical methods
  
   
  
  Proteus vulgaris OX2, Proteus vulgaris O4, Proteus vulgaris O8, Proteus penneri 2, Proteus penneri 11, Proteus penneri 17, Proteus penneri 19, Proteus penneri 107
  CSDB ID 5622 (all data & tools)
• Article ID: 892
  Kondakova AN, Vinogradov EV, Lindner B, Knirel YA, Amano K "Structural studies on the lipopolysaccharide core of Proteus OX strains used in Weil-Felix test: a mass spectrometric approach" - Carbohydrate Research 338(23) (2003) 2697-2709
  

  The core region of the lipopolysaccharides of Proteus group OX bacteria, which are used as antigens in Weil-Felix test for serodiagnosis of rickettsiosis, were studied by chemical degradations in combination with ESI FTMS, including infrared multi-photon dissociation (IRMPD) MS/MS and capillary skimmer dissociation. Structural variants of the inner core region were found to be the same as in Proteus non-OX strains that have been studied earlier. The outer core region has essentially the same structure in Proteus vulgaris OX19 (serogroup O1) and OX2 (serogroup O2) and a different structure in Proteus mirabilis OXK (serogroup O3). A fragmentation due to the rupture of the linkage between GlcN or GalN and GalA was observed in IRMPD-MS/MS of core oligosaccharides and found to be useful for screening of Proteus strains to assign structures of the relatively conserved inner core region and to select for further studies strains with distinct structures of a more variable outer core region.

  Lipopolysaccharide, core structures, Weil-Felix test, ESI FT-MS, IRMPD-MS/MS, Proteus OX

  Publication DOI: 10.1016/S0008-6215(03)00383-5
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: knirel@ioc.ac.ru
  Institutions: N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russian Federation, Research Center Borstel, Center for Medicine and Biosciences, 23845 Borstel, Germany, Institute for Biological Sciences, National Research Council, Ottawa ON, Canada K1A 0R6, Central Research Laboratory, Akita University, School of Medicine, 1-1-1 Hondo, Akita 010, Japan
  Methods: NMR, MS, deamination
  
   
  
  Proteus vulgaris OX19 (O1), Proteus vulgaris OX2 (O2)
  CSDB ID 2858 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: core oligosaccharide, LPS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130670,IEDB_137473,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_142488,IEDB_146664,IEDB_2189046,IEDB_2189047,IEDB_226811,IEDB_983931,SB_192

• Article ID: 168
  Vinogradov E, Bock K "The structure of the core part of Proteus vulgaris OX2 lipopolysaccharide" - Carbohydrate Research 320(3-4) (1999) 239-243
  

  The identity of a novel structural component, an open-chain acetalic linkage, in the core part of the lipopolysac-charide (LPS) from Proteus vulgar is serotype OX2 has been determined by extensive NMR spectroscopic analysis of fragments isolated after mild acid hydrolysis of the intact LPS. The open-chain A^-acetylgalactosamine fragment is substituted in the 4-position by non-stoichiometric amounts of a p-galactopyranose residue and the overall structure of the core is as follows: [formula: see text]. All sugars except the TV-acetylgalactosamine are in the pyranose form, a-Hep refers to L-glycero-a-D-manno-heptopyranose and a-DDHep to D-glycero-a-D-manno-heptopyranose. Bold italics indicate non-stoichiometric substituents.

  Lipopolysaccharide, oligosaccharide, core, Proteus, Proteus vulgaris OX2, core structure

  NCBI PubMed ID: 10573861
  Publication DOI: 10.1016/S0008-6215(99)00181-0
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: kbo@crc.dk
  Institutions: Department of Chemistry, Carlsberg Laboratory, Gamle Carlsberg Vej 10, DK-2500 Valby, Copenhagen, Denmark
  Methods: NMR-2D, NMR
  
   
  
  Proteus vulgaris OX2
  CSDB ID 5330 (all data & tools)
• Article ID: 892
  Kondakova AN, Vinogradov EV, Lindner B, Knirel YA, Amano K "Structural studies on the lipopolysaccharide core of Proteus OX strains used in Weil-Felix test: a mass spectrometric approach" - Carbohydrate Research 338(23) (2003) 2697-2709
  

  The core region of the lipopolysaccharides of Proteus group OX bacteria, which are used as antigens in Weil-Felix test for serodiagnosis of rickettsiosis, were studied by chemical degradations in combination with ESI FTMS, including infrared multi-photon dissociation (IRMPD) MS/MS and capillary skimmer dissociation. Structural variants of the inner core region were found to be the same as in Proteus non-OX strains that have been studied earlier. The outer core region has essentially the same structure in Proteus vulgaris OX19 (serogroup O1) and OX2 (serogroup O2) and a different structure in Proteus mirabilis OXK (serogroup O3). A fragmentation due to the rupture of the linkage between GlcN or GalN and GalA was observed in IRMPD-MS/MS of core oligosaccharides and found to be useful for screening of Proteus strains to assign structures of the relatively conserved inner core region and to select for further studies strains with distinct structures of a more variable outer core region.

  Lipopolysaccharide, core structures, Weil-Felix test, ESI FT-MS, IRMPD-MS/MS, Proteus OX

  Publication DOI: 10.1016/S0008-6215(03)00383-5
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: knirel@ioc.ac.ru
  Institutions: N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russian Federation, Research Center Borstel, Center for Medicine and Biosciences, 23845 Borstel, Germany, Institute for Biological Sciences, National Research Council, Ottawa ON, Canada K1A 0R6, Central Research Laboratory, Akita University, School of Medicine, 1-1-1 Hondo, Akita 010, Japan
  Methods: NMR, MS, deamination
  
   
  
  Proteus vulgaris OX19 (O1), Proteus vulgaris OX2 (O2)
  CSDB ID 3040 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: phosphate
Compound class: LPS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130659,IEDB_130670,IEDB_135394,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_150908,IEDB_151531,IEDB_2189046,IEDB_2189047,IEDB_226811,IEDB_983931,SB_192

• Article ID: 168
  Vinogradov E, Bock K "The structure of the core part of Proteus vulgaris OX2 lipopolysaccharide" - Carbohydrate Research 320(3-4) (1999) 239-243
  

  The identity of a novel structural component, an open-chain acetalic linkage, in the core part of the lipopolysac-charide (LPS) from Proteus vulgar is serotype OX2 has been determined by extensive NMR spectroscopic analysis of fragments isolated after mild acid hydrolysis of the intact LPS. The open-chain A^-acetylgalactosamine fragment is substituted in the 4-position by non-stoichiometric amounts of a p-galactopyranose residue and the overall structure of the core is as follows: [formula: see text]. All sugars except the TV-acetylgalactosamine are in the pyranose form, a-Hep refers to L-glycero-a-D-manno-heptopyranose and a-DDHep to D-glycero-a-D-manno-heptopyranose. Bold italics indicate non-stoichiometric substituents.

  Lipopolysaccharide, oligosaccharide, core, Proteus, Proteus vulgaris OX2, core structure

  NCBI PubMed ID: 10573861
  Publication DOI: 10.1016/S0008-6215(99)00181-0
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: kbo@crc.dk
  Institutions: Department of Chemistry, Carlsberg Laboratory, Gamle Carlsberg Vej 10, DK-2500 Valby, Copenhagen, Denmark
  Methods: NMR-2D, NMR
  
   
  
  Proteus vulgaris OX2
  CSDB ID 5332 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: phosphate
Trivial name: core-lipid A backbone
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130648,IEDB_130650,IEDB_130659,IEDB_130670,IEDB_137473,IEDB_1391961,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141584,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151531,IEDB_2189046,IEDB_2189047,IEDB_226811,IEDB_885822,IEDB_983931,SB_192

• Article ID: 169
  Vinogradov E, Perry MB "Structural analysis of the core region of lipopolysaccharides from Proteus mirabilis serotypes O6, O48 and O57" - European Journal of Biochemistry 267(8) (2000) 2439-2446
  

  The structure of lipid A core region of the lipopolysaccharides (LPS) from Proteus mirabilis serotypes O6, O57 and O48 was determined using NMR, MS and chemical analysis of the oligosaccharides, obtained by mild acid hydrolysis, alkaline deacylation, and deamination of LPS: [see text for structure]. Incomplete substitutions are indicated by bold italic type. All sugars are present in pyranose form, α-Hep is the residue of L-glycero-α-D-manno-Hep, α-DD-Hep is the residue of D-glycero-α-D-manno-Hep, L-Ara4N is 4-amino-4-deoxy-L-arabinose, Qui4NAlaAla is the residue of 4-N-(L-alanyl-L-alanyl)-4-amino-4,6-dideoxyglucose. All sugars except L-Ara4N have D-configuration. β-GalA* is partially present in the form of amide with 1,4-diaminobutane (putrescine)-HN(CH2)4NH2 or spermidine-HN(CH2)3NH(CH2)4NH2.

  Lipopolysaccharide, lipopolysaccharides, LPS, core, structural, serotype, analysis, Proteus, Proteus mirabilis, structural analysis, core region, region, Serotypes

  NCBI PubMed ID: 10759870
  Publication DOI: 10.1046/j.1432-1327.2000.01262.x
  Journal NLM ID: 0107600
  Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
  Institutions: Institute for Biological Sciences, National Research Council, Ottawa, ON, Canada, Institute for Biological Sciences, National Research Council, Ottawa, ON, Canada.
  Methods: NMR-2D, NMR, mild acid hydrolysis, MS, alkaline deacylation, alkaline deamination
  
   
  
  Proteus mirabilis O57
  CSDB ID 5360 (all data & tools)