Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Trivial name: lipooligosaccharide core L1
Compound class: core oligosaccharide, LOS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130651,IEDB_136044,IEDB_136906,IEDB_137472,IEDB_1391964,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_144987,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_152217,IEDB_190606,IEDB_2189047,IEDB_418765,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_423106,IEDB_742247,IEDB_983931,SB_165,SB_166,SB_167,SB_178,SB_187,SB_192,SB_195,SB_31,SB_6,SB_62,SB_7,SB_88

• Article ID: 7
  Berrington AW, Tan YC, Srikhanta Y, Kuipers B, van der LP, Peak IR, Jennings MP "Phase variation in meningococcal lipooligosaccharide biosynthesis genes" - FEMS Immunology and Medical Microbiology 34(4) (2002) 267-275
  

  Neisseria meningitidis expresses a range of lipooligosaccharide (LOS) structures, comprising of at least 13 immunotypes (ITs). Meningococcal LOS is subject to phase variation of its terminal structures allowing switching between ITs, which is proposed to have functional significance in disease. The objectives of this study were to investigate the repertoire of structures that can be expressed in clinical isolates, and to examine the role of phase-variable expression of LOS genes during invasive disease. Southern blotting was used to detect the presence of LOS biosynthetic genes in two collections of meningococci, a global set of strains previously assigned to lineages of greater or lesser virulence, and a collection of local clinical isolates which included paired throat and blood isolates from individual patients. Where the phase-variable genes lgtA, lgtC or lgtG were identified, they were amplified by PCR and the homopolymeric tracts, responsible for their phase-variable expression, were sequenced. The results revealed great potential for variation between alternate LOS structures in the isolates studied, with most strains capable of expressing several alternative terminal structures. The structures predicted to be currently expressed by the genotype of the strains agreed well with conventional immunotyping. No correlation was observed between the structural repertoire and virulence of the isolate. Based on the potential for LOS phase variation in the clinical collection and observations with the paired patient isolates, our data suggest that phase variation of LOS structures is not required for translocation between distinct compartments in the host

  Lipopolysaccharide, biosynthesis, structure, Meningococcus, Phase variation, Lipooligosaccharide, Pathogenesis, Neisseria meningitidis, alternative, Bacterial Proteins, biosynthetic, blood, blotting, chemistry, clinical, correlation, disease, expression, functional, gene, Gene Expression Regulation, Bacterial, genetics, genotype, growth & development, host, human, immunotype, immunotyping, invasive, isolate, LOS, meningococcal, Meningococcal Infections, meningococci, metabolism, microbiology, Neisseria, pathogenicity, PCR, phase, phenotype, polymerase chain reaction, potential, role, Sequence Analysis, DNA, significance, strain, structural, Support, Non-U.S.Gov't, terminal, tract, translocation, variation, Variation (Genetics), virulence

  NCBI PubMed ID: 12443826
  Journal NLM ID: 9315554
  Publisher: Elsevier
  Correspondence: jennings@biosci.uq.edu.au
  Institutions: Department of Microbiology and Parasitology, University of Queensland, St. Lucia, Brisbane, Qld 4072, Australia, National Institute of Public Health and the Environment, Bilthoven, The Netherlands, School of Health Science, Gri?th University, Gold Coast Campus, Qld 4217, Australia
  Methods: PCR, DNA sequencing
  
   
  
  Neisseria meningitidis
  CSDB ID 1710 (all data & tools)
• Article ID: 1621
  Kahler CM, Datta A, Tzeng YL, Carlson RW, Stephens DS "Inner core assembly and structure of the lipooligosaccharide of Neisseria meningitidis: capacity of strain NMB to express all known immunotype epitopes" - Glycobiology 15(4) (2005) 409-419
  

  Neisseria meningitidis expresses a heterogeneous population of lipooligosaccharide (LOS) inner cores variously substituted with α1-3-linked glucose and O-3, O-6, and O-7 linked phosphoethanolamine (PEA), as well as glycine, attached to HepII. Combinations of these attachments to the LOS inner core represent immunodominant epitopes that are being exploited as future vaccine candidates. Historically, each LOS immunotype was structurally assessed and prescribed a certain unique inner core epitope. We report that a single isolate, strain NMB, possesses the capacity to produce all of the known neisserial LOS inner core immunotype structures. Analysis of the inner cores from parental LOS revealed the presence or absence of α1,3-linked glucose, O-6 and/or O-7 linked PEA, in addition to glycine attached at the 7 position of the HepII inner core. Identification and inactivation of lpt-6 in strain NMB resulted in the loss of both O-6 and O-7 linked PEA groups from the LOS inner core, suggesting that Lpt-6 of strain NMB may have bifunctional transferase activities or that the O-6 linked PEA groups once attached to the inner core undergo nonenzymatic transfer to the O-7 position of HepII. Although O-3 linked PEA was not detected in parental LOS inner cores devoid of α1-3-linked glucose residues, LOS glycoforms bearing O-3 PEA groups accumulated in a truncated mutant, NMBlgtK (Hep2Kdo2-lipid A). Because these structures disappeared upon inactivation of the lpt-3 locus, strain NMB expresses a functional O-3 PEA transferase. The LOS glycoforms expressed by NMBlgtK were also devoid of glycine attachments, indicating that glycine was added to the inner core after the completion of the gamma-chain by LgtK. In conclusion, strain NMB has the capability to express all known inner core structures, but in in vitro culture L2 and L4 immunotype structures are predominantly expressed.

  NMR, structure, core, Lipooligosaccharide, Neisseria meningitidis, immunotype, PCR, epitopes, mass spectrometry, inner core, MALDI-TOF, phosphoethanolamine, MS, vaccine, GLC, matrix-assisted laser desorption ionization time of flight, MDO, membrane-derived oligosaccharide, gas-liquid chromatography, heptose PEA transferase, PMAA, partially methylated/ethylated aldtitol acetate

  NCBI PubMed ID: 15574803
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Correspondence: charlene.kahler@med.monoash.edu.au
  Institutions: Department of Microbiology, Monash University, Clayton 3800, Australia
  Methods: methylation, NMR, sugar analysis, MALDI-TOF MS
  
   
  
  Neisseria meningitidis L1
  CSDB ID 10558 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: globotriose
Contained glycoepitopes: IEDB_130651,IEDB_136044,IEDB_136906,IEDB_137472,IEDB_1391964,IEDB_141794,IEDB_142487,IEDB_142488,IEDB_144987,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_152217,IEDB_190606,IEDB_423106,IEDB_742247,IEDB_983931,SB_165,SB_166,SB_167,SB_178,SB_187,SB_192,SB_195,SB_31,SB_6,SB_62,SB_7,SB_88

• Article ID: 16
  Blixt O, Van Die I, Norberg T, van den Eijnden DH "High-level expression of the Neisseria meningitidis lgtA gene in Escherichia coli and characterization of the encoded N-acetylglucosaminyltransferase as a useful catalyst in the synthesis of GlcNAcb1→3Gal and GalNAcb1-3Gal linkages" - Glycobiology 9(10) (1999) 1061-1071
  

  We have expressed the Neisseria meningitidis lgtA gene at a high level in Escherichia coli. The encoded β-N-acetylglucosaminyltransferase, referred to as LgtA, which in the bacterium is involved in the synthesis of the lacto-N-neo-tetraose structural element of the bacterial lipooligosaccharide, was obtained in an enzymatically highly active form. This glycosyltransferase appeared to be unusual in that it displays a broad acceptor specificity toward both α- and β-galactosides, whether structurally related to N- or O-protein-, or lipid-linked oligosaccharides. Product analysis by one- and two-dimensional 400 MHz 1H- and 13C NMR spectroscopy reveals that LgtA catalyzes the introduction of GlcNAc from UDP-GlcNAc in a β1→3-linkage to accepting Gal residues. The enzyme can thus be characterized as a UDP-GlcNAc:Gal α/β-R β 3-N-acetylglucosaminyltransferase. Although lactose is a highly preferred acceptor substrate the recombinant enzyme also acts efficiently on monomeric and dimeric N-acetyllactosamine revealing its potential value in the synthesis of polylactosaminoglycan structures in enzyme assisted procedures. Furthermore, LgtA shows a high donor promiscuity toward UDP-GalNAc, but not toward other UDP-sugars, and can catalyze the introduction of GalNAc in β1→3-linkage to α- or β-Gal in the acceptor structures at moderate rates. LgtA therefore shows promise to be a useful catalyst in the preparative synthesis of both GlcNAc β1→3 Gal and GalNAc β1→3 Gal linkages.

  oligosaccharide, enzyme-assisted-synthesis, recombinant glycosyltransferase, glycosidic linkage, polylactosaminoglycan, recombinant glycosyltrasferase

  NCBI PubMed ID: 10521543
  Publication DOI: 10.1093/glycob/9.10.1061
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Institutions: Department of Chemistry, Swedish University of Agricultural Sciences, Uppsala, Sweden, Department of Medical Chemistry, Vrije Universiteit, Van der Boechorstraat 7, 1081 BT Amsterdam, The Netherlands
  Methods: 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, enzyme-assisted synthesis, DNA techniques, glycosyltransferase assays, kinetics assays
  
   
  
  Escherichia coli
  CSDB ID 1748 (all data & tools)
• Article ID: 701
  Johnson KF "Synthesis of oligosaccharides by bacterial enzymes" - Glycoconjugate Journal 16(2) (1999) 141-146
  

  Many human pathogens initiate disease by utilizing their microbial adhesin proteins to attach to glycoconjugates on host cell mucosal surfaces. Soluble oligosaccharides of identical or similar structure to these naturally occurring ligands can both prevent bacterial attachment as well as mediate the release of attached bacteria. Since it has not been possible to isolate large quantities of these compounds, we have developed enzyme-based technologies to synthesize several relevant human oligosaccharides. Using cloned bacterial glycosyltransferases, we can synthesize several hundred grams of these oligosaccharides at a time. The availability of these large quantities will allow these compounds to be tested as anti-adhesive pharmaceutical agents as well as lead to expanded practical applications.

  synthesis, oligosaccharide, Bacterial, Oligosaccharides, enzyme, glycosyltransferase, Enzymes

  NCBI PubMed ID: 10612413
  Journal NLM ID: 8603310
  Publisher: Kluwer Academic Publishers
  Correspondence: Kjohnson@neose.com
  Institutions: Neose Technologies, Department of Molecular Biology, Horsham, USA, Neose Technologies, epartment of Molecular Biology, Horsham, USA
  
   
  
  (bacteria)
  CSDB ID 813 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: LPS
Contained glycoepitopes: IEDB_130650,IEDB_130651,IEDB_130659,IEDB_136044,IEDB_136906,IEDB_137472,IEDB_1391964,IEDB_140087,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_144987,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_152217,IEDB_190606,IEDB_2189047,IEDB_423106,IEDB_742247,IEDB_983931,SB_165,SB_166,SB_167,SB_178,SB_187,SB_192,SB_195,SB_31,SB_6,SB_62,SB_7,SB_88

• Article ID: 58
  Erwin AL, Haynes PA, Rice PA, Gotschlich EC "Conservation of the lipooligosaccharide synthesis locus lgt among strains of Neisseria gonorrhoeae: Requirement for lgtE in synthesis of the 2C7 epitope and of the b chain of strain 15253" - Journal of Experimental Medicine 184 (1996) 1233-1241
  

  The present study was undertaken to examine the extent to which the lgt locus varies among strains of gonococci. This locus encodes five glycosyl transferases involved in the synthesis of the lipooligosaccharide (LOS) of Neisseria gonorrhoeae. We examined seven gonococcal strains and found that the structure of the lgt locus is conserved among six of these strains. The locus is strikingly altered in strain 15253. This is one of the few strains where extensive structural analysis of its LOS is available, and therefore, we defined the altered lgt locus and focused on the reactivity of mAB 2C7. We found that strain 15253 contains only two lgt genes, lgtA and lgtE. As in F62, lgtA encodes a GlcNAc transferase and is subject to phase variation. In addition, by analysis of deletion mutants, we found that lgtE, which encodes a galactosyl transferase that is required for elongating the alpha-chain, is also necessary for completing the beta chain

  biosynthesis, synthesis, Lipooligosaccharide, genetics, LOS, Neisseria, strain, chain, locus, epitope, conservation, Gonorrhoeae, lgt, Neisseria gonorrhoeae, requirement

  NCBI PubMed ID: 8879194
  Journal NLM ID: 2985109R
  Publisher: Rockefeller University Press
  Institutions: Laboratory of Bacterial Pathogenesis and Immunology, Rockefeller University, New York, NY, USA
  
   
  
  Neisseria gonorrhoeae F62 (1291b)
  CSDB ID 2137 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130651,IEDB_130659,IEDB_136044,IEDB_136906,IEDB_137472,IEDB_1391964,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_144987,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_152217,IEDB_175430,IEDB_190606,IEDB_2189047,IEDB_226300,IEDB_418765,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_423106,IEDB_742247,IEDB_983931,SB_165,SB_166,SB_167,SB_178,SB_187,SB_192,SB_195,SB_31,SB_6,SB_62,SB_7,SB_88

• Article ID: 120
  Tsai C, Chen WH, Balakonis PA "Characterization of terminal NeuNAca2-3Galb1-4GlcNAc sequence in lipooligosaccharide of Neisseria meningitidis" - Glycobiology 8(4) (1998) 359-365
  

  Group B and C Neisseria meningitidis are the major cause of meningococcal disease in the United States and in Europe. N . meningitidis lipooligosaccharide (LOS), a major surface antigen, can be divided into 12 immunotypes of which L1 through L8 were found among Group B and C organisms. Groups B and C but not Group A may sialylate their LOSs with N-acetylneuraminic acid (NeuNAc) at the nonreducing end because they synthesize CMP-NeuNAc. Using sialic acid-galactose binding lectins as probes in an ELISA format, six of the eight LOS immunotypes (L2, L3, L4, L5, L7, and L8) in Groups B and C bound specifically to Maackia amurensis leukoagglutinin (MAL), which recognizes NeuNAcα2-3Galβ1-4GlcNAc/Glc sequence, but not to Sambucus nigra agglutinin, which binds NeuNAcα2-6Gal sequence. The combination of SDS-PAGE and MAL-blot analyses revealed that these six LOSs contained only the NeuNAcα2-3Galβ1-4GlcNAc trisaccharide sequence in their 4.1 kDa LOS components, which have a common terminal lacto-N-neotetraose (LNnT, Galβ1-4GlcNAcβ1-3Galβ1-4Glc) structure when nonsialylated as shown by previous studies. The LOS-lectin binding was abolished when the LOSs were treated with Newcastle disease viral neuraminidase which cleaves α2→3 linked sialic acid. Methylation analysis of a representative LOS (L2) confirmed that NeuNAc is 2→3 linked to Gal. Thus, these LOSs structurally mimic certain glycolipids, i.e., paragloboside (LNnT-ceramide) and sialylparagloboside and some glycoproteins in having LNnT and N-acetyllactosamine sequences, respectively, with or without α2→3 linked NeuNAc. The molecular mimicry of the LOSs may play a role in the pathogenesis of N.meningitidis by assisting the organism to evade host immune defenses in man.

  LPS, structure, core, Lipooligosaccharide, Neisseria meningitidis, Neisseria, terminal, characterization, neuraminic acid, lactosamine, sequence

  NCBI PubMed ID: 9499383
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Institutions: Division of Bacterial Products, Center for Biologics Evaluation and Research, FDA, Bethesda, MD, USA.
  Methods: methylation, ELISA
  
   
  
  Neisseria meningitidis
  CSDB ID 5233 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130651,IEDB_130659,IEDB_136044,IEDB_136794,IEDB_136906,IEDB_137472,IEDB_1391964,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_144987,IEDB_144998,IEDB_146100,IEDB_146664,IEDB_149174,IEDB_150933,IEDB_151528,IEDB_151531,IEDB_152217,IEDB_175430,IEDB_190606,IEDB_2189047,IEDB_226300,IEDB_418765,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_419430,IEDB_423106,IEDB_742247,IEDB_983931,SB_165,SB_166,SB_167,SB_170,SB_171,SB_172,SB_178,SB_187,SB_192,SB_195,SB_31,SB_39,SB_6,SB_62,SB_7,SB_84,SB_88

• Article ID: 121
  Tsai CM, Kao G, Zhu P "Influence of the length of the lipooligosaccharide a chain on its sialylation in Neisseria meningitidis" - Infection and Immunity 70(1) (2002) 407-411
  

  The sialylation of lipooligosaccharide (LOS) in Neisseria meningitidis plays a role in the resistance of the organism to killing by normal human serum. The length of the alpha chain extending out from the heptose I [Hep (I)] moiety of LOS influenced sialylation of N. meningitidis LOS in vitro and in vivo. The alpha chain required a terminal Gal and a trisaccharide or longer oligosaccharide to serve as an acceptor for sialylation. The disaccharide lactose (Galβ1-4Glc) in the alpha chain of immunotype L8 LOS could not function as an acceptor for the sialyltransferase, probably due to steric hindrance imposed by the neighboring Hep (II) with phosphorylethanolamine and another group attached.

  Lipooligosaccharide, Neisseria meningitidis, sialyltransferase, structure-activity relationship, Substrate Specificity

  NCBI PubMed ID: 11748209
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Correspondence: tsai@cber.fda.gov
  Institutions: Division of Bacterial, Parasitic, and Allergenic Products, Center for Biologics, Food and Drug Administration, Bethesda, MD, USA
  Methods: SDS-PAGE
  
   
  
  Neisseria meningitidis 126E (L1)
  CSDB ID 5375 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130650,IEDB_130651,IEDB_130659,IEDB_135394,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_1391964,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_144987,IEDB_146664,IEDB_150908,IEDB_151528,IEDB_151531,IEDB_152217,IEDB_190606,IEDB_2189047,IEDB_423106,IEDB_742247,IEDB_983931,SB_165,SB_166,SB_167,SB_178,SB_187,SB_192,SB_195,SB_31,SB_6,SB_62,SB_7,SB_88

• Article ID: 207
  Wakarchuk WW, Gilbert M, Martin A, Wu YY, Brisson JR, Thibault P, Richards JC "Structure of an a-2,6-sialylated lipooligosaccharide from Neisseria meningitidis immunotype L1" - European Journal of Biochemistry 254(3) (1998) 626-633
  

  The recent cloning of the lipooligosaccharide (LOS) α-2,3-sialyltransferase from Neisseria meningitidis immunotype L3 permitted us to examine other immunotypes for this structural gene. We identified the gene and measured the enzyme activity in the L1 immunotype strain which had previously been reported to lack sialic acid in its LOS because it contains a terminal α-linked galactose which was thought not to be an acceptor for the sialyltransferase. This finding prompted us to re-examine the structure of the LOS from the L1 immunotype, which revealed the presence of sialic acid on the terminal α-linked galactose. Oligosaccharides derived from the LOS were shown to be sialylated by composition and methylation analysis, mass spectrometry and nuclear magnetic resonance. The detailed structural analysis showed the sialic acid to occur only at O6 of the teminal α-D-galactopyranose residue of the α-D-Gal-1,4-β-D-Gal-1,4-β-D-glc trisaccharide (Pk epitope) chain of the LOS, in the alfa-D configuration. These data are the first report of a α-2,6-linked sialic acid in a bacterial LOS or lipopolysaccharide, and also the first report of a sialylated Pk epitope.

  structure, Lipooligosaccharide, Neisseria meningitidis, immunotype, Neisseria, sialyltransferase, glycosyltransferase

  NCBI PubMed ID: 9688275
  Journal NLM ID: 0107600
  Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
  Correspondence: warren.wakarchuk@nrc.ca
  Institutions: Institute for Biological Sciences, National Research Council of Canada, Ontario, Canada
  Methods: NMR-2D, NMR, ESI-MS
  
   
  
  Neisseria meningitidis L1 126E (NRCC 4010)
  CSDB ID 5548 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_115009,IEDB_116046,IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130651,IEDB_136044,IEDB_136906,IEDB_137338,IEDB_137472,IEDB_137777,IEDB_137779,IEDB_138949,IEDB_1391964,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_140624,IEDB_141794,IEDB_142487,IEDB_142488,IEDB_144987,IEDB_144998,IEDB_146664,IEDB_148488,IEDB_151528,IEDB_152217,IEDB_190606,IEDB_2189047,IEDB_423106,IEDB_742247,IEDB_983931,SB_165,SB_166,SB_167,SB_178,SB_187,SB_192,SB_195,SB_31,SB_6,SB_62,SB_7,SB_88

• Article ID: 244
  Griffin R, Cox AD, Makepeace K, Richards JC, Moxon ER, Hood DW "The role of lex2 in lipopolysaccharide biosynthesis in Haemophilus influenzae strains RM7004 and RM153" - Microbiology (2003) 3165-3175
  

  The locus lex2, comprising lex2A and lex2B, contributes to the phase-variable expression of lipopolysaccharide (LPS) of Haemophilus influenzae and was found to be present in 74 % of strains investigated. lex2A contains 5'-GCAA repeats which vary in number from 4 to 46 copies between strains. The locus was cloned from the serotype b strains RM7004 and RM153 and showed >99 % nucleotide sequence identity between these strains and the published lex2 sequence. Disruption of the lex2B gene in strain RM7004 resulted in truncation of some LPS glycoforms, shown by gel fractionation, with only one glycoform reacting with a digalactoside-specific monoclonal antibody, 4C4, compared with four LPS glycoforms in the more elongated LPS of the parent strain. Mass spectrometry and NMR analyses of LPS from the lex2B mutant revealed loss of the terminal digalactoside as well as the second β-glucose extending from the first heptose of the inner core. The authors conclude that Lex2B is the β-(1-4)-glucosyltransferase that adds the second β-glucose to the first β-glucose as part of the oligosaccharide extension from the first heptose of the LPS of strain RM7004. Investigation of the expression of the lex2 locus indicated that the genes are co-transcribed and that both reading frames are required for addition of this second β-glucose in a phase-variable manner

  Lipopolysaccharide, biosynthesis, Haemophilus influenzae, core, lipopolysaccharide biosynthesis, monoclonal antibodies, inner core

  NCBI PubMed ID: 14600228
  Journal NLM ID: 0376646
  Publisher: Washington, DC: Kluwer Academic/Plenum Publishers
  Correspondence: dhood@molbiol.ox.ac.uk
  Institutions: Molecular Infectious Diseases Group, University of Oxford Department of Paediatrics, Weatherall Institute of Molecular Medicine, John Radcliffe Hospital, Headington, Oxford OX3 9DS, UK. Institute for Biological Sciences, National Research Council of Canada, Ottawa, Ontario, Canada K1A 0R6
  
   
  
  Haemophilus influenzae RM7004
  CSDB ID 6866 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_115009,IEDB_116046,IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130651,IEDB_136044,IEDB_136906,IEDB_137472,IEDB_137777,IEDB_137779,IEDB_138949,IEDB_1391964,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_140624,IEDB_141794,IEDB_142487,IEDB_142488,IEDB_144987,IEDB_144998,IEDB_146664,IEDB_148488,IEDB_151528,IEDB_152217,IEDB_190606,IEDB_2189047,IEDB_423106,IEDB_742247,IEDB_983931,SB_165,SB_166,SB_167,SB_178,SB_187,SB_192,SB_195,SB_31,SB_6,SB_62,SB_7,SB_88

• Article ID: 244
  Griffin R, Cox AD, Makepeace K, Richards JC, Moxon ER, Hood DW "The role of lex2 in lipopolysaccharide biosynthesis in Haemophilus influenzae strains RM7004 and RM153" - Microbiology (2003) 3165-3175
  

  The locus lex2, comprising lex2A and lex2B, contributes to the phase-variable expression of lipopolysaccharide (LPS) of Haemophilus influenzae and was found to be present in 74 % of strains investigated. lex2A contains 5'-GCAA repeats which vary in number from 4 to 46 copies between strains. The locus was cloned from the serotype b strains RM7004 and RM153 and showed >99 % nucleotide sequence identity between these strains and the published lex2 sequence. Disruption of the lex2B gene in strain RM7004 resulted in truncation of some LPS glycoforms, shown by gel fractionation, with only one glycoform reacting with a digalactoside-specific monoclonal antibody, 4C4, compared with four LPS glycoforms in the more elongated LPS of the parent strain. Mass spectrometry and NMR analyses of LPS from the lex2B mutant revealed loss of the terminal digalactoside as well as the second β-glucose extending from the first heptose of the inner core. The authors conclude that Lex2B is the β-(1-4)-glucosyltransferase that adds the second β-glucose to the first β-glucose as part of the oligosaccharide extension from the first heptose of the LPS of strain RM7004. Investigation of the expression of the lex2 locus indicated that the genes are co-transcribed and that both reading frames are required for addition of this second β-glucose in a phase-variable manner

  Lipopolysaccharide, biosynthesis, Haemophilus influenzae, core, lipopolysaccharide biosynthesis, monoclonal antibodies, inner core

  NCBI PubMed ID: 14600228
  Journal NLM ID: 0376646
  Publisher: Washington, DC: Kluwer Academic/Plenum Publishers
  Correspondence: dhood@molbiol.ox.ac.uk
  Institutions: Molecular Infectious Diseases Group, University of Oxford Department of Paediatrics, Weatherall Institute of Molecular Medicine, John Radcliffe Hospital, Headington, Oxford OX3 9DS, UK. Institute for Biological Sciences, National Research Council of Canada, Ottawa, Ontario, Canada K1A 0R6
  
   
  
  Haemophilus influenzae RM153
  CSDB ID 6929 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: LPS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130651,IEDB_136044,IEDB_136906,IEDB_137472,IEDB_137777,IEDB_137779,IEDB_138949,IEDB_1391964,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141794,IEDB_142487,IEDB_142488,IEDB_144987,IEDB_144998,IEDB_146664,IEDB_148488,IEDB_151528,IEDB_152217,IEDB_190606,IEDB_2189047,IEDB_423106,IEDB_742247,IEDB_983931,SB_165,SB_166,SB_167,SB_178,SB_187,SB_192,SB_195,SB_31,SB_6,SB_62,SB_7,SB_88

• Article ID: 262
  Hood DW, Deadman ME, Allen T, Masoud H, Martin A, Brisson JR, Fleischmann R, Venter JC, Richards JC, Moxon ER "Use of the complete genome sequence information of Haemophilus influenzae strain Rd to investigate lipopolysaccharide biosynthesis" - Molecular Microbiology 22(5) (1996) 951-965
  

  The availability of the complete 1.83-megabase-pair sequence of the Haemophilus influenzae strain Rd genome has facilitated significant progress in investigating the biology of H.influenzae lipopolysaccharide (LPS), a major virulence determinant of this human pathogen. By searching the H. influenzae genomic database, with sequences of known LPS biosynthetic genes from other organisms, we identified and then cloned 25 candidate LPS genes. Construction of mutant strains and characterization of the LPS by reactivity with monoclonal antibodies, PAGE fractionation patterns and electrospray mass spectrometry comparative analysis have confirmed a potential role in LPS biosynthesis for the majority of these candidate genes. Virulence studies in the infant rat have allowed us to estimate the minimal LPS structure required for intravascular dissemination. This study is one of the first to demonstrate the rapidity, economy and completeness with which novel biological information can be accessed once the complete genome sequence of an organism is available.

  Haemophilus influenzae, lipopolysaccharide biosynthesis, genome, R-type LPS

  NCBI PubMed ID: 8971716
  Journal NLM ID: 8712028
  Publisher: Blackwell Publishing
  Correspondence: dhood@worf.molbiol.ox.ac.uk
  Institutions: Molecular Infectious Diseases Group, University of Oxford Department of Paediatrics, Institute of Molecular Medicine, John Radcliffe Hospital, Headington, Oxford, OX3 9DU, U, Institute for Biological Sciences, National Research Council of Canada, Ottawa, Ontario, Canada, K1A OR6, The Institute for Genomic Research, 9712 Medical Centre Drive, Rockville, Maryland 20850, USA.
  Methods: MS
  
   
  
  Haemophilus influenzae Rd
  CSDB ID 7129 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130648,IEDB_130650,IEDB_130651,IEDB_136044,IEDB_136906,IEDB_137472,IEDB_137473,IEDB_137779,IEDB_138949,IEDB_1391961,IEDB_1391964,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141582,IEDB_141584,IEDB_141794,IEDB_142487,IEDB_142488,IEDB_144987,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_152217,IEDB_153207,IEDB_153208,IEDB_190606,IEDB_2189047,IEDB_423106,IEDB_742247,IEDB_885822,IEDB_983931,SB_165,SB_166,SB_167,SB_178,SB_187,SB_192,SB_195,SB_21,SB_31,SB_6,SB_62,SB_7,SB_88

• Article ID: 464
  St-Michael F, Vinogradov E, Li J, Cox AD "Structural analysis of the lipopolysaccharide from Pasteurella multocida genome strain Pm70 and identification of the putative lipopolysaccharide glycosyltransferases" - Glycobiology 15(4) (2005) 323-333
  

  Pasteurella multocida is an important multi-species veterinary pathogen. The cell surface lipopolysaccharide (LPS) is an important virulence factor and forms the basis of the serotyping scheme, although little structural information about the LPS is known. The structure of the LPS from the Pasteurella multocida genome strain Pm70 was elucidated in this study. The LPS was subjected to a variety of degradative procedures. The structures of the purified products were established by monosaccharide and methylation analyses, NMR spectroscopy and mass spectrometry. The following structure for the core oligosaccharide was determined on the basis of the combined data from these experiments, where based on the NMR data all sugars were found in pyranose ring forms. Glucose, galactose and N-acetyl-galactosamine residues were all present as D-isomers. Kdo is 2-keto-3-deoxy-octulosonic acid, L-α-D-Hep is L-glycero-D-manno-heptose, and PEtn is phosphoethanolamine. Identification of the core oligosaccharide structure enabled a search for glycosyltransferase homologues in the Pm70 genome, and revealed a clustering of the genes putatively responsible for outer core oligosaccharide biosynthesis.

  Lipopolysaccharide, NMR, core oligosaccharide, mass spectrometry, nuclear magnetic resonance, Pasteurella multocida

  NCBI PubMed ID: 15537789
  Publication DOI: 10.1093/glycob/cwi015
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Correspondence: andrew.cox@nrc-cnrc.gc.ca
  Institutions: Institute for Biological Sciences, National Research Council, Ottawa, ON, Canada, K1A 0R6, Institute for Biological Sciences, National Research Council, Ottawa, Ontario, Canada, K1A 0R6
  Methods: 13C NMR, 1H NMR, NMR-2D, methylation, GLC-MS, sugar analysis, 31P NMR, ESI-MS, GLC, CE-MS
  
   
  
  Pasteurella multocida Pm70
  CSDB ID 10152 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: core oligosaccharide, LOS, LPS
Contained glycoepitopes: IEDB_115009,IEDB_116046,IEDB_120354,IEDB_123890,IEDB_130648,IEDB_130650,IEDB_130651,IEDB_136044,IEDB_136906,IEDB_137472,IEDB_137473,IEDB_137777,IEDB_137779,IEDB_138949,IEDB_1391964,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_140624,IEDB_141794,IEDB_142487,IEDB_142488,IEDB_144987,IEDB_146664,IEDB_151528,IEDB_152217,IEDB_190606,IEDB_2189047,IEDB_241118,IEDB_423106,IEDB_742247,IEDB_983931,SB_165,SB_166,SB_167,SB_178,SB_187,SB_192,SB_195,SB_21,SB_31,SB_6,SB_62,SB_7,SB_88

• Article ID: 482
  Wright JC, Hood DW, Randle GA, Makepeace K, Cox AD, Li J, Chalmers R, Richards JC, Moxon ER "lpt6, a gene required for addition of phosphoethanolamine to inner-core lipopolysaccharide of Neisseria meningitidis and Haemophilus influenzae" - Journal of Bacteriology 186(20) (2004) 6970-6982
  

  We previously described a gene, lpt3, required for the addition of phosphoethanolamine (PEtn) at the 3 position on the beta-chain heptose (HepII) of the inner-core Neisseria meningitidis lipopolysaccharide (LPS), but it has long been recognized that the inner-core LPS of some strains possesses PEtn at the 6 position (PEtn-6) on HepII. We have now identified a gene, lpt6 (NMA0408), that is required for the addition of PEtn-6 on HepII. The lpt6 gene is located in a region previously identified as Lgt-3 and is associated with other LPS biosynthetic genes. We screened 113 strains, representing all serogroups and including disease and carriage strains, for the lpt3 and lpt6 genes and showed that 36% contained both genes, while 50% possessed lpt3 only and 12% possessed lpt6 only. The translated amino acid sequence of lpt6 has a homologue (72.5% similarity) in a product of the Haemophilus influenzae Rd genome sequence. Previous structural studies have shown that all H. influenzae strains investigated have PEtn-6 on HepII. Consistent with this, we found that, among 70 strains representing all capsular serotypes and nonencapsulated H. influenzae strains, the lpt6 homologue was invariably present. Structural analysis of LPS from H. influenzae and N. meningitidis strains where lpt6 had been insertionally inactivated revealed that PEtn-6 on HepII could not be detected. The translated amino acid sequences from the N. meningitidis and H. influenzae lpt6 genes have conserved residues across their lengths and are part of a family of proven or putative PEtn transferases present in a wide range of gram-negative bacteria.

  Haemophilus influenzae, Neisseria meningitidis, serotype, phosphoethanolamine, inner-core lipopolysaccharide, transferases

  NCBI PubMed ID: 15466050
  Journal NLM ID: 2985120R
  Publisher: American Society for Microbiology
  Correspondence: claire.wright@paediatrics.ox.ac.uk
  Institutions: Molecular Infectious Diseases Group, Dept. of Pediatrics, Weatherall Institute of Molecular Medicine, John Radcliffe Hospital, Headington, Oxford OX3 9DS, United Kingdom., Molecular Infectious Diseases Group, Dept. of Pediatrics, Weatherall Institute of Molecular Medicine, John Radcliffe Hospital, Headington, Oxford OX3 9DS, United Kingdom
  
   
  
  Haemophilus influenzae Rd
  CSDB ID 9057 (all data & tools)
• Article ID: 817
  Hood DW, Cox AD, Wakarchuk WW, Schur M, Schweda EK, Walsh SL, Deadman ME, Martin A, Moxon ER, Richards JC "Genetic basis for expression of the major globotetraose-containing lipopolysaccharide from H. influenzae strain Rd (RM118)" - Glycobiology 11(11) (2001) 957-967
  

  A genetic basis for the biosynthetic assembly of the globotetraose containing lipopolysaccharide (LPS) of Haemophilus influenzae strain RM118 (Rd) was determined by structural analysis of LPS derived from mutant strains. We have previously shown that the parent strain RM118 elaborates a population of LPS molecules made up of a series of related glycoforms differing in the degree of oligosaccharide chain extension from the distal heptose residue of a conserved phosphorylated inner- core element, L-α-D-Hepp-(1→2)-L-α-D-Hepp-(1→3)-[β-D-Glcp-(1→4)-]-L-α-D-Hepp-(1→5)-α-Kdo. The fully extended LPS glycoform expresses the globotetraose structure, β-D-GalpNAc-(1→3)-α-D-Galp-(1→4)-β-D-Galp-(1→4)-β-D-Glcp. A fingerprinting strategy was employed to establish the structure of LPS from strains mutated in putative glycosyltransferase genes compared to the parent strain. This involved glycose and linkage analysis on intact LPS samples and analysis of O-deacylated LPS samples by electrospray ionization mass spectrometry and 1D (1)H-nuclear magnetic resonance spectroscopy. Four genes, lpsA, lic2A, lgtC, and lgtD, were required for sequential addition of the glycoses to the terminal inner-core heptose to give the globotetraose structure. lgtC and lgtD were shown to encode glycosyltransferases by enzymatic assays with synthetic acceptor molecules. This is the first genetic blueprint determined for H. influenzae LPS oligosaccharide biosynthesis, identifying genes involved in the addition of each glycose residue

  Lipopolysaccharide, biosynthesis, genetic, Haemophilus, Haemophilus influenzae, LPS, oligosaccharide, structure, core, heptose, biosynthetic, disease, expression, gene, strain, structural, terminal, analysis, structural analysis, chain, group, molecular, molecule, degree, conserved, infectious disease, electrospray, ionization mass spectrometry, spectrometry, mutant, linkage, glycosyltransferases, assembly, putative, mass spectrometry, enzymatic, inner core, Magnetic Resonance Spectroscopy, medicine, resonance, spectroscopy, phosphorylated, ionization, glycosyltransferase, population, O-deacylated, acceptor, Synthetic, assay, Electrospray Ionization, globotetraose, electrospray-ionization, fingerprinting, linkage analysis, sequential

  NCBI PubMed ID: 11744630
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Institutions: Molecular Infectious Diseases Group, University of Oxford Department of Paediatrics, Weatherall Institute of Molecular Medicine, John Radcliffe Hospital, Headington, Oxford, OX3 9DS, UK, Institute for Biologicl Sciences, National Research Council of Canada, Ottawa, Ontario, K1A OR6 Canada, Clinical research Centre, Karolinska Institutet and University College of South Stokholm, NOVUM, S-141 86 Huddinge, Sweden
  Methods: PCR, GLC-MS, ESI-MS, electrophoresis, immunoblotting
  
   
  
  Haemophilus influenzae RM118 (Rd)
  CSDB ID 2433 (all data & tools)
• Article ID: 1143
  Risberg A, Masoud H, Martin A, Richards JC, Moxon ER, Schweda EKH "Structural analysis of the lipopolysaccharide oligosaccharide epitopes expressed by a capsule-deficient strain of Haemophilus influenzae Rd" - European Journal of Biochemistry 261(1) (1999) 171-180
  

  Structural elucidation of the lipopolysaccharide (LPS) of Haemophilus influenzae, strain Rd, a capsule-deficient type d strain, has been achieved by using high-field NMR techniques and electrospray ionization-mass spectrometry (ESI-MS) on delipidated LPS and core oligosaccharide samples. It was found that this organism expresses heterogeneous populations of LPS of which the oligosaccharide (OS) epitopes are subject to phase variation. ESI-MS of O-deacylated LPS revealed a series of related structures differing in the number of hexose residues linked to a conserved inner-core element, L-α-D-Hepp-(1→2)-L-α-D-Hepp-(1→3)-[β-D-Glcp- (1→4)-]- L-α-D-Hepp-(1→5)-α-Kdo, and the degree of phosphorylation. The structures of the major LPS glycoforms containing three (two Glc and one Gal), four (two Glc and two Gal) and five (two Glc, two Gal and one GalNAc) hexoses were substituted by both phosphocholine (PCho) and phosphoethanolamine (PEtn) and were determined in detail. In the major glycoform, Hex3, a lactose unit, β-D-Galp-(1→4)-β-D-Glcp, is attached at the O-2 position of the terminal heptose of the inner-core element. The Hex4 glycoform contains the PK epitope, α-D-Galp-(1→4)-β-D-Galp-(1→4)-β-D-Glcp while in the Hex5 glycoform, this OS is elongated by the addition of a terminal β-D-GalpNAc residue, giving the P antigen, β-D-GalpNAc-(1→3)-α-D-Galp-(1→4)-β-D-Galp-(1→4)-D-Glcp. The fully extended LPS glycoform (Hex5) has the following structure. [see text] The structural data provide the first definitive evidence demonstrating the expression of a globotetraose OS epitope, the P antigen, in LPS of H. influenzae. It is noteworthy that the molecular environment in which PCho units are found differs from that observed in an Rd- derived mutant strain (RM.118-28) [Risberg, A., Schweda, E. K. H. & Jansson, P-E. (1997) Eur. J. Biochem. 243, 701-707]

  Lipopolysaccharide, Haemophilus, Haemophilus influenzae, oligosaccharide, strain, structural, analysis, structural analysis, epitope, epitopes, structural studies, Haemophilus influenzae LPS

  NCBI PubMed ID: 10103048
  Journal NLM ID: 0107600
  Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
  Correspondence: elke.schweda@kfcmail.hs.sll.se
  Institutions: Institute for Biological Sciences, National Research Council of Canada, Ottawa, Ontario, Canada, Clinical Research Centre, Karolinska Institute, University College of South Stockholm, Huddinge, Sweden, Molecular Infectious Diseases Group and Department of Pediatrics, Institute for Molecular Medicine, John Radcliffe Hospital, Oxford, UK, University College of South Stockholm, Huddinge, Sweden
  Methods: GLC-MS, NMR, de-O-acylation, GLC, mild acid hydrolysis, DOC-PAGE, immunoblotting
  
   
  
  Haemophilus influenzae Rd
  CSDB ID 4347 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130651,IEDB_130659,IEDB_136044,IEDB_136906,IEDB_137472,IEDB_1391964,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_144987,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_152217,IEDB_190606,IEDB_2189047,IEDB_226300,IEDB_418767,IEDB_418769,IEDB_419429,IEDB_419431,IEDB_423106,IEDB_742247,IEDB_983931,SB_165,SB_166,SB_167,SB_178,SB_187,SB_192,SB_195,SB_31,SB_6,SB_62,SB_7,SB_88

• Article ID: 521
  St-Michael F, Howard MD, Li J, Duncan J, Inzana TJ, Cox AD "Structural analysis of the lipooligosaccharide from the commensal Haemophilus somnus genome strain 129Pt" - Carbohydrate Research 339 (2004) 529-535
  

  The structure for the carbohydrate moiety of the lipooligosaccharide (LOS) from the commensal Haemophilus somnus strain 129Pt was elucidated. The structure of the core oligosaccharide and O-deacylated LOS was established by monosaccharide and methylation analyses, NMR spectroscopy and mass spectrometry. The following structure for the major fully extended carbohydrate glycoform of the LOS was determined on the basis of the combined data from these experiments. In the structure Kdo is 3-deoxy-D-manno-octulosonic acid, Hep is L-glycero-D-manno-heptose and PEtn is phosphoethanolamine. Minor amounts of glycoforms containing nonstoichiometric substituents glycine and phosphate at the distal heptose residue were also identified.

  NMR, Lipooligosaccharide, mass spectrometry, Haemophilus somnus, Commensal

  NCBI PubMed ID: 15013390
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: andrew.cox@nrc-cnrc.gc.ca
  Institutions: Institute for Biological Sciences, National Research Council, 100 Sussex Drive, Room 3101, Ottawa, ON, Canada K1A 0R6, Centre for Molecular Medicine and Infectious Diseases, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061-0342, USA
  Methods: NMR-2D, methylation, NMR, sugar analysis, MS
  
   
  
  Haemophilus somnus 129Pt
  CSDB ID 9254 (all data & tools)
• Article ID: 982
  McQuiston JH, McQuiston JR, Cox AD, Wu YP, Boyle SM, Inzana TJ "Characterization of a DNA region containing 5'-(CAAT)n-3' DNA sequences involved in lipooligosaccharide biosynthesis in Haemophilus somnus" - Microbial Pathogenesis 28(5) (2000) 301-312
  

  biosynthesis, Haemophilus, Phase variation, Lipooligosaccharide, DNA, characterization, region, sequence, Haemophilus somnus

  Journal NLM ID: 8606191
  Publisher: Academic Press
  Correspondence: tinzana@vt.edu
  Institutions: Center for Molecular Medicine and Infectious Diseases, Virginia-Maryland Regional College of Veterinary Madicine,Blacksburg,U.S.A.
  
   
  
  Haemophilus somnus 129Pt
  CSDB ID 3429 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_115009,IEDB_116046,IEDB_120354,IEDB_123890,IEDB_130648,IEDB_130650,IEDB_130651,IEDB_136044,IEDB_136906,IEDB_137472,IEDB_137473,IEDB_137777,IEDB_137779,IEDB_138949,IEDB_1391964,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_140624,IEDB_141794,IEDB_142487,IEDB_142488,IEDB_144987,IEDB_146664,IEDB_151528,IEDB_152217,IEDB_190606,IEDB_2189047,IEDB_241118,IEDB_423106,IEDB_742247,IEDB_983931,SB_165,SB_166,SB_167,SB_178,SB_187,SB_192,SB_195,SB_25,SB_31,SB_6,SB_62,SB_7,SB_88

• Article ID: 558
  Hood DW, Randle G, Cox AD, Makepeace K, Li J, Schweda EK, Richards JC, Moxon ER "Biosynthesis of cryptic lipopolysaccharide glycoforms in Haemophilus influenzae involves a mechanism similar to that required for O-antigen synthesis" - Journal of Bacteriology 186(21) (2004) 7429-7439
  

  It is generally thought that mucosal bacterial pathogens of the genera Haemophilus, Neisseria, and Moraxella elaborate lipopolysaccharide (LPS) that is fundamentally different from that of enteric organisms that express O-specific polysaccharide side chains. Haemophilus influenzae elaborates short-chain LPS that has a role in the pathogenesis of H. influenzae infections. We show that the synthesis of LPS in this organism can no longer be as clearly distinguished from that in other gram-negative bacteria that express an O antigen. We provide evidence that a region of the H. influenzae genome, the hmg locus, is involved in the synthesis of glycoforms in which tetrasaccharide units are added en bloc, not stepwise, to the normal core glycoforms, similar to the biosynthesis of an O-antigen.

  Lipopolysaccharide, antigen, Haemophilus influenzae, Pathogenesis, Neisseria, O-specific polysaccharide, Moraxella, Gram-negative bacteria

  NCBI PubMed ID: 15489455
  Journal NLM ID: 2985120R
  Publisher: American Society for Microbiology
  Correspondence: derek.hood@paediatrics.oxford.ac.uk
  Institutions: Molecular Infectious Diseases Group, University of Oxford Department of Paediatrics, Weatherall Institute of Molecular Medicine, John Radcliffe Hospital, Headington, Oxford OX3 9DS, United Kingdom
  Methods: PCR, SDS-PAGE, ESI-MS
  
   
  
  Haemophilus influenzae RM118
  CSDB ID 9503 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: LOS, LPS
Contained glycoepitopes: IEDB_115009,IEDB_116046,IEDB_120354,IEDB_123890,IEDB_130646,IEDB_130648,IEDB_130650,IEDB_130651,IEDB_130679,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136794,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137473,IEDB_137776,IEDB_137777,IEDB_137779,IEDB_138949,IEDB_1391964,IEDB_1391966,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_140624,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_144987,IEDB_146100,IEDB_146664,IEDB_149144,IEDB_149174,IEDB_150933,IEDB_151528,IEDB_151531,IEDB_152217,IEDB_190606,IEDB_2189047,IEDB_241118,IEDB_423106,IEDB_423120,IEDB_742247,IEDB_983931,SB_115,SB_116,SB_131,SB_145,SB_165,SB_166,SB_167,SB_170,SB_171,SB_172,SB_173,SB_178,SB_187,SB_192,SB_195,SB_25,SB_30,SB_31,SB_37,SB_39,SB_6,SB_62,SB_68,SB_7,SB_76,SB_84,SB_88

• Article ID: 558
  Hood DW, Randle G, Cox AD, Makepeace K, Li J, Schweda EK, Richards JC, Moxon ER "Biosynthesis of cryptic lipopolysaccharide glycoforms in Haemophilus influenzae involves a mechanism similar to that required for O-antigen synthesis" - Journal of Bacteriology 186(21) (2004) 7429-7439
  

  It is generally thought that mucosal bacterial pathogens of the genera Haemophilus, Neisseria, and Moraxella elaborate lipopolysaccharide (LPS) that is fundamentally different from that of enteric organisms that express O-specific polysaccharide side chains. Haemophilus influenzae elaborates short-chain LPS that has a role in the pathogenesis of H. influenzae infections. We show that the synthesis of LPS in this organism can no longer be as clearly distinguished from that in other gram-negative bacteria that express an O antigen. We provide evidence that a region of the H. influenzae genome, the hmg locus, is involved in the synthesis of glycoforms in which tetrasaccharide units are added en bloc, not stepwise, to the normal core glycoforms, similar to the biosynthesis of an O-antigen.

  Lipopolysaccharide, antigen, Haemophilus influenzae, Pathogenesis, Neisseria, O-specific polysaccharide, Moraxella, Gram-negative bacteria

  NCBI PubMed ID: 15489455
  Journal NLM ID: 2985120R
  Publisher: American Society for Microbiology
  Correspondence: derek.hood@paediatrics.oxford.ac.uk
  Institutions: Molecular Infectious Diseases Group, University of Oxford Department of Paediatrics, Weatherall Institute of Molecular Medicine, John Radcliffe Hospital, Headington, Oxford OX3 9DS, United Kingdom
  Methods: PCR, SDS-PAGE, ESI-MS
  
   
  
  Haemophilus influenzae RM118
  CSDB ID 9602 (all data & tools)
• Article ID: 4395
  Spahich NA, Hood DW, Moxon ER, St GJ "Inactivation of Haemophilus influenzae lipopolysaccharide biosynthesis genes interferes with outer membrane localization of the hap autotransporter" - Journal of Bacteriology 194(7) (2012) 1815-1822
  

  Nontypeable Haemophilus influenzae is a major cause of localized respiratory tract disease and initiates infection by colonizing the nasopharynx. Colonization requires adherence to host epithelial cells, which is mediated by surface proteins such as the Hap adhesin. In this study, we identified a relationship between Hap levels in the outer membrane and lipopolysaccharide (LPS) biosynthesis enzymes. We found that mutation of the rfaF, pgmB, lgtC, kfiC, orfE, rfbP, lsgB, or lsgD genes, which are involved in the synthesis of the LPS oligosaccharide core in H. influenzae strain Rd/HapS243A, resulted in loss of Hap in the bacterial outer membrane and a decrease in hap transcript levels. In contrast, the same mutations had no effect on outer membrane localization of H. influenzae P5 or IgA1 protease or levels of p5 or iga1 transcripts, suggesting a Hap-specific effect. Elimination of the HtrA periplasmic protease resulted in a return of Hap to the outer membrane and restoration of hap transcript levels. Consistently, in lgtC phase-off bacteria, Hap was absent from the outer membrane, and hap transcript levels were reduced. Hap localization and hap transcript levels were not related to LPS size but to the functions of the LPS biosynthesis enzymes themselves. We speculate that the lack of certain LPS biosynthesis enzymes causes Hap to mislocalize and accumulate in the periplasm, where it is degraded by HtrA. This degradation then leads to a decrease in hap transcript levels. Together, these data highlight a novel interplay between Hap and LPS biosynthesis that can influence H. influenzae interactions with the host.

  Lipopolysaccharide, biosynthesis, Haemophilus influenzae, gene, mutation, epithelial cells, bacterial outer membrane proteins, nasopharynx

  NCBI PubMed ID: 22287523
  Publication DOI: 10.1128/JB.06316-11
  Journal NLM ID: 2985120R
  Publisher: American Society for Microbiology
  Correspondence: j.stgeme@duke.edu (Joseph W. St. Geme III)
  Institutions: Departments of Pediatrics and Molecular Genetics and Microbiology, Duke University Medical Center, Children's Health Center, Durham, NC, USA
  Methods: PCR, SDS-PAGE, Western blotting, genetic methods
  
   
  
  Haemophilus influenzae
  CSDB ID 27324 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130651,IEDB_136044,IEDB_136906,IEDB_137472,IEDB_1391964,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_144987,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_152217,IEDB_190606,IEDB_2189047,IEDB_418765,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_423106,IEDB_742247,IEDB_983931,SB_165,SB_166,SB_167,SB_178,SB_187,SB_192,SB_195,SB_31,SB_6,SB_62,SB_7,SB_88

• Article ID: 659
  Griffiss JM, Brandt BL, Saunders NB, Zollinger W "Structural relationships and sialylation among meningococcal L1, L8, and L3,7 lipooligosaccharide serotypes" - Journal of Biological Chemistry 275(13) (2000) 9716-9724
  

  Eighteen of 34 endemic meningococcal case strains were of the L8 lipooligosaccharide (LOS) type; four of these were both L3 and L7 (L3,7), and seven were L1. L1 structures arose by alternative terminal Gal substitutions of lactosyl diheptoside L8 structures, as determined by electrospray ionization and other mass spectrometric techniques, and enzymatic and chemical degradations (Structures L1 and L1a). [see text for structure] The more abundant molecule, designated L1, had a trihexose globosyl alpha chain; the less abundant one, designated L1a, had a β-lactosyl alpha chain and a parallel α-lactosaminyl gamma chain. A P(k) globoside (Gal α1→4 Gal β1→4 Glc-R) monoclonal antibody bound 9/10 L1 strains, but a P(1) globoside (Gal α1→4 Gal β1→4 GlcNAc-R) mAb bound none of them. α-Galactosidase caused loss of both L1 structures and creation of L8 structures; β-galactosidase caused loss of the L8 determinant. The L1/P(k) glycose was partially sialylated. Some LOS also had unsubstituted basal β-GlcNAc additions. These structural relationships explain co-expression of L8, L1, and L3,7 serotypes.

  Lipooligosaccharide, meningococcal, structural, serotype, Serotypes, relationship, sialylation

  NCBI PubMed ID: 10734124
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: crapaud@vacom.ucsf.edu
  Institutions: Centre for Immunochemistry and Department of Laboratory Medicine, University of California, San Francisco, California 94121, Department of Bacterial Diseases, Walter Reed Army Institute of Research, Washington, D. C. 20307
  Methods: dephosphorylation, ESI-MS, MS/MS, enzymatic degradation, LSI-MS
  
   
  
  Neisseria meningitidis L1
  CSDB ID 439 (all data & tools)