Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130646,IEDB_130650,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_149144,IEDB_149174,IEDB_150933,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_418761,IEDB_418762,IEDB_418763,IEDB_418764,IEDB_418765,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_423120,IEDB_983931,SB_115,SB_116,SB_131,SB_145,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_187,SB_192,SB_195,SB_30,SB_39,SB_6,SB_68,SB_7,SB_84,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 1709 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130646,IEDB_130650,IEDB_130659,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_144998,IEDB_146100,IEDB_146664,IEDB_149144,IEDB_149174,IEDB_150933,IEDB_151531,IEDB_175430,IEDB_190606,IEDB_2189047,IEDB_226300,IEDB_418761,IEDB_418762,IEDB_418763,IEDB_418764,IEDB_418765,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_419430,IEDB_423120,IEDB_983931,SB_115,SB_116,SB_131,SB_145,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_187,SB_192,SB_195,SB_30,SB_39,SB_6,SB_68,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 M986-NCV
  CSDB ID 5234 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Trivial name: core oligosaccharide L7
Compound class: core oligosaccharide, LOS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130646,IEDB_130650,IEDB_130659,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_146664,IEDB_149144,IEDB_151531,IEDB_175430,IEDB_190606,IEDB_2189047,IEDB_226300,IEDB_418761,IEDB_418762,IEDB_418763,IEDB_418764,IEDB_418765,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_983931,SB_145,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_6,SB_7,SB_88

• Article ID: 206
  Wakarchuk W, Martin A, Jennings MP, Moxon ER, Richards JC "Functional relationships of the genetic locus encoding the glycosyltransferase enzymes involved in expression of the lacto-N-neotetraose terminal lipopolysaccharide structure in Neisseria meningitidis" - Journal of Biological Chemistry 271 (1996) 19166-19173
  

  The biosynthetic function of the lgtABE genetic locus of Neisseria meningititds was determined by structural analysis of lipopolysaccharide (LPS) derived from mutant strains and inzymic assay for glycosyltransferase activity. LPS was obtained from mutants generated by insertion of antibiotic resistance cassets in each of the three genes lgtA, lgtB, lgtE of the N. meningitidis immunotype L3 strain f3 MC58. LPS from the garent strain expresses the terminal lacto-N-neotetraose structure, Gal b1→4 GlcNAc b1→3 Gal b1→4 Glc. Mild hydrazine treatment of the LPS afforded O-deacylated samples that were analyzed directly by electrospray ionization mass spectrometry (ESI-MS) in the negative ioc mode. In conjunction with results from sugar analysis, ESI-MS revealed successive loss of the sugars Gal, GlcNAc, and Gal in lgt B, lgt A and lgt E LPS, respectively. The structure of a sample of O- and N-deacylated LPS derived by aqweous KOH treatment of lgt B LPS was determined i detail by two-dimensional homo- and heteronuclear NMR methods. Using a synthetic b-GlcNAc acceptor and a b-lactose acceptor, the glycosytransferase activities encoded by the lgtB and lgtA genes were unambiguously established. These data provide the first definitive evidence that the three genes encode the respective glycosyltransferases reqwired for biosynthesis of the terminal trisaccharide moity of the lacto-N-neotetraose structure in Neisseria LPS. From ESI-MS data, it was also determined that the Gal-deficient LPS expressed by the lgt E mutant is identical to that of the major component expressed by immunotype L3 galE-deficient strains. The galE gene which encodes for UDP-glucose-4-epimerase plays an essential role in the incorporation of Gal into meningococcal LPS.

  Lipopolysaccharide, biosynthesis, genetic, Haemophilus, LPS, oligosaccharide, structure, core, Neisseria meningitidis, expression, functional, Neisseria, terminal, polysaccharide, locus, monoclonal antibody, specificity, Neisseria gonorrhoeae, enzyme, glycosyltransferase, coupling constant, Enzymes, lacto-N-neotetraose, lipopolysaccharide structure, relationship

  NCBI PubMed ID: 8702594
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: RICHARDS@biologysx.lan.nrc.ca
  Institutions: Institute fro Biological Sciences, National Research Council of Canada, Ottawa, Ontario, K1A OR6, Canada, Molecular Infectious Diseases Group and Department of Paediatrics, Institute for Molecular Medicine, John Radcliffe Hospital, Headington, Oxford, OX3 3DU, United Kingdom
  Methods: NMR-2D, ESI-MS, NMR-1D, genetic methods
  
   
  
  Neisseria meningitidis L3
  CSDB ID 5791 (all data & tools)
• 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
  
   
  
  Neisseria meningitidis L3
  CSDB ID 9055 (all data & tools)
• Article ID: 6049
  Di Lorenzo F, Duda KA, Lanzetta R, Silipo A, De Castro C, Molinaro A "A Journey from Structure to Function of Bacterial Lipopolysaccharides" - Chemical Reviews (2021)
  

  Lipopolysaccharide (LPS) is a crucial constituent of the outer membrane of most Gram-negative bacteria, playing a fundamental role in the protection of bacteria from environmental stress factors, in drug resistance, in pathogenesis, and in symbiosis. During the last decades, LPS has been thoroughly dissected, and massive information on this fascinating biomolecule is now available. In this Review, we will give the reader a third millennium update of the current knowledge of LPS with key information on the inherent peculiar carbohydrate chemistry due to often puzzling sugar residues that are uniquely found on it. Then, we will drive the reader through the complex and multifarious immunological outcomes that any given LPS can raise, which is strictly dependent on its chemical structure. Further, we will argue about issues that still remain unresolved and that would represent the immediate future of LPS research. It is critical to address these points to complete our notions on LPS chemistry, functions, and roles, in turn leading to innovative ways to manipulate the processes involving such a still controversial and intriguing biomolecule.

  Lipopolysaccharide, LPS, structure, Pathogenesis, carbohydrate, function, gram negative bacteria

  NCBI PubMed ID: 34286971
  Publication DOI: 10.1021/acs.chemrev.0c01321
  Journal NLM ID: 2985134R
  Publisher: Chem Rev
  Correspondence: Antonio Molinaro
  Institutions: Department of Chemical Sciences, University of Naples Federico II, via Cinthia 4, 80126 Naples, Italy, Task Force on Microbiome Studies, University of Naples Federico II, Via Cinthia 4, 80126 Naples, Italy, Research Center Borstel Leibniz Lung Center, Parkallee 4a, 23845 Borstel, Germany, Department of Agricultural Sciences, University of Naples Federico II, Via Universita 96, 80055 Portici, Naples, Italy, Department of Chemistry, School of Science, Osaka University, 1-1 Osaka University Machikaneyama, Toyonaka, Osaka 560-0043, Japan
  
   
  
  Neisseria meningitidis
  CSDB ID 7919 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130646,IEDB_130650,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_146664,IEDB_149144,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_418761,IEDB_418762,IEDB_418763,IEDB_418764,IEDB_418765,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_983931,SB_145,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_6,SB_7,SB_88

• Article ID: 879
  Kogan G, Uhrin D, Brisson J, Jennings HJ "Structural basis of the Neisseria meningitidis immunotypes including the L4 and L7 immunotypes" - Carbohydrate Research 298 (1997) 191-199
  

  The application of high-resolution 1H, 13C and 31P NMR and MS analyses to the oligosaccharide moieties of the L4 and L7 immunotypes of Neisseria meningitidis revealed that they had the following structures: [formula: see text] The fact that the L7 LPS is not sialylated at O-3 of its terminal β-D-galactopyranosyl residue implies that it is a mutant strain unable to endogenously sialylate its lacto-N-neotetraose antenna. With the structural elucidation of the L4 and L7 LPS immunotypes, a more comprehensive structural profile of the LPS involved in disease isolates can now be assembled. This provides valuable insights into the structural basis of the N. meningitidis immunotyping system which could be of use in formulating an LPS-based vaccine against meningococcal meningitis.

  Lipopolysaccharide, NMR, LPS, oligosaccharide, core, Neisseria meningitidis, immunotype, Neisseria, structural, neuraminic acid, MS

  NCBI PubMed ID: 9090813
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: Institute for Biological Sciences, National Research Council of Canada, Ottawa, Canada K1A 0R6
  Methods: NMR, MS
  
   
  
  Neisseria meningitidis L7
  CSDB ID 2985 (all data & tools)
• Article ID: 2749
  Verheul AFM, Snippe H, Poolman JT "Meningococcal lipopolysaccharides: virulence factor and potential vaccine component" - Microbiological Reviews 57 (1993) 34-49
  
  Journal NLM ID: 7806086
  
   
  
  Neisseria meningitidis
  CSDB ID 143628 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130646,IEDB_130650,IEDB_130659,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_149144,IEDB_149174,IEDB_150933,IEDB_151531,IEDB_175430,IEDB_190606,IEDB_2189047,IEDB_226300,IEDB_418761,IEDB_418762,IEDB_418763,IEDB_418764,IEDB_418765,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_423120,IEDB_983931,SB_115,SB_116,SB_131,SB_145,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_187,SB_192,SB_195,SB_30,SB_39,SB_6,SB_68,SB_7,SB_84,SB_88

• Article ID: 1110
  Plested JS, Makepeace K, Jennings MP, Gidney MAJ, Lacelle S, Brisson JR, Cox AD, Martin A, Bird AG, Tang CM, Mackinnon FM, Richards JC, Moxon ER "Conservation and accessibility of an inner core lipopolysaccharide epitope of Neisseria meningitidis" - Infection and Immunity 67(10) (1999) 5417-5426
  

  We investigated the conservation and antibody accessibility of inner core epitopes of Neisseria meningitidis lipopolysaccharide (LPS) because of their potential as vaccine candidates. An immunoglobulin G3 murine monoclonal antibody (MAb), designated MAb B5, was obtained by immunizing mice with a galE mutant of N. meningitidis H44/76 (B.15.P1.7,16 immunotype L3). We have shown that MAb B5 can bind to the core LPS of wild-type encapsulated MC58 (B.15.P1.7,16 immunotype L3) organisms in vitro and ex vivo. An inner core structure recognized by MAb B5 is conserved and accessible in 26 of 34 (76%) of group B and 78 of 112 (70%) of groups A, C, W, X, Y, and Z strains. N. meningitidis strains which possess this epitope are immunotypes in which phosphoethanolamine (PEtn) is linked to the 3-position of the b-chain heptose (HepII) of the inner core. In contrast, N. meningitidis strains lacking reactivity with MAb B5 have an alternative core structure in which PEtn is linked to an exocyclic position (i.e., position 6 or 7) of HepII (immunotypes L2, L4, and L6) or is absent (immunotype L5). We conclude that MAb B5 defines one or more of the major inner core glycoforms of N. meningitidis LPS. These findings support the possibility that immunogens capable of eliciting functional antibodies specific to inner core structures could be the basis of a vaccine against invasive infections caused by N. meningitidis.

  Lipopolysaccharide, core, Neisseria meningitidis, Neisseria, epitope, conservation, inner core

  NCBI PubMed ID: 10496924
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Correspondence: Joyce.Plested@paediatrics.ox.ac.uk
  Institutions: Molecular Infectious Disease Group, Oxford University Department of Paediatrics, John Radcliffe Hospital, Oxford OX3 9DU, Department of Clinical Immunology, Churchill Hospital, Headington, Oxford OX3 7LJ, United Kingdom, Department of Microbiology, University of Queensland, St. Lucia, Brisbane, Australia, the Institute for Biological Sciences, National Research Council, Ottawa, Canada K1A OR64
  
   
  
  Neisseria meningitidis L3
  CSDB ID 4184 (all data & tools)
• Article ID: 4791
  Reinhardt A, Yang Y, Claus H, Pereira CL, Cox AD, Vogel U, Anish C, Seeberger PH "Antigenic Potential of a Highly Conserved Neisseria meningitidis Lipopolysaccharide Inner Core Structure Defined by Chemical Synthesis" - Chemistry and Biology 22(1) (2015) 38-49
  

  Neisseria meningitidis is a leading cause of bacterial meningitis worldwide. We studied the potential of synthetic lipopolysaccharide (LPS) inner core structures as broadly protective antigens against N. meningitidis. Based on the specific reactivity of human serum antibodies to synthetic LPS cores, we selected a highly conserved LPS core tetrasaccharide as a promising antigen. This LPS inner core tetrasaccharide induced a robust IgG response in mice when formulated as an immunogenic glycoconjugate. Binding of raised mouse serum to a broad collection of N. meningitidis strains demonstrated the accessibility of the LPS core on viable bacteria. The distal trisaccharide was identified as the crucial epitope, whereas the proximal Kdo moiety was immunodominant and induced mainly nonprotective antibodies that are responsible for lack of functional protection in polyclonal serum. Our results identified key antigenic determinants of LPS core glycan and, hence, may aid the design of a broadly protective immunization against N. meningitidis.

  Lipopolysaccharide, Neisseria meningitidis, vaccine, LPS-core

  Publication DOI: 10.1016/j.chembiol.2014.11.016
  Journal NLM ID: 9500160
  Publisher: Maryland Heights, MO: Elsevier
  Correspondence: chakkumkal.anish@mpikg.mpg.de (C.A.); peter.seeberger@mpikg.mpg.de (P.H.S.)
  Institutions: Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, 14424 Potsdam, Germany, Institute of Chemistry and Biochemistry, Freie Universitat Berlin, Arnimallee 22, 14195 Berlin, Germany, Institute for Hygiene and Microbiology, University of Wurzburg, Germany, 97080 Wurzburg, Germany, Vaccine Program, Human Health Therapeutics Portfolio, National Research Council, 100 Sussex Drive, Ottawa, ON K1A 0R6, Canada
  Methods: ELISA, chemical synthesis, chemical methods, biological assays, serological methods, conjugation
  
   
  
  Neisseria meningitidis L3
  CSDB ID 30661 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130646,IEDB_130650,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_149144,IEDB_149174,IEDB_150933,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_418761,IEDB_418762,IEDB_418763,IEDB_418764,IEDB_418765,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_423120,IEDB_983931,SB_115,SB_116,SB_131,SB_145,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_187,SB_192,SB_195,SB_30,SB_39,SB_6,SB_68,SB_7,SB_84,SB_88

• Article ID: 1306
  Zamze S, Martinez-Pomares L, Jones H, Taylor PR, Stillion RJ, Gordon S, Wong SY "Recognition of bacterial capsular polysaccharides and lipopolysaccharides by the macrophage mannose receptor" - Journal of Biological Chemistry 277(44) (2002) 41613-41623
  

  The in vitro binding of the macrophage mannose receptor to a range of different bacterial polysaccharides was investigated. The receptor was shown to bind to purified capsular polysaccharides from Streptococcus pneumoniae and to the lipopolysaccharides, but not capsular polysaccharides, from Klebsiella pneumoniae. Binding was Ca(2+)- dependent and inhibitable with d-mannose. A fusion protein of the mannose receptor containing carbohydrate recognition domains 4-7 and a full-length soluble form of the mannose receptor containing all domains external to the transmembrane region both displayed very similar binding specificities toward bacterial polysaccharides, suggesting that domains 4-7 are sufficient for recognition of these structures. Surprisingly, no direct correlation could be made between polysaccharide structure and binding to the mannose receptor, suggesting that polysaccharide conformation may play an important role in recognition. The full-length soluble form of the mannose receptor was able to bind simultaneously both polysaccharide via the carbohydrate recognition domains and sulfated oligosaccharide via the cysteine-rich domain. The possible involvement of the mannose receptor, either cell surface or soluble, in the innate and adaptive immune responses to bacterial polysaccharides is discussed

  Lipopolysaccharide, conformation, lipopolysaccharides, oligosaccharide, structure, correlation, Bacterial, role, capsular, polysaccharide, Streptococcus, Streptococcus pneumoniae, D-mannose, capsular polysaccharide, capsular polysaccharides, polysaccharides, carbohydrate, cell, Research, form, recognition, involvement, protein, response, specificity, Klebsiella, Bacterial polysaccharide, region, external, surface, polysaccharide structure, purified, Klebsiella pneumoniae, bacterial polysaccharides, binding, domain, domains, vaccine, immune response, Mannose, immune, in vitro, macrophage, soluble, receptor, sulfated, pathology, carbohydrate recognition, carbohydrate recognition domain, fusion, fusion protein, transmembrane

  NCBI PubMed ID: 12196537
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: susanne.zamze@jenner.ac.uk
  Institutions: Edward Jenner Institute for Vaccine Research, Compton, Berkshire RG20 7NN, United Kingdom and the Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, United Kingdom
  
   
  
  Neisseria meningitidis L3
  CSDB ID 6094 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130646,IEDB_130650,IEDB_130659,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_149144,IEDB_149174,IEDB_150933,IEDB_151531,IEDB_175430,IEDB_190606,IEDB_2189047,IEDB_226300,IEDB_418761,IEDB_418762,IEDB_418763,IEDB_418764,IEDB_418765,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_423120,IEDB_983931,SB_115,SB_116,SB_131,SB_145,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_187,SB_192,SB_195,SB_30,SB_39,SB_6,SB_68,SB_7,SB_84,SB_88

• Article ID: 1352
  Andersen SR, Guthrie T, Guile GR, Kolberg J, Hou S, Hyland L, Wong SY "Cross-reactive polyclonal antibodies to the inner core of lipopolysaccharide from Neisseria meningitidis" - Infection and Immunity 70(3) (2002) 1293-1300
  

  Sera from mice immunized with native or detergent-extracted outer membrane vesicles derived from lipopolysaccharide (LPS) mutant 44/76(Mu- 4) of Neisseria meningitidis were analyzed for antibodies to LPS. The carbohydrate portion of 44/76(Mu-4) LPS consists of the complete inner core, Glc β1→4 [GlcNAc α1→2 Hep α 1→3]Hep α1→5 KDO[4→2 αKDO]. Immunoblot analysis revealed that some sera contained antibodies to wild-type LPS which has a fully extended carbohydrate chain of immunotype L3,7, as well as to the homologous LPS. Sera reacted only weakly to LPS from 44/76(Mu-3), which lacks the terminal glucose of the inner core. No binding to more truncated LPS was observed. Consequently, the cross-reactive epitopes are expressed mainly by the complete inner core. Dephosphorylation of wild-type LPS abolished antibody binding to LPS in all but one serum. Thus, at least two specificities of cross-reactive antibodies exist: one is dependent on phosphoethanolamine groups in LPS, and one is not. Detection of these cross-reactive antibodies strongly supports the notion that epitopes expressed by meningococcal LPS inner core are also accessible to antibodies when the carbohydrate chain is fully extended. Also, these inner core epitopes are sufficiently immunogenic to induce antibody levels detectable in polyclonal antibody responses. Meningococci can escape being killed by antibodies to LPS that bind only to a specific LPS variant, by altering the carbohydrate chain length. Cross-reactive antibodies may prevent such escape. Therefore, inner core LPS structures may be important antigens in future vaccines against meningococcal disease.

  Lipopolysaccharide, core, Neisseria meningitidis, Neisseria, antibodies, antibody, inner core, cross-reactive

  NCBI PubMed ID: 11854213
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Correspondence: svein.r.andersen@jenner.ac.uk
  Institutions: The Edward Jenner Institute for Vaccine Research, Compton, Newbury, Berkshire RG20 7NN, United Kingdom
  Methods: serological methods
  
   
  
  Neisseria meningitidis 44/76-I (L3)
  CSDB ID 6211 (all data & tools)
• Article ID: 1353
  Andersen SR, Kolberg J, Hoiby EA, Namork E, Caugant DA, Froholm LO, Jantzen E, Bjune G "Lipopolysaccharide heterogeneity and escape mechanism of Neisseria meningitidis: Possible consequences for vaccine development" - Microbial Pathogenesis 23(3) (1997) 139-155
  

  We wanted to compare the potential protective capacity of antibodies to meningococcal lipopolysaccharides (LPS). The frequency of occurrence and degree of expression of the epitopes recognized by murine monoclonal antibodies (MAbs) to immunotypes L3,7,9 (9-2-L379) and L8 (2-1-L8) and to the LPS inner core (216-Lc and 217-Lc), were determined among 77 consecutive Norwegian meningococcal patient isolates from 1995. The immunotype L3,7,9 was strongly expressed by 95% of the isolates, whereas L8 was weakly to moderately expressed by 9%. The inner core epitopes, were widely distributed among the serogroup B organisms, but were proved weakly expressed. The bactericidal activity of the four MAbs to various selected strains, was found to correlate positively with the quantity of the LPS epitopes recognized by these four MAbs in the bacteria. When tested in the serum bactericidal assay (SBA), often a few percent of the colonies of the inocula survived high concentrations of the MAbs. The results indicate that escape from the bactericidal action could be achieved through: (i) selection of variants not expressing the LPS-epitope of the actual MAb, (ii) a relative reduction in the density of the LPS-epitope achieved by dilution with another LPS structure or (iii) other factors, not yet understood. In conclusion, antibodies to the L3,7,9 epitope seem to be of importance for protection, whereas antibodies to the epitopes of the LPS inner core or immunotype L8, are not likely to offer protection alone. However, in order to prevent escape through alteration of the LPS pattern of the microbes, various LPS structures should probably be present in the OMV vaccine.

  lipopolysaccharides, Neisseria meningitidis, vaccine, escape mechanisms, bacterial antibodies

  NCBI PubMed ID: 9281472
  Publication DOI: 10.1006/mpat.1997.0143
  Journal NLM ID: 8606191
  Publisher: Academic Press
  Institutions: Department of Vaccinology, National Institute of Public Health, P.O. Box 4404 Torshov, Oslo, N-0403, Norway, Department of Bacteriology, National Institute of Public Health, P.O. Box 4404 Torshov, Oslo, N-0403, Norway, Department of Environmental Medicine, National Institute of Public Health, P.O. Box 4404 Torshov, Oslo, N-0403, Norway
  
   
  
  Neisseria meningitidis L3
  CSDB ID 6213 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130646,IEDB_130650,IEDB_130659,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_146664,IEDB_149144,IEDB_151531,IEDB_175430,IEDB_190606,IEDB_2189047,IEDB_226300,IEDB_418761,IEDB_418762,IEDB_418763,IEDB_418764,IEDB_418765,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_983931,SB_145,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_6,SB_7,SB_88

• Article ID: 1352
  Andersen SR, Guthrie T, Guile GR, Kolberg J, Hou S, Hyland L, Wong SY "Cross-reactive polyclonal antibodies to the inner core of lipopolysaccharide from Neisseria meningitidis" - Infection and Immunity 70(3) (2002) 1293-1300
  

  Sera from mice immunized with native or detergent-extracted outer membrane vesicles derived from lipopolysaccharide (LPS) mutant 44/76(Mu- 4) of Neisseria meningitidis were analyzed for antibodies to LPS. The carbohydrate portion of 44/76(Mu-4) LPS consists of the complete inner core, Glc β1→4 [GlcNAc α1→2 Hep α 1→3]Hep α1→5 KDO[4→2 αKDO]. Immunoblot analysis revealed that some sera contained antibodies to wild-type LPS which has a fully extended carbohydrate chain of immunotype L3,7, as well as to the homologous LPS. Sera reacted only weakly to LPS from 44/76(Mu-3), which lacks the terminal glucose of the inner core. No binding to more truncated LPS was observed. Consequently, the cross-reactive epitopes are expressed mainly by the complete inner core. Dephosphorylation of wild-type LPS abolished antibody binding to LPS in all but one serum. Thus, at least two specificities of cross-reactive antibodies exist: one is dependent on phosphoethanolamine groups in LPS, and one is not. Detection of these cross-reactive antibodies strongly supports the notion that epitopes expressed by meningococcal LPS inner core are also accessible to antibodies when the carbohydrate chain is fully extended. Also, these inner core epitopes are sufficiently immunogenic to induce antibody levels detectable in polyclonal antibody responses. Meningococci can escape being killed by antibodies to LPS that bind only to a specific LPS variant, by altering the carbohydrate chain length. Cross-reactive antibodies may prevent such escape. Therefore, inner core LPS structures may be important antigens in future vaccines against meningococcal disease.

  Lipopolysaccharide, core, Neisseria meningitidis, Neisseria, antibodies, antibody, inner core, cross-reactive

  NCBI PubMed ID: 11854213
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Correspondence: svein.r.andersen@jenner.ac.uk
  Institutions: The Edward Jenner Institute for Vaccine Research, Compton, Newbury, Berkshire RG20 7NN, United Kingdom
  Methods: serological methods
  
   
  
  Neisseria meningitidis 44/76-I (L7)
  CSDB ID 6301 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130646,IEDB_130648,IEDB_130650,IEDB_130659,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137473,IEDB_137776,IEDB_1391966,IEDB_139427,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_149144,IEDB_151531,IEDB_175430,IEDB_190606,IEDB_2189047,IEDB_226300,IEDB_418761,IEDB_418762,IEDB_418763,IEDB_418764,IEDB_418765,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_419430,IEDB_419431,IEDB_419432,IEDB_983931,SB_145,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_21,SB_30,SB_6,SB_7,SB_88

• Article ID: 1363
  Banerjee A, Wang R, Uljon SN, Rice PA, Gotschlich EC, Stein DC "Identification of the gene (lgtG) encoding the lipooligosaccharide b chain synthesizing glucosyl transferase from Neisseria gonorrhoeae" - Proceedings of the National Academy of Sciences of the USA 95(18) (1998) 10872-10877
  

  The lipooligosaccharide from Neisseria gonorrhoeae (GC), consists of lipid A, an oligosaccharide core and three branches, alpha, beta, and gamma. We report the cloning of the gene (lgtG, lipooligosaccharide glycosyl transferase G) encoding the glucosyl transferase of GC that initiates the beta chain which consists of a lactosyl moiety. This gene contains a homopolymeric tract of cytidine [poly(C)] and we demonstrate that changes in the number of Cs in poly(C) account for the variation of beta chain expression in different GC strains. Biochemical analyses and mass spectrometry clearly attribute the reactivity of mAb 2C7 to the presence of the lactosyl beta chain. In addition, we demonstrate that in the absence of the lactosyl group, a phosphoethanolamine is added to generate a new antigenic epitope as evidenced by the gain of reactivity to mAb 2-L1-8. These results show that, like the alpha chain, the beta chain of lipooligosaccharide is subject to antigenic variation.

  Lipooligosaccharide, gene, Neisseria, identification, transferase, Gonorrhoeae, Neisseria gonorrhoeae

  NCBI PubMed ID: 9724797
  Journal NLM ID: 7505876
  Publisher: National Academy of Sciences
  Correspondence: ecg@rockvax.rockefeller.edu
  Institutions: Department of Microbiology, University of Maryland, College Park
  
   
  
  Neisseria gonorrhoeae
  CSDB ID 6238 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130646,IEDB_130650,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_149144,IEDB_149174,IEDB_150933,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_418761,IEDB_418762,IEDB_418763,IEDB_418764,IEDB_418765,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_423120,IEDB_983931,SB_115,SB_116,SB_131,SB_145,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_187,SB_192,SB_195,SB_30,SB_39,SB_6,SB_68,SB_7,SB_84,SB_88

• 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 L3
  CSDB ID 10718 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130646,IEDB_130650,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136095,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_146664,IEDB_149144,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_418761,IEDB_418762,IEDB_418763,IEDB_418764,IEDB_418765,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_983931,SB_145,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_6,SB_7,SB_88

• 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 L7
  CSDB ID 10722 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: LOS, LPS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130646,IEDB_130650,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_146664,IEDB_149144,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_418761,IEDB_418762,IEDB_418763,IEDB_418764,IEDB_418765,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_419431,IEDB_983931,SB_145,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_6,SB_7,SB_88

• Article ID: 2164
  Dell A, Azadi P, Tiller P, Thomas-Oates J, Jennings HJ, Beurret M, Michon F "Analysis of oligosaccharide epitopes of meningococcal lipopolysaccharides by fast-atom-bombardment mass spectrometry" - Carbohydrate Research 200 (1990) 59-76
  

  A mass-spectrometric approach is presented for the analysis of the structures of lipopolysaccharide-derived oligosaccharides, which are frequently difficult to define by classical methods since they contain chemically labile components. The method involves f.a.b.-m.s. of the oligosaccharides, their peracetylated and permethylated derivatives, their deuterioacetylated and methylated analogues, and the fragments obtained during graded methanolysis of the methylated analogues. Data obtained from two representative meningococcal LPS oligosaccharides define the sequence, patterns of branching, and the extent and location of the phosphorylethanolamine and O-acetyl substituents.

  NCBI PubMed ID: 1696172
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: Department of Biochemistry, Imperial College, London, Great Britain.
  Methods: FAB-MS
  
   
  
  Neisseria meningitidis L4
  CSDB ID 115898 (all data & tools)
• Article ID: 2513
  Mandrell RE, Apicella MA "Lipo-oligosaccharides (LOS) of mucosal pathogens: molecular mimicry and host-modification of LOS" - Immunobiology 187 (1993) 382-402
  

  Immunochemical studies of the lipo-oligosaccharides (LOS) of the Gram-negative bacteria Neisseria gonorrhoeae and Neisseria meningitidis have revealed some interesting structural characteristics of these LOS that might relate to their roles during pathogenesis. The carbohydrate moieties of the LOS of pathogenic Neisseria mimic carbohydrates present in glycosphingolipids of human cells. Firstly, an LOS component present among a number of Neisseria species is antigenically and/or chemically identical to lactoneoseries glycosphingolipids present in human cells. The lactoneoseries LOS becomes sialylated on Neisseria gonorrhoeae when they are grown in the presence of cytidine 5'-monophospho-N-acetyl-neuraminic acid (CMP-NANA), the nucleotide sugar for sialic acid. Examination of gonococci present in exudates from males with natural infection indicates that sialylation also occurs in vivo. The mechanism for this process apparently involves a bacterial sialyltransferase scavenging available host CMP-NANA ("host-modification" of LOS) and transferring the sialic acid to the lactoneoserieslike LOS. Strains of N. meningitidis and Haemophilus influenzae also express similarly sialylated LOS suggesting that this is a common mechanism of pathogenesis among these bacteria. Additional examples of LOS that mimic other glycosphingolipid series have been identified also and the fact that multiple series can be expressed in a single population of gonococci suggests that a diverse set of LOS can be presented to the host during infection. It is possible that this diverse set of LOS serve different functions for the bacteria in various hosts and/or environments during infection.

  NCBI PubMed ID: 8330904
  Publication DOI: 10.1016/S0171-2985(11)80352-9
  Journal NLM ID: 8002742
  Publisher: Amsterdam: Elsevier
  Institutions: Division of Infectious Diseases, San Francisco General Hospital, University of California
  
   
  
  Neisseria gonorrhoeae 1291
  CSDB ID 129895 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: LPS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130646,IEDB_130650,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_146664,IEDB_149144,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_418761,IEDB_418762,IEDB_418763,IEDB_418764,IEDB_418765,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_419431,IEDB_983931,SB_145,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_6,SB_7,SB_88

• Article ID: 2164
  Dell A, Azadi P, Tiller P, Thomas-Oates J, Jennings HJ, Beurret M, Michon F "Analysis of oligosaccharide epitopes of meningococcal lipopolysaccharides by fast-atom-bombardment mass spectrometry" - Carbohydrate Research 200 (1990) 59-76
  

  A mass-spectrometric approach is presented for the analysis of the structures of lipopolysaccharide-derived oligosaccharides, which are frequently difficult to define by classical methods since they contain chemically labile components. The method involves f.a.b.-m.s. of the oligosaccharides, their peracetylated and permethylated derivatives, their deuterioacetylated and methylated analogues, and the fragments obtained during graded methanolysis of the methylated analogues. Data obtained from two representative meningococcal LPS oligosaccharides define the sequence, patterns of branching, and the extent and location of the phosphorylethanolamine and O-acetyl substituents.

  NCBI PubMed ID: 1696172
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: Department of Biochemistry, Imperial College, London, Great Britain.
  Methods: FAB-MS
  
   
  
  Neisseria meningitidis L4
  CSDB ID 115899 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130646,IEDB_130650,IEDB_130659,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136095,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_149144,IEDB_149174,IEDB_150933,IEDB_151531,IEDB_175430,IEDB_190606,IEDB_2189047,IEDB_226300,IEDB_418761,IEDB_418762,IEDB_418763,IEDB_418764,IEDB_418765,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_423120,IEDB_983931,SB_115,SB_116,SB_131,SB_145,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_187,SB_192,SB_195,SB_30,SB_39,SB_6,SB_68,SB_7,SB_84,SB_88

• Article ID: 3173
  Zhu P, Boykins RA, Tsai CM "Genetic and functional analyses of the lgtH gene, a member of the β-1,4-galactosyltransferase gene family in the genus Neisseria" - Microbiology (2006) 123-134
  

  Lipooligosaccharide (LOS) is a major virulence factor of the pathogenic Neisseria. Three galactosyltransferase genes, lgtB, lgtE and lgtH, responsible for the biosynthesis of LOS oligosaccharide chains, were analysed in five Neisseria species. The function of lgtH in Neisseria meningitidis 6,275 was determined by mutagenesis and chemical characterization of the parent and mutant LOS chains. The chemical characterization included SDS-PAGE, immunoblot, hexose and mass spectrometry analyses. Compared with the parent LOS, the mutant LOS lacked galactose, and its oligosaccharide decreased by three or four sugar units in matrix-assisted laser desorption ionization (MALDI)-MS analysis. The results show that lgtH encodes a β-1,4-galactosyltransferase, and that the glucose moiety linked to heptose (Hep) in the alpha chain is the acceptor site in the biosynthesis of Neisseria LOS. To understand the sequence diversity and relationships of lgtB, lgtE and lgtH, the entire lgt-1 locus was further sequenced in three N. meningitidis strains and three commensal Neisseria strains, and compared with the previously reported lgt genes from Neisseria species. Comparison of the protein sequences of the three enzymes LgtB, LgtE and LgtH showed a conserved N-terminal region, and a highly variable C-terminal region, suggesting functional constraint for substrate and acceptor specificity, respectively. The analyses of allelic variation and evolution of 23 lgtB, 12 lgtE and 14 lgtH sequences revealed a distinct evolutionary history of these genes in Neisseria. For example, the splits graph of lgtE displayed a network evolution, indicating frequent DNA recombination, whereas splits graphs of lgtB and lgtH displayed star-tree-like evolution, indicating the accumulation of point mutations. The data presented here represent examples of the evolution and variation of prokaryotic glycosyltransferase gene families. These imply the existence of multiple enzyme isoforms for biosynthesis of a great diversity of oligosaccharides in nature.

  biosynthesis, Lipooligosaccharide, Neisseria, MALDI-TOF, ACTH, adrenocorticotropic hormone, galactosyltransferase genes, lgtB, lgtE, lgtH, N-acetylneuramic acid

  NCBI PubMed ID: 16385122
  Publication DOI: 10.1099/mic.0.28327-0
  Journal NLM ID: 0376646
  Publisher: Washington, DC: Kluwer Academic/Plenum Publishers
  Correspondence: Peixuan Zhu
  Institutions: Division of Bacterial, Parasitic and Allergenic Products, Center for Biologics Evaluation and Research, FDA, 8800 Rockville Pike, Bethesda, MD, USA
  Methods: SDS-PAGE, MALDI-TOF MS, MS, composition analysis, genetic methods, immunoblotting
  
   
  
  Neisseria meningitidis 6275, Neisseria meningitidis L3
  CSDB ID 20177 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130646,IEDB_130650,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136794,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_149144,IEDB_149174,IEDB_150933,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_418761,IEDB_418762,IEDB_418763,IEDB_418764,IEDB_418765,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_423120,IEDB_983931,SB_115,SB_116,SB_131,SB_145,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_187,SB_192,SB_195,SB_30,SB_39,SB_6,SB_68,SB_7,SB_84,SB_88

• Article ID: 3228
  Kahler CM, Lyons-Schindler S, Choudhury B, Glushka J, Carlson RW, Stephens DS "O-Acetylation of the terminal N-acetylglucosamine of the lipooligosaccharide inner core in Neisseria meningitidis. Influence on inner core structure and assembly" - Journal of Biological Chemistry 281(29) (2006) 19939-19948
  

  O-Acetylation is a common decoration on endotoxins derived from many Gram-negative bacterial species, and it has been shown to be instrumental (e.g. in Salmonella typhimurium) in determining the final tertiary structure of the endotoxin and the immunogenicity of the molecule. Structural heterogeneity of endotoxins produced by mucosal pathogens such as Neisseria meningitidis is determined by decorations on the heptose inner core, including O-acetylation of the terminal N-acetylglucosamine (GlcNAc) attached to HepII. In this report, we show that O-acetylation of the meningococcal lipooligosaccharide (LOS) inner core has an important role in determining inner core assembly and immunotype expression. The gene encoding the LOS O-acetyltransferase, lot3, was identified by homology to NodX from Rhizobium leguminosarum. Inactivation of lot3 in strain NMB resulted in the loss of the O-acetyl group located at the C-3 position of the terminal GlcNAc of the LOS inner core. Inactivation of either lot3 or lgtG, which encodes the HepII glucosyltransferase, did not result in the appearance of the O-3-linked phosphoethanolamine (PEA) groups on the LOS inner core. Construction of a double mutant in which both lot3 and lgtG were inactivated resulted in the appearance of O-3-linked PEA groups on the LOS inner core. In conclusion, O-acetylation status of the terminal GlcNAc of the gamma-chain of the meningococcal LOS inner core is an important determinant for the appearance or exclusion of the O-3-linked PEA group on the LOS inner core and contributes to LOS structural diversity. O-Acetylation also likely influences resistance to complement-mediated lysis and may be important in LOS conjugate vaccine design.

  Lipooligosaccharide, Neisseria meningitidis, O-acetylation, endotoxin, inner core, glucosyltransferase, Rhizobium leguminosarum, conjugate vaccine

  NCBI PubMed ID: 16687398
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: 30322ckahler@cyllene.uwa.edu.au
  Institutions: Department of Microbiology, Monash University, Wellington Road, Melbourne, Australia, Complex Carbohydrate Research Center, University of Georgia, Athens, GA, USA, Departments of Medicine and Microbiology and Immunology and Laboratories of Microbial Pathogenesis, Emory University School of Medicine and Veterans Affairs Medical Center, Atlanta, Georgia
  Methods: NMR, MALDI-TOF MS
  
   
  
  Neisseria meningitidis L3
  CSDB ID 20313 (all data & tools)