Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Trivial name: lipooligosaccharide core L2
Compound class: LOS
Contained glycoepitopes: 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_144998,IEDB_146100,IEDB_146664,IEDB_149144,IEDB_149174,IEDB_150933,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_418762,IEDB_418764,IEDB_418767,IEDB_418769,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: 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 1606 (all data & tools)
• Article ID: 277
  Kahler CM, Carlson RW, Rahman MM, Martin LE, Stephens DS "Two glycosyltransferase genes, lgtF and rfaK, constitute the lipooligosaccharide ice (inner core extension) biosynthesis operon of Neisseria meningitidis" - Journal of Bacteriology 178(23) (1996) 6677-6684
  

  We have characterized an operon required for inner-core biosynthesis of the lipooligosaccharide (LOS) of Neisseria meningitidis. Using Tn916 mutagenesis, we recently identified the α-1,2-N-acetylglucosamine (GlcNAc) transferase gene (rfaK), which when inactivated prevents the addition of GlcNAc and alpha chain to the meningococcal LOS inner core (C. M. Kahler, R. W. Carlson, M. M. Rahman, L. E. Martin, and D. S. Stephens, J. Bacteriol. 178:1265-1273, 1996). During the study of rfaK, a second open reading frame (lgtF) of 720 bp was found upstream of rfaK. An amino acid sequence homology search of the GenBank and EMBL databases revealed that the amino terminus of LgtF has significant homology with a family of β-glycosyltransferases involved in the biosynthesis of polysaccharides and O antigen of lipopolysaccharides. The chromosomal copy of lgtF was mutagenized with a nonpolar antibiotic resistance cassette to minimize potential polar effects on rfaK. Tricine sodium dodecyl sulfate-polyacrylamide gel electrophoresis and composition analysis of the LOS from the nonpolar lgtF mutant showed that this strain produced a truncated LOS structure which contained a LOS inner core of GlcNAc1Hep2KDO2lipid A but without the addition of lacto-N-neotetraose to HepI or glucose to HepII. These results and the amino acid homology with β-glycosyltransferases suggest that lgtF encodes the UDP-glucose:LOS-β-1,4-glucosyltransferase which attaches the first glucose residue to HepI of LOS. Reverse transcriptase PCR and primer extension analysis indicate that both lgtF and rfaK are cotranscribed as a polycistronic message from a promoter upstream of lgtF. This arrangement suggests that completion of the LOS inner core and the initiation of the alpha chain addition are tightly coregulated in N. meningitidis.

  biosynthesis, Lipooligosaccharide, Neisseria meningitidis, gene, inner core, glycosyltransferase, operon

  NCBI PubMed ID: 8955282
  Journal NLM ID: 2985120R
  Publisher: American Society for Microbiology
  Correspondence: dstep01@emory.edu
  Institutions: Departments of Medicine and Microbiology and Immunology, Emory University School of Medicine and Department of Veterans Affairs Medical Center, Atlanta, and The Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia
  Methods: genetic methods
  
   
  
  Neisseria meningitidis L2
  CSDB ID 7176 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: 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_418762,IEDB_418764,IEDB_418767,IEDB_418769,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 1708 (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: 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_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_150939,IEDB_151531,IEDB_158549,IEDB_190606,IEDB_2189047,IEDB_226300,IEDB_418762,IEDB_418764,IEDB_418767,IEDB_418769,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: 106
  Tong Y, Arking D, Ye S, Reinhold B, Reinhold V, Stein DC "Neisseria gonorrhoeae strain PID2 simultaneously expresses six chemically related lipooligosaccharide structures" - Glycobiology 12(9) (2002) 523-533
  

  Neisseria gonorrhoeae strain PID2 was isolated from a woman suffering from pelvic inflammatory disease. When LOS expressed by this strain is analyzed on SDS-PAGE gels, at least six different lipooligosaccharide (LOS) components are visualized. We characterized the LOSs made by this strain by exoglycosidase digestion, sugar composition analysis, mass spectrometry, and analysis of the genes needed for its synthesis. DNA sequence analysis showed that the lgt gene cluster in this strain has undergone a rearrangement and that it possesses two copies of lgtA, one copy of lgtB and lgtC, and a hybrid gene containing sequences from lgtB and lgtE. We determined that the hybrid lgtB/E gene retained the lgtE gene function. DNA sequence analysis of the gene organization suggested that an intramolecular recombination between lgtA and lgtD and lgtB and lgtE had occurred via homologous recombination between similar sequences. Our studies demonstrated that fluorophore-assisted carbohydrate electrophoresis can be utilized to rapidly determine the composition of LOS. By combining exoglycosidase digestion, in combination with mass spectrometry analysis and compositional analysis, the data indicate that all of the LOS components produced by PID2 extend off of the alpha chain. The longest alpha chain oligosaccharide structure is Gal-GlcNAc-Gal-GlcNAc-Gal-Glc-Heptose I, and the six LOS components are built up by sequentially adding sugars onto the first heptose. PID2 LOS is the first Neisserial LOS to be shown to be devoid of phosphoethanolamine modifications. Because PID2 can surface express its LOS, it indicates that the addition of phosphoethanolamine is not required for LOS surface expression.

  LOS, mass spectrometry, carbohydrate epitopes, FACE analysis, lipooligosaccharide structure

  NCBI PubMed ID: 12213785
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Methods: mild acid hydrolysis, MS, serological methods, electrophoresis
  
   
  
  Neisseria gonorrhoeae PID2
  CSDB ID 5216 (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
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_190606,IEDB_2189047,IEDB_226300,IEDB_418762,IEDB_418764,IEDB_418767,IEDB_418769,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: 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 5394 (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_146100,IEDB_146664,IEDB_149144,IEDB_149174,IEDB_150933,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_226300,IEDB_418762,IEDB_418764,IEDB_418767,IEDB_418769,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: 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 5395 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: 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_190606,IEDB_2189047,IEDB_226300,IEDB_418762,IEDB_418764,IEDB_418767,IEDB_418769,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: 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 5396 (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_130659,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_1391966,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_146664,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_226300,IEDB_418764,IEDB_418767,IEDB_418769,IEDB_419429,IEDB_983931,SB_145,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_6,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 5398 (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
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_146100,IEDB_146664,IEDB_149144,IEDB_149174,IEDB_150933,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_226300,IEDB_418762,IEDB_418764,IEDB_418767,IEDB_418769,IEDB_419429,IEDB_419431,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: 377
  Shih GC, Kahler CM, Carlson RW, Rahman MM, Stephens DS "gmhX, a novel gene required for the incorporation of L-glycero-D-manno-heptose into lipooligosaccharide in Neisseria meningitidis" - Microbiology 147(8) (2001) 2367-2377
  

  Lipooligosaccharide (LOS) is a critical virulence factor of Neisseria meningitidis. A Tn916 insertion mutant, designated 469, was found to exhibit a markedly truncated LOS of 2<9 kDa when compared by Tricine/SDS-PAGE to the parental LOS (4<6 kDa). Electrospray mass spectrometry analysis of 469 LOS revealed that it consisted of the deep rough, heptose-deficient structure, Kdo2-lipid A. Sequencing of chromosomal DNA flanking the Tn916 insertion in mutant 469 revealed that the transposon had inserted into an ORF predicted to encode a 187 aa protein with sequence homology to the histidinol-phosphate phosphatase domain of Escherichia coli HisB and to a family of genes of unknown function. The gene, designated gmhX, is part of a polycistronic operon (ice-2) containing two other genes, nlaB and orfC. nlaB encodes a lysophosphatidic-acid acyltransferase and orfC is predicted to encode a Nacetyltransferase. Specific polar and non-polar gmhX mutations in the parental strain, NMB, exhibited the truncated LOS structure of mutant 469, and repair of gmhX mutants by homologous recombination with the wild-type gmhX restored the LOS parental phenotype. GmhX mutants demonstrated increased sensitivity to polymyxin B. GmhX mutants and other Kdo2-lipid A mutants also demonstrated increased sensitivity to killing by normal human serum but were not as sensitive as inner-core mutants containing heptose. In the genomes of Helicobacter pylori and Synechocystis, gmhX homologues are associated with heptose biosynthesis genes; however, in N. meningitidis, gmhX was found in a location distinct from that of gmhA, rfaD, rfaE, aut and rfaC. GmhX is a novel enzyme required for the incorporation of L-glycero-D-manno-heptose into meningococcal LOS, and is a candidate for the 2-D-glycero-manno-heptose phosphatase of the heptose biosynthesis pathway.

  L-glycero-D-manno-heptose, lipopolysaccharides, Meningococcus, Lipooligosaccharide, Neisseria meningitidis, gene, Neisseria, heptose biosynthesis, incorporation

  NCBI PubMed ID: 11496013
  Journal NLM ID: 0376646
  Publisher: Washington, DC: Kluwer Academic/Plenum Publishers
  Correspondence: dstep01@emory.edu
  Institutions: Departments of Medicine, and Microbiology and Immunology, Emory University School of Medicine, Atlanta, GA 30322, USA, Department of Veterans Affairs Medical Center, Atlanta, GA 30033, USA, The Complex Carbohydrate Research Center, University of Georgia, Athens, GA 30602, USA
  Methods: genetic methods
  
   
  
  Neisseria meningitidis NMB (L2)
  CSDB ID 8315 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Trivial name: lipooligosaccharide core L3
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130646,IEDB_130648,IEDB_130650,IEDB_130659,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137473,IEDB_137776,IEDB_1391961,IEDB_1391966,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141584,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_146664,IEDB_149144,IEDB_149569,IEDB_151531,IEDB_152213,IEDB_153205,IEDB_190606,IEDB_2189047,IEDB_226300,IEDB_418762,IEDB_418764,IEDB_418767,IEDB_418769,IEDB_419429,IEDB_885822,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: 432
  Zhu P, Klutch MJ, Bash MC, Tsang RS, Ng LK, Tsai CM "Genetic diversity of three lgt loci for biosynthesis of lipooligosaccharide (LOS) in Neisseria species" - Microbiology 148(6) (2002) 1833-1844
  

  Lipooligosaccharide (LOS) is a major virulence factor of the pathogenic NEISSERIA: Nine lgt genes at three chromosomal loci (lgt-1, 2, 3) encoding the glycosyltransferases responsible for the biosynthesis of LOS oligosaccharide chains were examined in 26 Neisseria meningitidis, 51 Neisseria gonorrhoeae and 18 commensal Neisseria strains. DNA hybridization, PCR and nucleotide sequence data were compared to previously reported lgt genes. Analysis of the genetic organization of the lgt loci revealed that in N. meningitidis, the lgt-1 and lgt-3 loci were hypervariable genomic regions, whereas the lgt-2 locus was conserved. In N. gonorrhoeae, no variability in the composition or organization of the three lgt loci was observed. lgt genes were detected only in some commensal Neisseria species. The genetic organization of the lgt-1 locus was classified into eight types and the lgt-3 locus was classified into four types. Two types of arrangement at lgt-1 (II and IV) and one type of arrangement at lgt-3 (IV) were novel genetic organizations reported in this study. Based on the three lgt loci, 10 LOS genotypes of N. meningitidis were distinguished. Phylogenetic analysis revealed a gene cluster, lgtH, which separated from the homologous genes lgtB and lgtE. The lgtH and lgtE genes were mutually exclusive and were located at the same position in lgt-1. The data demonstrated that pathogenic and commensal Neisseria share a common lgt gene pool and horizontal gene transfer appears to contribute to the genetic diversity of the lgt loci in Neisseria

  biosynthesis, oligosaccharide structure, Neisseria meningitidis, Neisseria, gene cluster, glycosyltransferases, Gonorrhoeae, Neisseria gonorrhoeae, genetic diversity, lipooligosaccharide (LOS), phylogenetic analysis, virulence factor

  NCBI PubMed ID: 12055303
  Journal NLM ID: 0376646
  Publisher: Washington, DC: Kluwer Academic/Plenum Publishers
  Correspondence: zhu@cber.fda.gov
  Institutions: Division of Bacterial, Parasitic and Allergenic Products and Division of Viral Products, Center for Biologics Evaluation and Research, FDA, 8800 Rockville Pike, Bethesda, MD, USA
  Methods: PCR, DNA sequencing, DNA techniques, genetic methods, RT-PCR
  
   
  
  Neisseria meningitidis 6275, Neisseria meningitidis M986, Neisseria meningitidis BB-305, Neisseria meningitidis 44/76, Neisseria meningitidis MC58, Neisseria meningitidis 89I
  CSDB ID 8726 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Trivial name: lipooligosaccharide core L6 / L12
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130650,IEDB_130659,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_1391966,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_146664,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_226300,IEDB_418764,IEDB_418767,IEDB_418769,IEDB_419429,IEDB_983931,SB_145,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_6,SB_7,SB_88

• Article ID: 432
  Zhu P, Klutch MJ, Bash MC, Tsang RS, Ng LK, Tsai CM "Genetic diversity of three lgt loci for biosynthesis of lipooligosaccharide (LOS) in Neisseria species" - Microbiology 148(6) (2002) 1833-1844
  

  Lipooligosaccharide (LOS) is a major virulence factor of the pathogenic NEISSERIA: Nine lgt genes at three chromosomal loci (lgt-1, 2, 3) encoding the glycosyltransferases responsible for the biosynthesis of LOS oligosaccharide chains were examined in 26 Neisseria meningitidis, 51 Neisseria gonorrhoeae and 18 commensal Neisseria strains. DNA hybridization, PCR and nucleotide sequence data were compared to previously reported lgt genes. Analysis of the genetic organization of the lgt loci revealed that in N. meningitidis, the lgt-1 and lgt-3 loci were hypervariable genomic regions, whereas the lgt-2 locus was conserved. In N. gonorrhoeae, no variability in the composition or organization of the three lgt loci was observed. lgt genes were detected only in some commensal Neisseria species. The genetic organization of the lgt-1 locus was classified into eight types and the lgt-3 locus was classified into four types. Two types of arrangement at lgt-1 (II and IV) and one type of arrangement at lgt-3 (IV) were novel genetic organizations reported in this study. Based on the three lgt loci, 10 LOS genotypes of N. meningitidis were distinguished. Phylogenetic analysis revealed a gene cluster, lgtH, which separated from the homologous genes lgtB and lgtE. The lgtH and lgtE genes were mutually exclusive and were located at the same position in lgt-1. The data demonstrated that pathogenic and commensal Neisseria share a common lgt gene pool and horizontal gene transfer appears to contribute to the genetic diversity of the lgt loci in Neisseria

  biosynthesis, oligosaccharide structure, Neisseria meningitidis, Neisseria, gene cluster, glycosyltransferases, Gonorrhoeae, Neisseria gonorrhoeae, genetic diversity, lipooligosaccharide (LOS), phylogenetic analysis, virulence factor

  NCBI PubMed ID: 12055303
  Journal NLM ID: 0376646
  Publisher: Washington, DC: Kluwer Academic/Plenum Publishers
  Correspondence: zhu@cber.fda.gov
  Institutions: Division of Bacterial, Parasitic and Allergenic Products and Division of Viral Products, Center for Biologics Evaluation and Research, FDA, 8800 Rockville Pike, Bethesda, MD, USA
  Methods: PCR, DNA sequencing, DNA techniques, genetic methods, RT-PCR
  
   
  
  Neisseria meningitidis M992, Neisseria meningitidis 7897
  CSDB ID 8729 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Trivial name: lipooligosaccharide core L7 / L9
Compound class: core oligosaccharide
Contained glycoepitopes: 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_190606,IEDB_2189047,IEDB_226300,IEDB_418762,IEDB_418764,IEDB_418767,IEDB_418769,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: 432
  Zhu P, Klutch MJ, Bash MC, Tsang RS, Ng LK, Tsai CM "Genetic diversity of three lgt loci for biosynthesis of lipooligosaccharide (LOS) in Neisseria species" - Microbiology 148(6) (2002) 1833-1844
  

  Lipooligosaccharide (LOS) is a major virulence factor of the pathogenic NEISSERIA: Nine lgt genes at three chromosomal loci (lgt-1, 2, 3) encoding the glycosyltransferases responsible for the biosynthesis of LOS oligosaccharide chains were examined in 26 Neisseria meningitidis, 51 Neisseria gonorrhoeae and 18 commensal Neisseria strains. DNA hybridization, PCR and nucleotide sequence data were compared to previously reported lgt genes. Analysis of the genetic organization of the lgt loci revealed that in N. meningitidis, the lgt-1 and lgt-3 loci were hypervariable genomic regions, whereas the lgt-2 locus was conserved. In N. gonorrhoeae, no variability in the composition or organization of the three lgt loci was observed. lgt genes were detected only in some commensal Neisseria species. The genetic organization of the lgt-1 locus was classified into eight types and the lgt-3 locus was classified into four types. Two types of arrangement at lgt-1 (II and IV) and one type of arrangement at lgt-3 (IV) were novel genetic organizations reported in this study. Based on the three lgt loci, 10 LOS genotypes of N. meningitidis were distinguished. Phylogenetic analysis revealed a gene cluster, lgtH, which separated from the homologous genes lgtB and lgtE. The lgtH and lgtE genes were mutually exclusive and were located at the same position in lgt-1. The data demonstrated that pathogenic and commensal Neisseria share a common lgt gene pool and horizontal gene transfer appears to contribute to the genetic diversity of the lgt loci in Neisseria

  biosynthesis, oligosaccharide structure, Neisseria meningitidis, Neisseria, gene cluster, glycosyltransferases, Gonorrhoeae, Neisseria gonorrhoeae, genetic diversity, lipooligosaccharide (LOS), phylogenetic analysis, virulence factor

  NCBI PubMed ID: 12055303
  Journal NLM ID: 0376646
  Publisher: Washington, DC: Kluwer Academic/Plenum Publishers
  Correspondence: zhu@cber.fda.gov
  Institutions: Division of Bacterial, Parasitic and Allergenic Products and Division of Viral Products, Center for Biologics Evaluation and Research, FDA, 8800 Rockville Pike, Bethesda, MD, USA
  Methods: PCR, DNA sequencing, DNA techniques, genetic methods, RT-PCR
  
   
  
  Neisseria meningitidis 6155, Neisseria meningitidis M120, Neisseria meningitidis Z2491
  CSDB ID 8730 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
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_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_190606,IEDB_2189047,IEDB_226300,IEDB_418762,IEDB_418764,IEDB_418767,IEDB_418769,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_30,SB_6,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
  
   
  
  Neisseria meningitidis L2
  CSDB ID 8983 (all data & tools)
• 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 L2, Neisseria meningitidis L4
  CSDB ID 4185 (all data & tools)