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1. Compound ID: 381
a-D-Galp-(1-4)-b-D-Galp-(1-4)-b-D-Glcp-(1-4)-+
|
a-D-GlcpNAc-(1-2)-+ | a-Kdop-(2-4)-+
| | |
EtN-(1--P--3)--L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/ |
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Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130651,IEDB_130659,IEDB_136044,IEDB_136906,IEDB_137472,IEDB_1391964,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_144987,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_152217,IEDB_175430,IEDB_190606,IEDB_2189047,IEDB_226300,IEDB_418765,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_423106,IEDB_742247,IEDB_983931,SB_165,SB_166,SB_167,SB_178,SB_187,SB_192,SB_195,SB_31,SB_6,SB_62,SB_7,SB_88
The structure is contained in the following publication(s):
- 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: 9499383Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Institutions: Division of Bacterial Products, Center for Biologics Evaluation and Research, FDA, Bethesda, MD, USA.
Methods: methylation, ELISA
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2. Compound ID: 382
a-D-GlcpNAc-(1-2)-+
|
/Variants 0/-L-gro-a-D-manHepp-(1-3)-+ a-Kdop-(2-4)-+
| |
?%a-Neup5Ac-(2-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-Glcp-(1-4)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/
/Variants 0/ is:
EtN-(1--P--3)--
OR (exclusively)
a-D-Glcp-(1-3)- |
Show graphically |
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
The structure is contained in the following publication(s):
- 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: 11748209Journal NLM ID: 0246127Publisher: 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
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3. Compound ID: 511
a-D-GlcpNAc-(1-2)-+
|
/Variants 0/-L-gro-a-D-manHepp-(1-3)-+ a-Kdop-(2-4)-+
| |
?%a-Neup5Ac-(2-3)-a-D-Galp-(1-4)-b-D-Galp-(1-4)-b-D-Glcp-(1-4)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/
/Variants 0/ is:
EtN-(1--P--3)--
OR (exclusively)
a-D-Glcp-(1-3)- |
Show graphically |
Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130651,IEDB_130659,IEDB_136044,IEDB_136794,IEDB_136906,IEDB_137472,IEDB_1391964,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_144987,IEDB_144998,IEDB_146100,IEDB_146664,IEDB_149174,IEDB_150933,IEDB_151528,IEDB_151531,IEDB_152217,IEDB_175430,IEDB_190606,IEDB_2189047,IEDB_226300,IEDB_418765,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_419430,IEDB_423106,IEDB_742247,IEDB_983931,SB_165,SB_166,SB_167,SB_170,SB_171,SB_172,SB_178,SB_187,SB_192,SB_195,SB_31,SB_39,SB_6,SB_62,SB_7,SB_84,SB_88
The structure is contained in the following publication(s):
- 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: 11748209Journal NLM ID: 0246127Publisher: 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
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4. Compound ID: 512
a-D-GlcpNAc-(1-2)-+
|
/Variants 0/-L-gro-a-D-manHepp-(1-3)-+ a-Kdop-(2-4)-+
| |
?%a-Neup5Ac-(2-3)-b-D-Galp-(1-4)-b-D-Glcp-(1-4)-b-D-Glcp-(1-4)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/
/Variants 0/ is:
EtN-(1--P--3)--
OR (exclusively)
a-D-Glcp-(1-3)- |
Show graphically |
Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130659,IEDB_130679,IEDB_136044,IEDB_136794,IEDB_137472,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_144998,IEDB_146100,IEDB_146664,IEDB_149174,IEDB_150933,IEDB_151531,IEDB_175430,IEDB_190606,IEDB_2189047,IEDB_226300,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_419430,IEDB_983931,SB_116,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_192,SB_195,SB_37,SB_39,SB_6,SB_68,SB_7,SB_76,SB_84,SB_88
The structure is contained in the following publication(s):
- 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: 11748209Journal NLM ID: 0246127Publisher: 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
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5. Compound ID: 513
b-D-Galp-(1-4)-b-D-Glcp-(1-4)-+
|
a-D-GlcpNAc-(1-2)-+ | a-Kdop-(2-4)-+
| | |
/Variants 0/-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/
/Variants 0/ is:
EtN-(1--P--3)--
OR (exclusively)
a-D-Glcp-(1-3)- |
Show graphically |
Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130659,IEDB_136044,IEDB_137472,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151531,IEDB_175430,IEDB_190606,IEDB_2189047,IEDB_226300,IEDB_418765,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_419430,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_6,SB_7,SB_88
The structure is contained in the following publication(s):
- 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: 11748209Journal NLM ID: 0246127Publisher: 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
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6. Compound ID: 526
b-D-Galp-(1-4)-b-D-Glcp-(1-4)-+
|
a-D-GlcpNAc-(1-2)-+ | a-Kdop-(2-4)-+
| | |
EtN-(1--P--3)--L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/ |
Show graphically |
Structure type: oligomer
Aglycon: lipid A
Trivial name: core oligosaccharide L8
Compound class: core oligosaccharide, LOS, LPS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130659,IEDB_136044,IEDB_137472,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_146664,IEDB_151531,IEDB_175430,IEDB_190606,IEDB_2189047,IEDB_226300,IEDB_418765,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_6,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 107
Tong YH, Reinhold V, Reinhold B, Brandt B, Stein DC "Structural and immunochemical characterization of the lipooligosaccharides expressed by Neisseria subflava 44" -
Journal of Bacteriology 183(3) (2001) 942-950
Neisserial lipooligosaccharides (LOSs) are a family of complex cell surface glycolipids. We used mass spectrometry techniques (electrospray ionization, collision-induced dissociation, and multiple step), combined with fluorophore-assisted carbohydrate electrophoresis monosaccharide composition analysis, to determine the structure of the two low-molecular-mass LOS molecules (LOSI and LOSII) expressed by Neisseria subflava 44. We determined that LOSI contains one glucose on both the alpha and beta chains. LOSII is structurally related to LOSI and differs from it by the addition of a hexose (either glucose or galactose) on the alpha chain. LOSI and LOSII were able to bind monoclonal antibody (MAb) 25-1-LC1 when analyzed by Western blotting experiments. We used a set of genetically defined Neisseria gonorrhoeae mutants that expressed single defined LOS epitopes and a group of Neisseria meningitidis strains that expresses chemically defined LOS components to determine the structures recognized by MAb 25-1-LC1. We found that extensions onto the beta-chain glucose of LOSI block the recognition by this MAb, as does further elongation from the LOSII alpha chain. The LOSI structure was determined to be the minimum structure that is recognized by MAb 25-1-LC1.
Lipooligosaccharide, Neisseria, structural, characterization, immunochemical, lipooligosaccharides
NCBI PubMed ID: 11208793Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Correspondence: DS64@UMAIL.UMD.EDTJ
Institutions: Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, Maryland 20742
Methods: ESI-MS, CID-MS/MS, FACE
- 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: 10496924Journal NLM ID: 0246127Publisher: 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
- Article ID: 3525
O'Connor ET, Swanson KV, Cheng H, Fluss K, Griffiss JM, Stein DC "Structural requirements for monoclonal antibody 2-1-L8 recognition of neisserial lipooligosaccharides" -
Hybridoma 27(2) (2008) 71-79
Monoclonal antibodies (MAbs) that bind neisserial lipooligosaccharides (LOS) have been widely used in structural studies of these glycolipids. MAb 2-1-L8 binds LOS with a lactosyl a chain (Gal β1-4 Glc β1-4 [Glc-NAc α1-2 Hep2 α1-3] Hep1 α1-KDO) and at least one phosphoethanolamine (PEA) substitution of Hep2, but the requirement for PEA substitution and/or the exact position of this substitution, cyclic or exocyclic, remains unclear. In order to clarify the exact specificity of this MAb, we engineered an isogenic family of lpt mutants that each make LOS with a lactosyl a chain, but that lacked cyclic (-3Hep2), exocyclic (-6Hep2), or any PEA residues. Mass spectrometry showed that mutants that lack either Lpt3 or Lpt6 make small amounts of LOS with two PEA substitutions. Thus, each enzyme is able to phosphoethanolaminylate the alternate site, albeit with low efficiency. LOS made by the mutant that lacked both Lpt3 and Lpt6 was devoid of PEA. LOS made by the ∆lpt3 mutant did not bind MAb 2-1-L8 on Western blot analysis, whereas ∆ pt6 LOS did. Analysis of intact mutants by fluorescence-activated cell sorting confirmed that PEA substitution at 3Hep2, but not at 6Hep2, is needed for optimal binding of MAb 2-1-L8. These data confirm that the MAb 2-1-L8 epitope requires a -3Hep2 cyclic PEA substitution for optimal conformation and that this MAb specifies the PEA-3Hep2 lactosyl LOS structure
conformation, monoclonal antibodies, epitopes, spectrometry, Neisseria gonorrhoeae, lipooligosaccharides, Binding Sites
NCBI PubMed ID: 18642671Journal NLM ID: 8202424Publisher: Mary Ann Liebert
Correspondence: dcstein@umd.edu
Institutions: Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, Maryland 20742, USA
Methods: PCR, SDS-PAGE, MALDI-TOF MS, serological methods, genetic methods, immunoblotting, fluorescence-activated cell sorter analysis
- 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: 34286971Publication DOI: 10.1021/acs.chemrev.0c01321Journal NLM ID: 2985134RPublisher: 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
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7. Compound ID: 527
a-D-GlcpNAc-(1-2)-+ b-D-Glcp-(1-4)-+ a-Kdop-(2-4)-+
| | |
EtN-(1--P--3)--L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/ |
Show graphically |
Structure type: oligomer
Aglycon: lipid A
Compound class: LOS, LPS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130659,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_151531,IEDB_175430,IEDB_2189047,IEDB_226300,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_983931,SB_192
The structure is contained in the following publication(s):
- Article ID: 107
Tong YH, Reinhold V, Reinhold B, Brandt B, Stein DC "Structural and immunochemical characterization of the lipooligosaccharides expressed by Neisseria subflava 44" -
Journal of Bacteriology 183(3) (2001) 942-950
Neisserial lipooligosaccharides (LOSs) are a family of complex cell surface glycolipids. We used mass spectrometry techniques (electrospray ionization, collision-induced dissociation, and multiple step), combined with fluorophore-assisted carbohydrate electrophoresis monosaccharide composition analysis, to determine the structure of the two low-molecular-mass LOS molecules (LOSI and LOSII) expressed by Neisseria subflava 44. We determined that LOSI contains one glucose on both the alpha and beta chains. LOSII is structurally related to LOSI and differs from it by the addition of a hexose (either glucose or galactose) on the alpha chain. LOSI and LOSII were able to bind monoclonal antibody (MAb) 25-1-LC1 when analyzed by Western blotting experiments. We used a set of genetically defined Neisseria gonorrhoeae mutants that expressed single defined LOS epitopes and a group of Neisseria meningitidis strains that expresses chemically defined LOS components to determine the structures recognized by MAb 25-1-LC1. We found that extensions onto the beta-chain glucose of LOSI block the recognition by this MAb, as does further elongation from the LOSII alpha chain. The LOSI structure was determined to be the minimum structure that is recognized by MAb 25-1-LC1.
Lipooligosaccharide, Neisseria, structural, characterization, immunochemical, lipooligosaccharides
NCBI PubMed ID: 11208793Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Correspondence: DS64@UMAIL.UMD.EDTJ
Institutions: Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, Maryland 20742
Methods: ESI-MS, CID-MS/MS, FACE
- Article ID: 3964
Wenzel CQ, St-Michael F, Stupak J, Li J, Cox AD, Richards JC "Functional characterization of Lpt3 and Lpt6, the inner-core lipooligosaccharide phosphoethanolamine transferases from Neisseria meningitidis" -
Journal of Bacteriology 192(1) (2010) 208-216
The lipooligosaccharide (LOS) of Neisseria meningitidis contains heptose (Hep) residues that are modified with phosphoethanolamine (PEtn) at the 3 (3-PEtn) and/or 6 (6-PEtn) position. The lpt3 (NMB2010) and lpt6 (NMA0408) genes of N. meningitidis, which are proposed to encode the required HepII 3- and 6-PEtn transferases, respectively, were cloned and overexpressed as C-terminally polyhistidine-tagged fusion proteins in Escherichia coli and found to localize to the inner membrane, based on sucrose density gradient centrifugation. Lpt3-His(6) and Lpt6-His(6) were purified from Triton X-100-solubilized membranes by nickel chelation chromatography, and dot blot analysis of enzymatic reactions with 3-PEtn- and 6-PEtn-specific monoclonal antibodies demonstrated conclusively that Lpt3 and Lpt6 are phosphatidylethanolamine-dependent LOS Hep.
lipopolysaccharides, Neisseria meningitidis, gene, Escherichia coli, antibodies, inner core, Ethanolaminephosphotransferase
NCBI PubMed ID: 19854897Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Correspondence: Cory.Wenzel@nrc-cnrc.gc.ca
Institutions: Institute for Biological Sciences, 100 Sussex Drive, National Research Council, Ottawa, ON, Canada K1A 0R6
Methods: DNA techniques, genetic methods, CE-MS
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8. Compound ID: 795
a-D-GlcpNAc-(1-2)-+
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EtN-(1--P--3)--L-gro-a-D-manHepp-(1-3)-+ a-Kdop-(2-4)-+
| |
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-Glcp-(1-4)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/ |
Show graphically |
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
The structure is contained in the following publication(s):
- 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: 8702594Journal NLM ID: 2985121RPublisher: 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
- 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: 15466050Journal NLM ID: 2985120RPublisher: 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
- 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: 34286971Publication DOI: 10.1021/acs.chemrev.0c01321Journal NLM ID: 2985134RPublisher: 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
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9. Compound ID: 1080
EtN-(1--P--6)--+ b-D-Glcp-(1-4)-+ a-Kdop-(2-4)-+
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EtN-(1--P--3)--L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/
|
a-D-GlcpNAc-(1-2)-+ |
Show graphically |
Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130659,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_151531,IEDB_175430,IEDB_2189047,IEDB_226300,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_419431,IEDB_983931,SB_192
The structure is contained in the following publication(s):
- Article ID: 328
Monteiro MA, Fortuna-Nevin M, Farley J, Pavliak V "Phase-variation of the truncated lipo-oligosaccharide of Neisseria meningitidis NMB phosphoglucomutase isogenic mutant NMB-R6" -
Carbohydrate Research 338(24) (2003) 2905-2912
The detection of antibodies specific to meningococcal lipo-oligosaccharides (LOSs; outer-core→inner-core→lipid A) in sera of patients convalescent from meningococcal infection suggests the potential use of LOS as a vaccine to combat pathogenic Neisseria spp. Removal of the outer-core region, which expresses glycans homologous to human blood-group antigens, is a required first-step in order to avoid undesirable immunological reactions following vaccination. To this end, we describe here the structural makeup of the LOS produced by serogroup B N. meningitidis NMB isogenic phosphoglucomutase (Pgm) mutant (NMB-R6). The dominant LOS types produced by NMB-R6 expressed a deep-truncated inner-core region, GlcNAc-(1→2)-LDHepII-(1→3)-LDHepI-(1→5)-[Kdo 2→4]-Kdo → lipid A, with one PEA unit attached at either O-6 or O-7 of LDHepII, or with two simultaneously PEA moieties attached at O-3 and O-6 or O-3 and O-7 of the same unit. Unexpectedly, this mutation did not completely deactivate the production of Glc, as some LOS molecules were observed to carry Glc at O-4 of LDHepI and at O-3 of LDHepII. A glycoconjugate vaccine comprised of NMB-R6 LOSs is currently being evaluated in our laboratory.
Phase variation, Lipooligosaccharide, Neisseria meningitidis, Neisseria, mutant, PAGE, 2-aminoethyl phosphate, phosphoglucomutase, vaccine, lipo-oligosaccharide, isogenic
NCBI PubMed ID: 14667712Journal NLM ID: 0043535Publisher: Elsevier
Institutions: Wyeth Vaccines Research, 211 Bailey Road, West Henrietta, NY 14586, USA
Methods: 1H NMR, GLC-MS, de-O-acylation, 31P NMR, ESI-MS, mild acid hydrolysis, PAGE
- Article ID: 789
Cox AD, Li J, Brisson J, Moxon ER, Richards JC "Structural analysis of the lipopolysaccharide from Neisseria meningitidis strain BZ157 galE: localisation of two phosphoethanolamine residues in the inner core oligosaccharide" -
Carbohydrate Research 337(16) (2002) 1435-1444
The structure of the phase-variable lipopolysaccharide (LPS) from the group B Neisseria meningitidis strain BZ157 galE was elucidated. The structural basis for the LPS's variation in reactivity with a monoclonal antibody (MAb) B5 that has specificity for the presence of phosphoethanolamine (PEtn) at the 3-position of the distal heptose residue (HepII) was established. The structure of the O-deacylated LPS was deduced by a combination of monosaccharide analyses, nuclear magnetic resonance (NMR) spectroscopy and mass spectrometry. These analyses revealed the presence of a novel inner core oligosaccharide (OS) structure in the MAb B5 reactive (B5+) LPS that contained two PEtn residues simultaneously substituting the 3- and 6-positions of the HepII residue. The determination of this structure has identified a further degree of variability within the inner core OS of meningococcal LPS that could contribute to the interaction of meningococcal strains with their host.
Lipopolysaccharide, oligosaccharide, core, Neisseria meningitidis, Neisseria, strain, structural, analysis, structural analysis, core oligosaccharide, inner core, phosphoethanolamine, galE, localisation
NCBI PubMed ID: 12204604Journal NLM ID: 0043535Publisher: Elsevier
Correspondence: andrew.cox@nrc.ca
Institutions: Institute for Biological Sciences, National Research Council, 100 Sussex Drive, Rm. 3089, Ottawa, ON, Canada K 1A 0R6, Institute for Molecular Medicine, John Radcliffe Hospital, University of Oxford, Oxford OX3 9DU, UK
Methods: NMR, sugar analysis, MS
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10. Compound ID: 1081
EtN-(1--P--7)--+ b-D-Glcp-(1-4)-+ a-Kdop-(2-4)-+
| | |
EtN-(1--P--3)--L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/
|
a-D-GlcpNAc-(1-2)-+ |
Show graphically |
Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130659,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_151531,IEDB_175430,IEDB_2189047,IEDB_226300,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_983931,SB_192
The structure is contained in the following publication(s):
- Article ID: 328
Monteiro MA, Fortuna-Nevin M, Farley J, Pavliak V "Phase-variation of the truncated lipo-oligosaccharide of Neisseria meningitidis NMB phosphoglucomutase isogenic mutant NMB-R6" -
Carbohydrate Research 338(24) (2003) 2905-2912
The detection of antibodies specific to meningococcal lipo-oligosaccharides (LOSs; outer-core→inner-core→lipid A) in sera of patients convalescent from meningococcal infection suggests the potential use of LOS as a vaccine to combat pathogenic Neisseria spp. Removal of the outer-core region, which expresses glycans homologous to human blood-group antigens, is a required first-step in order to avoid undesirable immunological reactions following vaccination. To this end, we describe here the structural makeup of the LOS produced by serogroup B N. meningitidis NMB isogenic phosphoglucomutase (Pgm) mutant (NMB-R6). The dominant LOS types produced by NMB-R6 expressed a deep-truncated inner-core region, GlcNAc-(1→2)-LDHepII-(1→3)-LDHepI-(1→5)-[Kdo 2→4]-Kdo → lipid A, with one PEA unit attached at either O-6 or O-7 of LDHepII, or with two simultaneously PEA moieties attached at O-3 and O-6 or O-3 and O-7 of the same unit. Unexpectedly, this mutation did not completely deactivate the production of Glc, as some LOS molecules were observed to carry Glc at O-4 of LDHepI and at O-3 of LDHepII. A glycoconjugate vaccine comprised of NMB-R6 LOSs is currently being evaluated in our laboratory.
Phase variation, Lipooligosaccharide, Neisseria meningitidis, Neisseria, mutant, PAGE, 2-aminoethyl phosphate, phosphoglucomutase, vaccine, lipo-oligosaccharide, isogenic
NCBI PubMed ID: 14667712Journal NLM ID: 0043535Publisher: Elsevier
Institutions: Wyeth Vaccines Research, 211 Bailey Road, West Henrietta, NY 14586, USA
Methods: 1H NMR, GLC-MS, de-O-acylation, 31P NMR, ESI-MS, mild acid hydrolysis, PAGE
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11. Compound ID: 1549
a-D-GlcpNAc-(1-2)-+ b-D-Glcp-(1-4)-+ a-Kdop-(2-4)-+
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EtN-(1--P--3)--L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-Kdo |
Show graphically |
Structure type: oligomer
Trivial name: inner core region
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130659,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_151531,IEDB_175430,IEDB_2189047,IEDB_226300,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_983931,SB_192
The structure is contained in the following publication(s):
- Article ID: 478
Gidney MA, Plested JS, Lacelle S, Coull PA, Wright JC, Makepeace K, Brisson JR, Cox AD, Moxon ER, Richards JC "Development, characterization, and functional activity of a panel of specific monoclonal antibodies to inner core lipopolysaccharide epitopes in Neisseria meningitidis" -
Infection and Immunity 72(1) (2004) 559-569
A panel of six murine monoclonal antibodies (MAbs) recognizing inner core lipopolysaccharide (LPS) epitopes of Neisseria meningitidis was prepared and characterized in order to determine the diversity of inner core LPS glycoforms among disease and carrier isolates. Two of these MAbs, L2-16 (immunoglobulin G2b [IgG2b]) and LPT3-1 (IgG2a), together with a third, previously described MAb, L3B5 (IgG3), showed reactivity, either individually or in combination, with all except 3 of 143 disease and carriage isolates (125 of 126 strains from blood, cerebrospinal fluid, or skin biopsy samples and 15 of 17 from nasopharyngeal cultures). MAbs L3B5, L2-16, and LPT3-1 were further characterized in an indirect immunofluorescence assay. All three MAbs bound to the bacterial cell surface, findings that correlated strongly with whole-cell enzyme-linked immunosorbent assay and immunodot blots. However, in contrast to our findings with L3B5, cell surface binding of L2-16 or LPT 3-1 did not correlate with functional activity as determined by bactericidal or infant rat passive protection assays against wild-type N. meningitidis strains. These findings are provocative with respect to the requirements for protective activity of antibodies and the development of inner core LPS vaccines against invasive meningococcal disease.
Lipopolysaccharide, Neisseria meningitidis, Neisseria, monoclonal antibodies, epitopes, inner core, vaccines, diversity
NCBI PubMed ID: 14688137Journal NLM ID: 0246127Publisher: American Society for Microbiology
Correspondence: margaretanne.gidney@nrc-cnrc.gc.ca
Institutions: Institute for Biological Sciences, National Research Council, Ottawa, ON, K1A OR6, Canada
Methods: NMR, ESI-MS
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12. Compound ID: 1554
EtN-(1--P--6)--+ b-D-Glcp-(1-4)-+ a-Kdop-(2-4)-+
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EtN-(1--P--3)--L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-Kdo
|
a-D-GlcpNAc-(1-2)-+ |
Show graphically |
Structure type: oligomer
Trivial name: inner core region
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130659,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_151531,IEDB_175430,IEDB_2189047,IEDB_226300,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_419431,IEDB_983931,SB_192
The structure is contained in the following publication(s):
- Article ID: 478
Gidney MA, Plested JS, Lacelle S, Coull PA, Wright JC, Makepeace K, Brisson JR, Cox AD, Moxon ER, Richards JC "Development, characterization, and functional activity of a panel of specific monoclonal antibodies to inner core lipopolysaccharide epitopes in Neisseria meningitidis" -
Infection and Immunity 72(1) (2004) 559-569
A panel of six murine monoclonal antibodies (MAbs) recognizing inner core lipopolysaccharide (LPS) epitopes of Neisseria meningitidis was prepared and characterized in order to determine the diversity of inner core LPS glycoforms among disease and carrier isolates. Two of these MAbs, L2-16 (immunoglobulin G2b [IgG2b]) and LPT3-1 (IgG2a), together with a third, previously described MAb, L3B5 (IgG3), showed reactivity, either individually or in combination, with all except 3 of 143 disease and carriage isolates (125 of 126 strains from blood, cerebrospinal fluid, or skin biopsy samples and 15 of 17 from nasopharyngeal cultures). MAbs L3B5, L2-16, and LPT3-1 were further characterized in an indirect immunofluorescence assay. All three MAbs bound to the bacterial cell surface, findings that correlated strongly with whole-cell enzyme-linked immunosorbent assay and immunodot blots. However, in contrast to our findings with L3B5, cell surface binding of L2-16 or LPT 3-1 did not correlate with functional activity as determined by bactericidal or infant rat passive protection assays against wild-type N. meningitidis strains. These findings are provocative with respect to the requirements for protective activity of antibodies and the development of inner core LPS vaccines against invasive meningococcal disease.
Lipopolysaccharide, Neisseria meningitidis, Neisseria, monoclonal antibodies, epitopes, inner core, vaccines, diversity
NCBI PubMed ID: 14688137Journal NLM ID: 0246127Publisher: American Society for Microbiology
Correspondence: margaretanne.gidney@nrc-cnrc.gc.ca
Institutions: Institute for Biological Sciences, National Research Council, Ottawa, ON, K1A OR6, Canada
Methods: NMR, ESI-MS
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13. Compound ID: 3075
b-D-Galp-(1-4)-b-D-Galp-(1-4)-b-D-Glcp-(1-4)-+
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a-D-GlcpNAc-(1-2)-+ | a-Kdop-(2-4)-+
| | |
EtN-(1--P--3)--L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/ |
Show graphically |
Structure type: oligomer
Aglycon: lipid A
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130659,IEDB_136044,IEDB_137472,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_146664,IEDB_151531,IEDB_175430,IEDB_190606,IEDB_2189047,IEDB_221845,IEDB_226300,IEDB_418765,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_6,SB_7,SB_88
The structure is contained in the following publication(s):
- 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: 10496924Journal NLM ID: 0246127Publisher: 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
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14. Compound ID: 3076
a-D-GlcpNAc-(1-2)-+
|
EtN-(1--P--3)--L-gro-a-D-manHepp-(1-3)-+ a-Kdop-(2-4)-+
| |
a-Neu5Ac-(2-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-Glcp-(1-4)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/ |
Show graphically |
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
The structure is contained in the following publication(s):
- 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: 10496924Journal NLM ID: 0246127Publisher: 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
- 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.2014.11.016Journal NLM ID: 9500160Publisher: 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
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15. Compound ID: 3601
a-D-GlcNAc-(1-2)-+
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EtN-(1--P--3)--L-gro-a-D-manHepp-(1-3)-+ a-Kdop-(2-4)-+
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a-Neup5Ac-(2-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-Glcp-(1-4)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/ |
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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
The structure is contained in the following publication(s):
- 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: 11854213Journal NLM ID: 0246127Publisher: 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
- 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: 9281472Publication DOI: 10.1006/mpat.1997.0143Journal NLM ID: 8606191Publisher: 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
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