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1. Compound ID: 1078
a-D-GlcpNAc-(1-2)-+ b-D-Glcp-(1-4)-+ a-Kdop-(2-4)-+
| | |
EtN-(1--P--6)--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, 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_2189047,IEDB_226300,IEDB_418767,IEDB_418769,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: 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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2. 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/
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a-D-GlcpNAc-(1-2)-+ |
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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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3. Compound ID: 1082
a-D-GlcpNAc-(1-2)-+ b-D-Glcp-(1-4)-+ a-Kdop-(2-4)-+
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EtN-(1--P--6)--L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/
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a-D-Glcp-(1-3)-+ |
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Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130659,IEDB_139427,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151531,IEDB_2189047,IEDB_226300,IEDB_418767,IEDB_418769,IEDB_419429,IEDB_419430,IEDB_419431,IEDB_419432,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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4. Compound ID: 1087
a-D-GlcpNAc-(1-2)-+ b-D-Glcp-(1-4)-+
| |
EtN-(1--P--6)--L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-Kdo |
Show graphically |
Structure type: oligomer
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_151531,IEDB_2189047,IEDB_418767,IEDB_418769,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
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5. Compound ID: 1089
EtN-(1--P--6)--+ b-D-Glcp-(1-4)-+
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EtN-(1--P--3)--L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-Kdo
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a-D-GlcpNAc-(1-2)-+ |
Show graphically |
Structure type: oligomer
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_151531,IEDB_2189047,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
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6. Compound ID: 1091
a-D-GlcpNAc-(1-2)-+ b-D-Glcp-(1-4)-+
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EtN-(1--P--6)--L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-Kdo
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a-D-Glcp-(1-3)-+ |
Show graphically |
Structure type: oligomer
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151531,IEDB_2189047,IEDB_418767,IEDB_418769,IEDB_419429,IEDB_419430,IEDB_419431,IEDB_419432,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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7. Compound ID: 1201
a-D-GlcpNAc-(1-2)-+
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EtN-(1--P--6)--L-gro-a-D-manHepp-(1-3)-+
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b-D-Glcp-(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
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
The structure is contained in the following publication(s):
- 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: 11496013Journal NLM ID: 0376646Publisher: 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
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8. Compound ID: 1502
a-D-GlcpNAc-(1-2)-+ b-D-Glcp-(1-4)-+ a-Kdop-(2-4)-+
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EtN-(1--P--6)--L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-Kdo
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a-D-Glcp-(1-3)-+ |
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_139427,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151531,IEDB_2189047,IEDB_226300,IEDB_418767,IEDB_418769,IEDB_419429,IEDB_419430,IEDB_419431,IEDB_419432,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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9. Compound ID: 1506
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-Glcp-(1-4)-+
|
a-D-GlcpNAc-(1-2)-+ | a-Kdop-(2-4)-+
| | |
EtN-(1--P--6)--L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/
|
a-D-Glcp-(1-3)-+ |
Show graphically |
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
The structure is contained in the following publication(s):
- 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: 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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10. Compound ID: 1550
a-D-GlcpNAc-(1-2)-+ b-D-Glcp-(1-4)-+ a-Kdop-(2-4)-+
| | |
EtN-(1--P--6)--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_2189047,IEDB_226300,IEDB_418767,IEDB_418769,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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11. Compound ID: 1554
EtN-(1--P--6)--+ 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)-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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12. Compound ID: 1555
a-D-GlcpNAc-(1-2)-+
|
EtN-(1--P--6)--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
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_190606,IEDB_2189047,IEDB_226300,IEDB_418762,IEDB_418764,IEDB_418767,IEDB_418769,IEDB_419429,IEDB_419431,IEDB_983931,SB_145,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_6,SB_7,SB_88
The structure is contained in the following publication(s):
- 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: 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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13. Compound ID: 1686
a-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--6)--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
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130651,IEDB_130659,IEDB_136044,IEDB_136906,IEDB_137472,IEDB_1391964,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_144987,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_152217,IEDB_190606,IEDB_2189047,IEDB_226300,IEDB_418767,IEDB_418769,IEDB_419429,IEDB_419431,IEDB_423106,IEDB_742247,IEDB_983931,SB_165,SB_166,SB_167,SB_178,SB_187,SB_192,SB_195,SB_31,SB_6,SB_62,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 521
St-Michael F, Howard MD, Li J, Duncan J, Inzana TJ, Cox AD "Structural analysis of the lipooligosaccharide from the commensal Haemophilus somnus genome strain 129Pt" -
Carbohydrate Research 339 (2004) 529-535
The structure for the carbohydrate moiety of the lipooligosaccharide (LOS) from the commensal Haemophilus somnus strain 129Pt was elucidated. The structure of the core oligosaccharide and O-deacylated LOS was established by monosaccharide and methylation analyses, NMR spectroscopy and mass spectrometry. The following structure for the major fully extended carbohydrate glycoform of the LOS was determined on the basis of the combined data from these experiments. In the structure Kdo is 3-deoxy-D-manno-octulosonic acid, Hep is L-glycero-D-manno-heptose and PEtn is phosphoethanolamine. Minor amounts of glycoforms containing nonstoichiometric substituents glycine and phosphate at the distal heptose residue were also identified.
NMR, Lipooligosaccharide, mass spectrometry, Haemophilus somnus, Commensal
NCBI PubMed ID: 15013390Journal NLM ID: 0043535Publisher: Elsevier
Correspondence: andrew.cox@nrc-cnrc.gc.ca
Institutions: Institute for Biological Sciences, National Research Council, 100 Sussex Drive, Room 3101, Ottawa, ON, Canada K1A 0R6, Centre for Molecular Medicine and Infectious Diseases, Virginia Polytechnic Institute and State University, Blacksburg, VA 24061-0342, USA
Methods: NMR-2D, methylation, NMR, sugar analysis, MS
- Article ID: 982
McQuiston JH, McQuiston JR, Cox AD, Wu YP, Boyle SM, Inzana TJ "Characterization of a DNA region containing 5'-(CAAT)n-3' DNA sequences involved in lipooligosaccharide biosynthesis in Haemophilus somnus" -
Microbial Pathogenesis 28(5) (2000) 301-312
biosynthesis, Haemophilus, Phase variation, Lipooligosaccharide, DNA, characterization, region, sequence, Haemophilus somnus
Journal NLM ID: 8606191Publisher: Academic Press
Correspondence: tinzana@vt.edu
Institutions: Center for Molecular Medicine and Infectious Diseases, Virginia-Maryland Regional College of Veterinary Madicine,Blacksburg,U.S.A.
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14. Compound ID: 2198
Lau-(1-3)-3HOMyr-(1-2)-+
|
Lau-(1-3)-3HOMyr-(1-2)-+ |
| |
a-Neup5Ac-(2-3)-b-D-Galp-(1-4)-b-D-GlcNAc-(1-3)-b-D-Galp-(1-4)-b-D-Glcp-(1-4)-+ | |
| | |
b-D-Glcp-(1-3)-+ | | |
| | | |
EtN-(1--P--7)--+ | | a-Kdop-(2-4)-+ | |
| | | | | |
EtN-(1--P--6)--L-gro-a-D-manHep-(1-3)-L-gro-a-D-manHep-(1-5)-a-Kdop-(2-6)-b-D-GlcpN-(1-6)-a-D-GlcpN-(1-P
| | |
a-D-GlcNAc-(1-2)-+ 3HOLau-(1-3)-+ 3HOLau-(1-3)-+ |
Show graphically |
Structure type: oligomer
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_534864,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: 712
Kahler CM, Martin LE, Shih GC, Rahman MM, Carlson RW, Stephens DS "The (a2->8)-linked polisyalic acid capsule and lipooligosaccharide structure both contribute to the ability of serogroup B Neisseria meningitidis to resist the bactericidal activity of normal human serum" -
Infection and Immunity 66(12) (1998) 5939-5947
The molecular basis for the resistance of serogroup B Neisseria meningitidis to the bactericidal activity of normal human sera (NHS) was examined with a NHS-resistant, invasive serogroup B meningococcal isolate and genetically and structurally defined capsule-, lipooligosaccharide (LOS)-, and sialylation-altered mutants of the wild-type strain. Expression of the (α2→8)-linked polysialic acid serogroup B capsule was essential for meningococcal resistance to NHS. The very NHS-sensitive phenotype of acapsular mutants (99.9 to 100% killed in 10, 25, and 50% NHS) was not rescued by complete LOS sialylation or changes in LOS structure. However, expression of the capsule was necessary but not sufficient for a fully NHS-resistant phenotype. In an encapsulated background, loss of LOS sialylation by interrupting the α2,3 sialyltransferase gene, lst, increased sensitivity to 50% NHS. In contrast, replacement of the lacto-N-neotetraose alpha-chain (Galβ1-4GlcNAcβ1-3Galβ1-4Glc) with glucose extensions (GlcN) in a galE mutant resulted in a strain resistant to killing by 50% NHS at all time points. Encapsulated meningococci expressing a Hep2(GlcNAc)→KDO2→lipid A LOS without an alpha-chain demonstrated enhanced sensitivity to 50% NHS (98% killed at 30 min) mediated through the antibody-dependent classical complement pathway. Encapsulated LOS mutants expressing truncated Hep2→KDO2→lipid A and KDO2→lipid A structures were also sensitive to 50% NHS (98 to 100% killed at 30 min) but, unlike the wild-type strain and mutants with larger oligosaccharide structures, they were killed by hypogammaglobulinemic sera. These data indicate that encapsulation is essential but that the LOS structure contributes to the ability of serogroup B N. meningitidis to resist the bactericidal activity of NHS.
structure, core, Lipooligosaccharide, Neisseria meningitidis, human, LOS, Neisseria, acid, serogroup, activity, capsule, CPS, serum, bactericidal, serogroup B, ability, bactericidal activity, human serum, polysialic acid
NCBI PubMed ID: 9826376Journal NLM ID: 0246127Publisher: American Society for Microbiology
Correspondence: dstep01@emory.edu
Institutions: Division of Infectious Diseases, Department of Medicine, Atlanta, GA, USA
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15. Compound ID: 2200
Lau-(1-3)-3HOMyr-(1-2)-+
|
Lau-(1-3)-3HOMyr-(1-2)-+ |
| |
b-D-Glcp-(1-4)-b-D-Glcp-(1-4)-+ | |
| | |
b-D-Glcp-(1-3)-+ | | |
| | | |
EtN-(1--P--7)--+ | | a-Kdop-(2-4)-+ | |
| | | | | |
EtN-(1--P--6)--L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2-6)-b-D-GlcpN-(1-6)-a-D-GlcpN-(1-P
| | |
a-D-GlcNAc-(1-2)-+ 3HOLau-(1-3)-+ 3HOLau-(1-3)-+ |
Show graphically |
Structure type: oligomer
Compound class: LOS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130659,IEDB_137340,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_151531,IEDB_2189047,IEDB_226300,IEDB_418767,IEDB_418769,IEDB_419429,IEDB_419431,IEDB_534864,IEDB_983931,SB_192
The structure is contained in the following publication(s):
- Article ID: 712
Kahler CM, Martin LE, Shih GC, Rahman MM, Carlson RW, Stephens DS "The (a2->8)-linked polisyalic acid capsule and lipooligosaccharide structure both contribute to the ability of serogroup B Neisseria meningitidis to resist the bactericidal activity of normal human serum" -
Infection and Immunity 66(12) (1998) 5939-5947
The molecular basis for the resistance of serogroup B Neisseria meningitidis to the bactericidal activity of normal human sera (NHS) was examined with a NHS-resistant, invasive serogroup B meningococcal isolate and genetically and structurally defined capsule-, lipooligosaccharide (LOS)-, and sialylation-altered mutants of the wild-type strain. Expression of the (α2→8)-linked polysialic acid serogroup B capsule was essential for meningococcal resistance to NHS. The very NHS-sensitive phenotype of acapsular mutants (99.9 to 100% killed in 10, 25, and 50% NHS) was not rescued by complete LOS sialylation or changes in LOS structure. However, expression of the capsule was necessary but not sufficient for a fully NHS-resistant phenotype. In an encapsulated background, loss of LOS sialylation by interrupting the α2,3 sialyltransferase gene, lst, increased sensitivity to 50% NHS. In contrast, replacement of the lacto-N-neotetraose alpha-chain (Galβ1-4GlcNAcβ1-3Galβ1-4Glc) with glucose extensions (GlcN) in a galE mutant resulted in a strain resistant to killing by 50% NHS at all time points. Encapsulated meningococci expressing a Hep2(GlcNAc)→KDO2→lipid A LOS without an alpha-chain demonstrated enhanced sensitivity to 50% NHS (98% killed at 30 min) mediated through the antibody-dependent classical complement pathway. Encapsulated LOS mutants expressing truncated Hep2→KDO2→lipid A and KDO2→lipid A structures were also sensitive to 50% NHS (98 to 100% killed at 30 min) but, unlike the wild-type strain and mutants with larger oligosaccharide structures, they were killed by hypogammaglobulinemic sera. These data indicate that encapsulation is essential but that the LOS structure contributes to the ability of serogroup B N. meningitidis to resist the bactericidal activity of NHS.
structure, core, Lipooligosaccharide, Neisseria meningitidis, human, LOS, Neisseria, acid, serogroup, activity, capsule, CPS, serum, bactericidal, serogroup B, ability, bactericidal activity, human serum, polysialic acid
NCBI PubMed ID: 9826376Journal NLM ID: 0246127Publisher: American Society for Microbiology
Correspondence: dstep01@emory.edu
Institutions: Division of Infectious Diseases, Department of Medicine, Atlanta, GA, USA
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