Found 8 structures.
Displayed structures from 1 to 8
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1. Compound ID: 1082
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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)-+ |
Show graphically |
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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2. Compound ID: 1502
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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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3. Compound ID: 1506
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-Glcp-(1-4)-+
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a-D-GlcpNAc-(1-2)-+ | 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)-+ |
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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4. Compound ID: 3642
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b-D-GalpNAc-(1-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-Glcp-(1-4)-+
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EtN-(1--P--?)--+ | a-Kdop-(2-4)-+
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b-D-Galp-(1-4)-a-D-Glcp-(1-3)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/
| |
a-D-GlcpNAc-(1-2)-+ EtN-(1--P--?)--+ |
Show graphically |
Structure type: oligomer
Aglycon: lipid A
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130646,IEDB_130648,IEDB_130650,IEDB_130659,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137473,IEDB_137776,IEDB_1391966,IEDB_139427,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_149144,IEDB_151531,IEDB_175430,IEDB_190606,IEDB_2189047,IEDB_226300,IEDB_418761,IEDB_418762,IEDB_418763,IEDB_418764,IEDB_418765,IEDB_418766,IEDB_418767,IEDB_418768,IEDB_418769,IEDB_418770,IEDB_419428,IEDB_419429,IEDB_419430,IEDB_419431,IEDB_419432,IEDB_983931,SB_145,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_21,SB_30,SB_6,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 1363
Banerjee A, Wang R, Uljon SN, Rice PA, Gotschlich EC, Stein DC "Identification of the gene (lgtG) encoding the lipooligosaccharide b chain synthesizing glucosyl transferase from Neisseria gonorrhoeae" -
Proceedings of the National Academy of Sciences of the USA 95(18) (1998) 10872-10877
The lipooligosaccharide from Neisseria gonorrhoeae (GC), consists of lipid A, an oligosaccharide core and three branches, alpha, beta, and gamma. We report the cloning of the gene (lgtG, lipooligosaccharide glycosyl transferase G) encoding the glucosyl transferase of GC that initiates the beta chain which consists of a lactosyl moiety. This gene contains a homopolymeric tract of cytidine [poly(C)] and we demonstrate that changes in the number of Cs in poly(C) account for the variation of beta chain expression in different GC strains. Biochemical analyses and mass spectrometry clearly attribute the reactivity of mAb 2C7 to the presence of the lactosyl beta chain. In addition, we demonstrate that in the absence of the lactosyl group, a phosphoethanolamine is added to generate a new antigenic epitope as evidenced by the gain of reactivity to mAb 2-L1-8. These results show that, like the alpha chain, the beta chain of lipooligosaccharide is subject to antigenic variation.
Lipooligosaccharide, gene, Neisseria, identification, transferase, Gonorrhoeae, Neisseria gonorrhoeae
NCBI PubMed ID: 9724797Journal NLM ID: 7505876Publisher: National Academy of Sciences
Correspondence: ecg@rockvax.rockefeller.edu
Institutions: Department of Microbiology, University of Maryland, College Park
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5. Compound ID: 3643
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a-D-Galp-(1-4)-b-D-Galp-(1-4)-b-D-Glcp-(1-4)-+
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EtN-(1--P--?)--+ | a-Kdop-(2-4)-+
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b-D-Galp-(1-4)-a-D-Glcp-(1-3)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/
| |
a-D-GlcpNAc-(1-2)-+ EtN-(1--P--?)--+ |
Show graphically |
Structure type: oligomer
Aglycon: lipid A
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130651,IEDB_130659,IEDB_136044,IEDB_136906,IEDB_137472,IEDB_1391964,IEDB_139427,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_144987,IEDB_144998,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_419430,IEDB_419431,IEDB_419432,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: 1363
Banerjee A, Wang R, Uljon SN, Rice PA, Gotschlich EC, Stein DC "Identification of the gene (lgtG) encoding the lipooligosaccharide b chain synthesizing glucosyl transferase from Neisseria gonorrhoeae" -
Proceedings of the National Academy of Sciences of the USA 95(18) (1998) 10872-10877
The lipooligosaccharide from Neisseria gonorrhoeae (GC), consists of lipid A, an oligosaccharide core and three branches, alpha, beta, and gamma. We report the cloning of the gene (lgtG, lipooligosaccharide glycosyl transferase G) encoding the glucosyl transferase of GC that initiates the beta chain which consists of a lactosyl moiety. This gene contains a homopolymeric tract of cytidine [poly(C)] and we demonstrate that changes in the number of Cs in poly(C) account for the variation of beta chain expression in different GC strains. Biochemical analyses and mass spectrometry clearly attribute the reactivity of mAb 2C7 to the presence of the lactosyl beta chain. In addition, we demonstrate that in the absence of the lactosyl group, a phosphoethanolamine is added to generate a new antigenic epitope as evidenced by the gain of reactivity to mAb 2-L1-8. These results show that, like the alpha chain, the beta chain of lipooligosaccharide is subject to antigenic variation.
Lipooligosaccharide, gene, Neisseria, identification, transferase, Gonorrhoeae, Neisseria gonorrhoeae
NCBI PubMed ID: 9724797Journal NLM ID: 7505876Publisher: National Academy of Sciences
Correspondence: ecg@rockvax.rockefeller.edu
Institutions: Department of Microbiology, University of Maryland, College Park
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6. Compound ID: 8766
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a-Neup5Ac-(2-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-+
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a-D-GlcpNAc-(1-2)-+ | 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)-+ |
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_139427,IEDB_140088,IEDB_140089,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146100,IEDB_146664,IEDB_149174,IEDB_150933,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_418769,IEDB_423120,IEDB_983931,SB_115,SB_116,SB_131,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_187,SB_192,SB_195,SB_30,SB_39,SB_68,SB_7,SB_84,SB_88
The structure is contained in the following publication(s):
- Article ID: 3803
Weynants V, Denoel P, Devos N, Janssens D, Feron C, Goraj K, Momin P, Monnom D, Tans C, Vandercammen A, Wauters F, Poolman JT "Genetically modified L3,7 and L2 lipooligosaccharides from Neisseria meningitidis serogroup B confer a broad cross-bactericidal response" -
Infection and Immunity 77(5) (2009) 2084-2093
Currently available Neisseria meningitidis serogroup B (MenB) vaccines are based on outer membrane vesicles (OMVs) that are obtained from wild-type strains. They are purified with the aim of decreasing the lipooligosaccharide (LOS) content and hence reduce the reactogenicity of the vaccine even though LOS is a potential protective antigen. In <2-year-old children, these MenB vaccines confer protection only against strains expressing homologous PorA, a major and variable outer membrane protein. Our objective was to develop a safe LOS-based vaccine against MenB. To this end, we used modified porA knockout strains expressing genetically detoxified (msbB gene-deleted) L2 and L3,7 LOSs, allowing the production of LOS-enriched OMVs. The vaccine-induced antibodies were found to be bactericidal against nearly all invasive strains, irrespective of capsular serogroup. In addition, we have also demonstrated that LOS lacking the terminal galactose (with a lgtB mutation; truncated L3 LOS), but not LOS produced without the galE gene, induced a bactericidal antibody response in mice similar to that seen for LOS containing the full lacto-N-neotetraose (L3,7 LOS). In conclusion, a bivalent detoxified LOS OMV-based vaccine demonstrated the potential to afford a broad cross-protection against meningococcal disease.
Neisseria meningitidis, gene, antibody response, lipooligosaccharides, lacto-N-neotetraose, serogroup B
NCBI PubMed ID: 19289516Journal NLM ID: 0246127Publisher: American Society for Microbiology
Correspondence: jan.poolman@gskbio.com
Institutions: Research & Development, GlaxoSmithKline Biologicals, Rue de l'Institut 89, B-1330 Rixensart, Belgium
Methods: ELISA, serological methods, genetic methods, statistical analysis
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7. Compound ID: 9004
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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)-+
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a-D-Glcp-(1-3)-+ |
| |
/Variants 0/-+ | | a-Kdop-(2-4)-+
| | | |
EtN-(1--P--6)--L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-Kdop-(2--/lipid A/
|
a-D-GlcpNAc-(1-2)-+
/Variants 0/ is:
EtN-(1--P--7)--
OR (exclusively)
Gly-(1-7)- |
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_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_146100,IEDB_146664,IEDB_149144,IEDB_149174,IEDB_150933,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_226300,IEDB_418762,IEDB_418764,IEDB_418767,IEDB_418769,IEDB_419429,IEDB_419430,IEDB_419431,IEDB_419432,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: 3868
Kabanov DS, Prokhorenko IR "Structural analysis of lipopolysaccharides from Gram-negative bacteria" -
Biochemistry (Moscow) 75(4) (2010) 383-404
This review covers data on composition and structure of lipid A, core, and O-polysaccharide of the known lipopolysaccharides from Gram-negative bacteria. The relationship between the structure and biological activity of lipid A is discussed. The data on roles of core and O-polysaccharide in biological activities of lipopolysaccharides are presented. The structural homology of some oligosaccharide sequences of lipopolysaccharides to gangliosides of human cell membranes is considered.
core, Lipooligosaccharide, O-antigen, lipid A, gangliosides, cytokines, lipopolysaccharide (endotoxin)
NCBI PubMed ID: 20618127Publication DOI: 10.1134/S0006297910040012Journal NLM ID: 0376536Publisher: Nauka/Interperiodica
Correspondence: kabanovd1@rambler.ru
Institutions: Institute of Basic Biological Problems, Russian Academy of Sciences, Pushchino, Russia
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8. Compound ID: 15673
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b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-4)-b-D-Glcp-(1-4)-+
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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/
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a-D-Glcp-(1-3)-+
/Variants 0/ is:
EtN-(1--P--7)--
OR (exclusively)
EtN-(1--P--6)-- |
Show graphically |
Structure type: oligomer
Aglycon: lipid A
Trivial name: core oligosaccharide L2
Compound class: 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: 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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