Found 78 structures.
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1. Compound ID: 98
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L-gro-a-D-manHepp-(1-7)-+
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a-D-Galp-(1-6)-+ | a-Kdop-(2-4)-+
| | |
a-D-GlcpNAc-(1-2)-a-D-Glcp-(1-2)-a-D-Galp-(1-3)-a-D-Galp-(1-3)-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: LPS
Contained glycoepitopes: IEDB_115013,IEDB_130645,IEDB_130650,IEDB_130659,IEDB_130670,IEDB_130693,IEDB_134624,IEDB_136906,IEDB_137472,IEDB_140088,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_226811,IEDB_742246,IEDB_918313,IEDB_983931,SB_163,SB_192,SB_7,SB_87
The structure is contained in the following publication(s):
- Article ID: 18
Borrelli S, Hegedus O, Shaw DH, Jansson P, Lindberg AA "The tetrasaccharide L-a-D-heptose1->2-L-a-D-heptose1->3-L-a-D-heptose1->(3-deoxy-D-manno-octulosonic acid) and phosphate in lipid A define the conserved epitope in Haemophilus lipopolysaccharides recognized by a monoclonal antibody" -
Infection and Immunity 63 (1995) 3683-3692
A murine monoclonal antibody, MAHI 3 (immunoglobulin G2b), that is broadly reactive with Haemophilus influenzae lipopolysaccharides (LPSs) but nonreactive with all enterobacterial LPSs tested was generated by fusing mouse myeloma cells with spleen cells of BALB/c mice immunized with azide-killed H. influenzae RM.7004. MAHI 3 bound to all H. influenzae, all other human Haemophilus spp., all Bordetella pertussis and Bordetella parapertussis, and all Aeromonas spp. tested but not to any Neisseria or Moraxella catarrhalis strains, as determined by enzyme immunoassay, colony dot immunoblotting, and immunoblotting. In an inhibition enzyme immunoassay, MAHI 3 reacted with all 45 H. influenzae LPSs tested but not with the LPS from the rough mutant I69 Rd-/b+, which has only 3-deoxy-D-manno-octulosonic acid (P) [Kdop(P)] and lipid A. The antibody was not inhibited by H. influenzae lipid A or lipid-free polysaccharide isolated after mild acid hydrolysis. Only native LPSs show positive inhibitory activity, indicating that part of lipid A is involved in the binding of MAHI 3. From the results, it is indicated that the structural element recognized by MAHI 3 is Hep α1→2 Hep α1→3 Hep α1→ Kdo together with part of lipid A, including the phosphate
Lipopolysaccharide, Haemophilus, L-glycero-D-manno-heptose, lipopolysaccharides, LPS, core, tetrasaccharide, acid, Kdo, antibodies, antibody, conserved, epitope, lipid, lipid A, monoclonal, monoclonal antibodies, monoclonal antibody, phosphate, recognition
NCBI PubMed ID: 7543887Journal NLM ID: 0246127Publisher: American Society for Microbiology
Correspondence: Pererk.Jansson@kfc.m13.hs.sll.se
Institutions: Department of Immunology, Microbiology, Pathology and Infectious Diseases, Karolinska Institute, Huddinge, Sweden
Methods: de-O-acylation, SDS-PAGE, alkaline de-O-N-acylation, dephosphorylation, chemical analysis, EIA, inhibition studies, dot immunoblotting
- Article ID: 4317
Huang JX, Azad MA, Yuriev E, Baker MA, Nation RL, Li J, Cooper MA, Velkov T "Molecular Characterization of Lipopolysaccharide Binding to Human a-1-Acid Glycoprotein" -
Journal of Lipids 2012 (2012) 475153
The ability of AGP to bind circulating lipopolysaccharide (LPS) in plasma is believed to help reduce the proinflammatory effect of bacterial lipid A molecules. Here, for the first time we have characterized human AGP binding characteristics of the LPS from a number of pathogenic Gram-negative bacteria: Escherichia coli, Salmonella typhimurium, Klebsiella pneumonia, Pseudomonas aeruginosa, and Serratia marcescens. The binding affinity and structure activity relationships (SAR) of the AGP-LPS interactions were characterized by surface plasma resonance (SPR). In order to dissect the contribution of the lipid A, core oligosaccharide and O-antigen polysaccharide components of LPS, the AGP binding affinity of LPS from smooth strains, were compared to lipid A, Kdo2-lipid A, R(a), R(d), and R(e) rough LPS mutants. The SAR analysis enabled by the binding data suggested that, in addition to the important role played by the lipid A and core components of LPS, it is predominately the unique species- and strain-specific carbohydrate structure of the O-antigen polysaccharide that largely determines the binding affinity for AGP. Together, these data are consistent with the role of AGP in the binding and transport of LPS in plasma during acute-phase inflammatory responses to invading Gram-negative bacteria.
O-antigen, lipid A, gram negative bacteria, lipopolysaccharide-binding, AGP binding, SPR
NCBI PubMed ID: 23316371Publication DOI: 10.1155/2012/475153Journal NLM ID: 101553819Publisher: Cairo: Hindawi Pub Corp
Correspondence: Tony Velkov
Institutions: Institute for Molecular Bioscience, The University of Queensland, 306 Carmody Road, St. Lucia, QLD 4072, Australia, Drug Development and Innovation, Drug Delivery, Disposition and Dynamics, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, VIC 3052, Australia, Medicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, VIC 3052, Australia, Priority Research Centre in Reproductive Science, School of Environmental and Life Sciences, University of Newcastle, Callaghan, NSW 2308, Australia
Methods: molecular modeling, fluorescence spectroscopy, surface plasmon resonance (SPR)
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2. Compound ID: 262
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a-D-GlcpNAc-(1-2)-+ a-D-Galp-(1-6)-+
| |
a-L-Rhap-(1-3)-a-L-Rhap-(1-2)-a-D-Galp-(1-3)-a-D-GlcpNAc-(1-4)-a-D-Glcp-(1-2)-a-D-Galp-(1-3)-D-Glc |
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Structure type: oligomer
Contained glycoepitopes: IEDB_125611,IEDB_130669,IEDB_130693,IEDB_136105,IEDB_136906,IEDB_137472,IEDB_140529,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_167069,IEDB_190606,IEDB_225177,IEDB_885823,IEDB_983931,SB_192,SB_7
The structure is contained in the following publication(s):
- Article ID: 68
Falt IC, Mills D, Schweda EKH, Timmis KN, Lindberg AA "Construction of recombinant aroA salmonellae stably producing the Shigella dysenteriae serotype 1 O-antigen and structural characterization of the Salmonella/Shigella hybrid LPS" -
Microbial Pathogenesis 20(1) (1996) 11-30
The TN501 mercury resistant transposon containing the rfp and rfb loci encoding biosynthesis of the O-antigen of Shigella dysenteriae serotype 1 lipopolysaccharide (LPS) was constructed and introduced into aroA mutants of Salmonella typhimurium and Salmonella dublin. In five recombinant strains, both homologous LPS and hybrid LPS, consisting of Salmonella lipid A-core and Shigella O-antigen, were produced. All derivatives but one (SL3235) stably inherited the new trait. Immunofluorescence microscopy, using mixtures of differentially-labelled antibodies specific for either the Salmonella or the Shigella O-antigen, demonstrated that individual bacteria produced both types of LPS. Qualitative and quantitative analysis of polysaccharides obtained by mild hydrolysis of purified LPS was carried out by methylation analysis and NMR spectroscopy, and revealed that the ratio of Salmonella to Shigella O-antigen repeating units in the high molecular weight fraction of isolated polysaccharides varied from 1.3: 1 to 8.4:1 as based on the relative proportions of 1,4,5-tri-O-acetyl-2,3-di-O-methyl-L-rhamnitol (Salmonella repeating unit) and 1,3,5-tri-O-acetyl-2,4-di-O-methyl-L-rhamnitol (Shigella repeating unit). The attachment site of the Shigella O-antigen to the Salmonella core was investigated by construction of a mutant rfp-rfb gene cluster encoding the synthesis of only one repeat unit of the Shigella dysenteriae type 1 O-antigen, and its introduction into a rough Salmonella strain. This hybrid organism produced a polysaccharide with the following structure, [formula: see text] demonstrating that the Shigella dysenteriae type 1 O-antigen is linked at position O-4 of the subterminal D-glucose unit in the Salmonella core
LPS, Salmonella, Shigella dysenteriae type 1, hybrids, vaccine.
NCBI PubMed ID: 8692007Journal NLM ID: 8606191Publisher: Academic Press
Institutions: Department of Immunology, Microbiology, Pathology and Infectious Diseases, Karolinska Institute, Huddinge Hospital, Sweden, Department of Medical Biochemistry, University of Geneva, Switzerland, Division of Microbiology, National Research Centre for Biotechnology, Braunschweig, Germany, Clinical Research Centre, Karolinska Institute, Novum, Huddinge Hospital, Sweden
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3. Compound ID: 268
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a-D-Galp-(1-6)-+
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a-D-GlcpNAc-(1-2)-a-D-Glcp-(1-2)-a-D-Galp-(1-3)-a-D-Glcp-(1--/lipid A/ |
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Structure type: oligomer
Aglycon: lipid A
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130693,IEDB_136906,IEDB_137472,IEDB_140529,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_983931,SB_192,SB_7
The structure is contained in the following publication(s):
- Article ID: 68
Falt IC, Mills D, Schweda EKH, Timmis KN, Lindberg AA "Construction of recombinant aroA salmonellae stably producing the Shigella dysenteriae serotype 1 O-antigen and structural characterization of the Salmonella/Shigella hybrid LPS" -
Microbial Pathogenesis 20(1) (1996) 11-30
The TN501 mercury resistant transposon containing the rfp and rfb loci encoding biosynthesis of the O-antigen of Shigella dysenteriae serotype 1 lipopolysaccharide (LPS) was constructed and introduced into aroA mutants of Salmonella typhimurium and Salmonella dublin. In five recombinant strains, both homologous LPS and hybrid LPS, consisting of Salmonella lipid A-core and Shigella O-antigen, were produced. All derivatives but one (SL3235) stably inherited the new trait. Immunofluorescence microscopy, using mixtures of differentially-labelled antibodies specific for either the Salmonella or the Shigella O-antigen, demonstrated that individual bacteria produced both types of LPS. Qualitative and quantitative analysis of polysaccharides obtained by mild hydrolysis of purified LPS was carried out by methylation analysis and NMR spectroscopy, and revealed that the ratio of Salmonella to Shigella O-antigen repeating units in the high molecular weight fraction of isolated polysaccharides varied from 1.3: 1 to 8.4:1 as based on the relative proportions of 1,4,5-tri-O-acetyl-2,3-di-O-methyl-L-rhamnitol (Salmonella repeating unit) and 1,3,5-tri-O-acetyl-2,4-di-O-methyl-L-rhamnitol (Shigella repeating unit). The attachment site of the Shigella O-antigen to the Salmonella core was investigated by construction of a mutant rfp-rfb gene cluster encoding the synthesis of only one repeat unit of the Shigella dysenteriae type 1 O-antigen, and its introduction into a rough Salmonella strain. This hybrid organism produced a polysaccharide with the following structure, [formula: see text] demonstrating that the Shigella dysenteriae type 1 O-antigen is linked at position O-4 of the subterminal D-glucose unit in the Salmonella core
LPS, Salmonella, Shigella dysenteriae type 1, hybrids, vaccine.
NCBI PubMed ID: 8692007Journal NLM ID: 8606191Publisher: Academic Press
Institutions: Department of Immunology, Microbiology, Pathology and Infectious Diseases, Karolinska Institute, Huddinge Hospital, Sweden, Department of Medical Biochemistry, University of Geneva, Switzerland, Division of Microbiology, National Research Centre for Biotechnology, Braunschweig, Germany, Clinical Research Centre, Karolinska Institute, Novum, Huddinge Hospital, Sweden
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4. Compound ID: 926
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?%a-Kdop-(2-4)-+
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EtN-(1-0)-?%P-7)-a-Kdop-(2-4)-+
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EtN-(1-0)-?%P-0)-?%P-4)-+ |
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L-gro-a-D-manHepp-(1-7)-+ | |
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a-D-GlcpNAc-(1-2)-+ | | |
| | | |
Subst-(1-2)-+ a-D-Glcp-(1-4)-+ | a-D-Galp-(1-6)-+ | | |
| | | | | | |
a-Abep2Ac-(1-3)-a-D-Manp-(1-4)-b-L-Rhap-(1-3)-a-D-Galp-(1-4)-a-D-Glcp-(1-2)-a-D-Galp-(1-3)-a-D-Glcp-(1-3)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/
|
?%P-4)-+
Subst = O-antigen |
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Structure type: oligomer
Aglycon: lipid A
Compound class: core oligosaccharide with O-unit
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130656,IEDB_130659,IEDB_130670,IEDB_130693,IEDB_130701,IEDB_133751,IEDB_135513,IEDB_136906,IEDB_137472,IEDB_140088,IEDB_140529,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144983,IEDB_144998,IEDB_146664,IEDB_150901,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_153307,IEDB_190606,IEDB_2189047,IEDB_225177,IEDB_226811,IEDB_885823,IEDB_983930,IEDB_983931,SB_192,SB_44,SB_67,SB_7,SB_72
The structure is contained in the following publication(s):
- Article ID: 265
Inagaki M, Kawaura T, Wakashima H, Kato M, Nishikawa S, Kashimura N "Different contributions of the outer and inner R-core residues of lipopolysaccharide to the recognition by spike H and G proteins of bacteriophage phiX174" -
FEMS Microbiology Letters 226(2) (2003) 221-227
The binding of spike H and G proteins of bacteriophage phiX174 with lipopolysaccharides (LPSs) were evaluated by a competitive enzyme-linked plate assay using the biotin-labeled LPS of Escherichia coli C, one of a host strain, and the non-labeled LPSs having different R-core polysaccharide lengths. H protein promptly decreased its affinity when some saccharide residues were truncated from the outer R-core. However, G protein showed significant affinity to the LPSs lacking all the residues of the outer R-core and some of the inner R-core. Thus, G protein rather than H protein well recognized the residues of the inner R-core of LPS
LPS, core, bacteriophage, proteins, G-protein, phiX174, host recognition, spike protein
NCBI PubMed ID: 14553915Journal NLM ID: 7705721Publisher: Blackwell Publishing
Correspondence: inagaki@bio.mie-u.ac.jp
Institutions: Department of Life Science, Faculty of Bioresources, Mie University, 1515 Kamihama, Tsu, 514-8507, Mie, Japan
Methods: DOC-PAGE, enzyme-linked plate assay
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5. Compound ID: 955
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a-Kdop-(2-4)-+
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EtN-(1-0)-?%P-7)-a-Kdop-(2-4)-+
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EtN-(1-0)-?%P-0)-?%P-4)-+ |
| |
L-gro-a-D-manHepp-(1-7)-+ | |
| | |
a-D-Galp-(1-6)-+ | | |
| | | |
a-D-GlcpNAc-(1-2)-a-D-Glcp-(1-2)-a-D-Galp-(1-3)-a-D-Glcp-(1-3)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/
|
?%P-4)-+ |
Show graphically |
Structure type: oligomer
Aglycon: lipid A
Compound class: core oligosaccharide with O-unit
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130656,IEDB_130659,IEDB_130670,IEDB_130693,IEDB_133751,IEDB_136906,IEDB_137472,IEDB_140088,IEDB_140529,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_150901,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_226811,IEDB_983931,SB_192,SB_7
The structure is contained in the following publication(s):
- Article ID: 265
Inagaki M, Kawaura T, Wakashima H, Kato M, Nishikawa S, Kashimura N "Different contributions of the outer and inner R-core residues of lipopolysaccharide to the recognition by spike H and G proteins of bacteriophage phiX174" -
FEMS Microbiology Letters 226(2) (2003) 221-227
The binding of spike H and G proteins of bacteriophage phiX174 with lipopolysaccharides (LPSs) were evaluated by a competitive enzyme-linked plate assay using the biotin-labeled LPS of Escherichia coli C, one of a host strain, and the non-labeled LPSs having different R-core polysaccharide lengths. H protein promptly decreased its affinity when some saccharide residues were truncated from the outer R-core. However, G protein showed significant affinity to the LPSs lacking all the residues of the outer R-core and some of the inner R-core. Thus, G protein rather than H protein well recognized the residues of the inner R-core of LPS
LPS, core, bacteriophage, proteins, G-protein, phiX174, host recognition, spike protein
NCBI PubMed ID: 14553915Journal NLM ID: 7705721Publisher: Blackwell Publishing
Correspondence: inagaki@bio.mie-u.ac.jp
Institutions: Department of Life Science, Faculty of Bioresources, Mie University, 1515 Kamihama, Tsu, 514-8507, Mie, Japan
Methods: DOC-PAGE, enzyme-linked plate assay
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6. Compound ID: 956
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/Variants 0/-a-Kdop-(2-4)-+
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EtN-(1-0)-?%P-0)-?%P-4)-+ |
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L-gro-a-D-manHepp-(1-7)-+ | |
| | |
a-D-Galp-(1-6)-+ | | |
| | | |
a-D-GlcpNAc-(1-2)-a-D-Glcp-(1-2)-a-D-Glcp-(1-3)-a-D-Glcp-(1-3)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/(->6) lipid A/
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?%P-4)-+
/Variants 0/ is:
a-D-Galp-(1-7)-
OR (exclusively)
EtN-(1-0)-?%P-7)- |
Show graphically |
Structure type: oligomer
Aglycon: (->6) lipid A
Compound class: core oligosaccharide with O-unit
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130659,IEDB_130670,IEDB_130693,IEDB_133751,IEDB_136906,IEDB_137472,IEDB_140088,IEDB_140529,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_226811,IEDB_232584,IEDB_983931,SB_192,SB_7
The structure is contained in the following publication(s):
- Article ID: 265
Inagaki M, Kawaura T, Wakashima H, Kato M, Nishikawa S, Kashimura N "Different contributions of the outer and inner R-core residues of lipopolysaccharide to the recognition by spike H and G proteins of bacteriophage phiX174" -
FEMS Microbiology Letters 226(2) (2003) 221-227
The binding of spike H and G proteins of bacteriophage phiX174 with lipopolysaccharides (LPSs) were evaluated by a competitive enzyme-linked plate assay using the biotin-labeled LPS of Escherichia coli C, one of a host strain, and the non-labeled LPSs having different R-core polysaccharide lengths. H protein promptly decreased its affinity when some saccharide residues were truncated from the outer R-core. However, G protein showed significant affinity to the LPSs lacking all the residues of the outer R-core and some of the inner R-core. Thus, G protein rather than H protein well recognized the residues of the inner R-core of LPS
LPS, core, bacteriophage, proteins, G-protein, phiX174, host recognition, spike protein
NCBI PubMed ID: 14553915Journal NLM ID: 7705721Publisher: Blackwell Publishing
Correspondence: inagaki@bio.mie-u.ac.jp
Institutions: Department of Life Science, Faculty of Bioresources, Mie University, 1515 Kamihama, Tsu, 514-8507, Mie, Japan
Methods: DOC-PAGE, enzyme-linked plate assay
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7. Compound ID: 1061
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a-D-Galp-(1-6)-+
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a-D-GlcpNAc-(1-2)-a-D-Glcp-(1-2)-a-D-Glcp-(1-3)-a-D-Glcp-(1--/inner core/ |
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Structure type: oligomer
Aglycon: inner core
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130693,IEDB_136906,IEDB_137472,IEDB_140529,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_232584,IEDB_983931,SB_192,SB_7
The structure is contained in the following publication(s):
- Article ID: 313
Lugowski C, Jachymek W, Niedziela T, Rowinski S "Serological characterisation of anti-endotoxin sera directed against the conjugates of oligosaccharide core of Escherichia coli type R1, R2, R3, J5 and Salmonella Ra with tetanus toxoid" -
FEMS Immunology and Medical Microbiology 16 (1996) 21-30
The covalent conjugates of oligosaccharide core: Escherichia coli type R1, R2, R3, J5 and Salmonella Ra with tetanus toxoid have been prepared using reaction of reductive amination. The neoglycoconjugates were good immunogens in rabbits yielding a high level of anti-lipopolysaccharide antibodies of IgG class. The antibodies were used to examine the possibility of their reactions with smooth lipopolysaccharides. We have found that all antisera were able to react with the lipopolysaccharide molecules of identical or related core type, possessing core oligosaccharides substituted with O-specific chains. These reactions were shown in both the ELISA assay and the immunoblotting test.
oligosaccharide, core, Escherichia coli, endotoxin, serological, Salmonella, anti-endotoxin, conjugate vaccine, tetanus toxoid
NCBI PubMed ID: 8954349Journal NLM ID: 9315554Publisher: Elsevier
Correspondence: lugowski@immuno.pan.wroc.pl
Institutions: Ludwik Hirszfeld Institute of Immunology and Experimental Therapy, Wroclaw, Poland.
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8. Compound ID: 1064
|
L-gro-a-D-manHepp-(1-7)-+
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a-D-Galp-(1-6)-+ | a-Kdop-(2-4)-a-Kdop-(2-4)-+
| | |
a-D-GlcpNAc-(1-2)-a-D-Glcp-(1-2)-a-D-Galp-(1-3)-a-D-Glcp-(1-3)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-Kdo |
Show graphically |
Structure type: oligomer
Trivial name: Ra core oligosaccharide
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130650,IEDB_130656,IEDB_130659,IEDB_130670,IEDB_130693,IEDB_136906,IEDB_137472,IEDB_140088,IEDB_140529,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_150901,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_226811,IEDB_983931,SB_192,SB_7
The structure is contained in the following publication(s):
- Article ID: 313
Lugowski C, Jachymek W, Niedziela T, Rowinski S "Serological characterisation of anti-endotoxin sera directed against the conjugates of oligosaccharide core of Escherichia coli type R1, R2, R3, J5 and Salmonella Ra with tetanus toxoid" -
FEMS Immunology and Medical Microbiology 16 (1996) 21-30
The covalent conjugates of oligosaccharide core: Escherichia coli type R1, R2, R3, J5 and Salmonella Ra with tetanus toxoid have been prepared using reaction of reductive amination. The neoglycoconjugates were good immunogens in rabbits yielding a high level of anti-lipopolysaccharide antibodies of IgG class. The antibodies were used to examine the possibility of their reactions with smooth lipopolysaccharides. We have found that all antisera were able to react with the lipopolysaccharide molecules of identical or related core type, possessing core oligosaccharides substituted with O-specific chains. These reactions were shown in both the ELISA assay and the immunoblotting test.
oligosaccharide, core, Escherichia coli, endotoxin, serological, Salmonella, anti-endotoxin, conjugate vaccine, tetanus toxoid
NCBI PubMed ID: 8954349Journal NLM ID: 9315554Publisher: Elsevier
Correspondence: lugowski@immuno.pan.wroc.pl
Institutions: Ludwik Hirszfeld Institute of Immunology and Experimental Therapy, Wroclaw, Poland.
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9. Compound ID: 1122
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a-Galp-(1-6)-+
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a-GlcpNAc-(1-2)-a-Glcp-(1-2)-a-Galp-(1-3)-a-Glcp |
Show graphically |
Structure type: fragment of a bigger structure
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130693,IEDB_136906,IEDB_137472,IEDB_140529,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_983931,SB_192,SB_7
The structure is contained in the following publication(s):
- Article ID: 338
Nnalue NA, Khan GN, Mustafa N "Cross-reactivity between six Enterobacteriaceae complete lipopolysaccharide core chemotypes" -
Journal of Medical Microbiology 48(5) (1999) 433-441
To gain insight into the value of lipopolysaccharide (LPS) core determinants for cross-protective immunisation the serological relationships between six complete (LPS) core types from Enterobacteriaceae were investigated. Hyperimmune sera were raised in mice by repeated immunisation with heat-killed strains of Salmonella choleraesuis (Ra core type) or Escherichia coli (core types R1, R2, R3, R4 and K12) and characterised for reactivity with complete and incomplete core chemotypes by ELISA and immunoblotting. Three sera (anti-Ra, anti-R2 and anti-R3) reacted strongly with 3-5 different complete core types whereas the other three (anti-R1, anti-R4 and anti-K12) reacted strongly only with their homologous core types in these assays. Two approaches were used to examine further the structural bases for cross-reactivity between these cores. By the first approach the anti-complete-core sera were tested for cross-reactivity with truncated forms of the Salmonella species core (incomplete cores) derived from core-defective mutants. By the second approach, antisera raised against some core-defective mutants were tested for cross-reactivity with complete cores. The results of these investigations revealed that several pair-wise combinations of core types can be used as immunogens to elicit immune responses that recognise all six core types and that the major determinants which mediate cross-reactivity between complete cores are localised in the outer core region.
Lipopolysaccharide, core, lipopolysaccharide core, chemotype, Chemotypes, cross-reactivity, crossreactivity, Enterobacteriaceae
NCBI PubMed ID: 10229540Journal NLM ID: 0224131Publisher: Reading, England: Society for General Microbiology
Institutions: Department of Medical Microbiology, Faculty of Medicine and Health Sciences, United Arab Emirates University, Al Ain, United Arab Emirates
Methods: SDS-PAGE, ELISA, biological assays, serological methods, immunoblotting
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10. Compound ID: 1124
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a-Galp-(1-6)-+
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a-GlcpNAc-(1-2)-a-Glcp-(1-2)-a-Glcp-(1-3)-a-Glcp |
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Structure type: fragment of a bigger structure
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130693,IEDB_136906,IEDB_137472,IEDB_140529,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_232584,IEDB_983931,SB_192,SB_7
The structure is contained in the following publication(s):
- Article ID: 338
Nnalue NA, Khan GN, Mustafa N "Cross-reactivity between six Enterobacteriaceae complete lipopolysaccharide core chemotypes" -
Journal of Medical Microbiology 48(5) (1999) 433-441
To gain insight into the value of lipopolysaccharide (LPS) core determinants for cross-protective immunisation the serological relationships between six complete (LPS) core types from Enterobacteriaceae were investigated. Hyperimmune sera were raised in mice by repeated immunisation with heat-killed strains of Salmonella choleraesuis (Ra core type) or Escherichia coli (core types R1, R2, R3, R4 and K12) and characterised for reactivity with complete and incomplete core chemotypes by ELISA and immunoblotting. Three sera (anti-Ra, anti-R2 and anti-R3) reacted strongly with 3-5 different complete core types whereas the other three (anti-R1, anti-R4 and anti-K12) reacted strongly only with their homologous core types in these assays. Two approaches were used to examine further the structural bases for cross-reactivity between these cores. By the first approach the anti-complete-core sera were tested for cross-reactivity with truncated forms of the Salmonella species core (incomplete cores) derived from core-defective mutants. By the second approach, antisera raised against some core-defective mutants were tested for cross-reactivity with complete cores. The results of these investigations revealed that several pair-wise combinations of core types can be used as immunogens to elicit immune responses that recognise all six core types and that the major determinants which mediate cross-reactivity between complete cores are localised in the outer core region.
Lipopolysaccharide, core, lipopolysaccharide core, chemotype, Chemotypes, cross-reactivity, crossreactivity, Enterobacteriaceae
NCBI PubMed ID: 10229540Journal NLM ID: 0224131Publisher: Reading, England: Society for General Microbiology
Institutions: Department of Medical Microbiology, Faculty of Medicine and Health Sciences, United Arab Emirates University, Al Ain, United Arab Emirates
Methods: SDS-PAGE, ELISA, biological assays, serological methods, immunoblotting
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11. Compound ID: 1131
Structure type: oligomer
Aglycon: remaining core-lipid A
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130693,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151531,IEDB_983931,SB_192
The structure is contained in the following publication(s):
- Article ID: 340
Nnalue NA "a-GlcNAc-1→2-a-Glc, the Salmonella homologue of a conserved lipopolysaccharide motif in the Enterobacteriaceae, elicits broadly cross-reactive antibodies" -
Infection and Immunity 66(9) (1998) 4389-4396
To define cross-reactive epitopes in Salmonella lipopolysaccharide (LPS), antisera designated anti-S, anti-Ra, and anti-Re were generated against smooth (S), complete-core (Ra), and deep-core mutant (Re) strains, respectively, and characterized immunochemically. The reactivities of anti-Ra and anti-S with rough LPS (rLPS) chemotypes in enzyme-linked immunosorbent assays (ELISA) decreased progressively with increasing truncation of the complete-core oligosaccharide (e.g., Ra > Rb1 >.Re), while that of anti-Re increased (Ra < Rb1 <.Re). Anti-Ra was relatively more reactive with nonhomologous smooth LPS (sLPS) than anti-S, which in turn was more reactive than anti-Re. This order reflected the relative reactivities of these sera with outer-core rLPS but not those with inner-core rLPS, which suggests that the cross-reactivities of all three sera with sLPS were mediated by antibodies which bind outer-core determinants. Anti-Ra, but not anti-S or anti-Re, reacted with molecules substituted by O chains in immunoblots and revealed ladder-like patterns in sLPSs of various serospecificities. Anti-Ra, however, did not react with O-antigen-specific neoglycoconjugates in ELISA, thus demonstrating specificity for core epitopes. Ra and Rb1 but not other Salmonella core chemotypes inhibited the reactivity of anti-Ra with sLPS in ELISA, which showed that the terminal outer-core disaccharide, αGlcNAc 1→2 αGlc (GlcNAc → Glc), was the major epitope of cross-reactive antibodies in the serum. GlcNAc → Glc represents the conserved motif α-hexose 1→2 α-hexose in cores of the Enterobacteriaceae, other homologues of which should likewise be cross-reactive. These results demonstrate that S or Re strains do not elicit cross-reactive antibodies and indicate that immunization with Ra strains may represent a general strategy for eliciting cross-reactive antibodies against LPSs from enteric bacteria
Lipopolysaccharide, antibodies, antibody, conserved, Salmonella, motif, Enterobacteriaceae, cross-reactive
NCBI PubMed ID: 9712792Journal NLM ID: 0246127Publisher: American Society for Microbiology
Correspondence: nnnalue@kumc.edu
Institutions: Department of Medical Microbiology, Faculty of Medicine and Health Sciences, United Arab Emirates University, Al Ain, United Arab Emirates
Methods: SDS-PAGE, ELISA, immunoblotting, stereoplotting
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12. Compound ID: 2210
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a-D-Galp-(1-6)-+
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a-D-GlcpNAc-(1-2)-a-D-Glcp-(1-2)-a-D-Galp-(1-3)-a-D-Glcp-(1-3)-L-gro-a-D-manHepp-(1--/inner region of the core/ |
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Structure type: oligomer
Aglycon: inner region of the core
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130693,IEDB_136906,IEDB_137472,IEDB_140529,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_983931,SB_192,SB_7
The structure is contained in the following publication(s):
- Article ID: 716
Kaniuk NA, Monteiro MA, Parker CT, Whitfield C "Molecular diversity of the genetic loci responsible for lipopolysaccharide core oligosaccharide assembly within the genus Salmonella" -
Molecular Microbiology 46(5) (2002) 1305-1318
The waa locus on the chromosome of Salmonella enterica encodes enzymes involved in the assembly of the core oligosaccharide region of the lipopolysaccharide (LPS) molecule. To date, there are two known core structures in Salmonella, represented by serovars Typhimurium (subspecies I) and Arizonae (subspecies IIIA). The waa locus for serovar Typhimurium has been characterized. Here, the corresponding locus from serovar Arizonae is described, and the molecular basis for the distinctive structures is established. Eleven of the 13 open reading frames (ORFs) are shared by the two loci and encode conserved proteins of known function. Two polymorphic regions distinguish the waa loci. One involves the waaK gene, the product of which adds a terminal α-1,2-linked N-acetylglucosamine residue that cha
Lipopolysaccharide, genetic, LPS, oligosaccharide, structure, core, gene, terminal, molecular, molecule, locus, conserved, core oligosaccharide, lipopolysaccharide core, lipopolysaccharide core oligosaccharide, protein, Salmonella, assembly, region, Open Reading Frames, Salmonella enterica, enzyme, function, genus, Enzymes, proteins, N-acetylglucosamine, diversity, subspecies, chromosome, Typhimurium
NCBI PubMed ID: 12453217Journal NLM ID: 8712028Publisher: Blackwell Publishing
Correspondence: cwhitfie@uoguelph.ca
Institutions: Department of Microbiology, University of Guelph, Guelph, ON, Canada
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13. Compound ID: 2350
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a-D-Galp-(1-6)-+
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a-D-GlcpNAc-(1-2)-a-D-Glcp-(1-2)-a-D-Glcp-(1-3)-a-D-Glcp-(1-3)-D-gro-a-D-manHepp-(1--/Kdo-lipid A/ |
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Structure type: oligomer
Aglycon: Kdo-lipid A
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130693,IEDB_136906,IEDB_137472,IEDB_140529,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_2189046,IEDB_232584,IEDB_983931,SB_192,SB_7
The structure is contained in the following publication(s):
- Article ID: 807
Heinrichs DE, Monteiro MA, Perry MB, Whitfield C "The assembly system for the lipopolysaccharide R2 core-type of Escherichia coli is a hybrid of those found in Escherichia coli K-12 and Salmonella enterica. Structure and function of the r2 waak and waal homologs" -
Journal of Biological Chemistry 273(15) (1998) 8849-8859
In Escherichia coli F632, the 14-kilobase pair chromosomal region located between waaC (formerly rfaC) and waaA (kdtA) contains genes encoding enzymes required for the synthesis of the type R2 core oligosaccharide portion of lipopolysaccharide. Ten of the 13 open reading frames encode predicted products sharing greater than 90% total similarity with homologs in E. coli K-12. However, the products of waaK (rfaK) and waaL (rfaL) each resemble homologs in Salmonella enterica serovar Typhimurium but share little similarity with E. coli K-12. The F632 WaaK and WaaL proteins therefore define differences between the type R2 and K-12 outer core oligosaccharides of E. coli lipopolysaccharides. Based on the chemical structure of the core oligosaccharide of an E. coli F632 waaK::aacC1 mutant and in vitro glycosyltransferase analyses, waaK encodes UDP-N-acetylglucosamine:(glucose) lipopolysaccharide a1,2-N-acetylglucosaminyltransferase. The WaaK enzyme adds a terminal GlcNAc side branch substituent that is crucial for the recognition of core oligosaccharide acceptor by the O-polysaccharide ligase, WaaL. Results of complementation analyses of E. coli K-12 and F632 waaL mutants suggest that structural differences between the WaaL proteins play a role in recognition of, and interaction with, terminal lipopolysaccharide core moieties.
Lipopolysaccharide, biosynthesis, structure, core, Escherichia, Escherichia coli, Salmonella, assembly, homolog, Salmonella enterica, function, hybrid
NCBI PubMed ID: 9535865Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: cwhitfie@uoguelph.ca
Institutions: Department of Microbiology, University of Guelph, Guelph, Ontario, Canada N1G 2W1, Institute for Biological Sciences, National Research Council, Ottawa, Ontario, Canada K1A OR6
Methods: methylation, PCR, DNA sequencing, FAB-MS, NMR, SDS-PAGE, enzymatic digestion, DNA restriction, endonuclease ligation
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14. Compound ID: 2365
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Subst-(?-4)-+
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a-D-GlcpNAc-(1-2)-a-D-Glcp-(1-2)-a-D-Galp-(1--/core-Lipid A/
Subst = O-antigen |
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Structure type: oligomer
Aglycon: core-Lipid A
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130693,IEDB_136906,IEDB_137472,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_983931,SB_192,SB_7
The structure is contained in the following publication(s):
- Article ID: 827
Ishiwa A, Komano T "Thin pilus PilV adhesins of plasmid R64 recognize specific structures of the lipopolysaccharide molecules of recipient cells" -
Journal of Bacteriology 185(17) (2003) 5192-5199
IncI1 plasmid R64 encodes a type IV pilus called a thin pilus, which includes PilV adhesins. Seven different sequences for the C-terminal segments of PilV adhesins can be produced by shufflon DNA rearrangement. The expression of the seven PilV adhesins determines the recipient specificity in liquid matings of plasmid R64. Salmonella enterica serovar Typhimurium LT2 was recognized by the PilVA' and PilVB' adhesins, while Escherichia coli K-12 was recognized by the PilVA', PilVC, and PilVC' adhesins. Lipopolysaccharide (LPS) on the surfaces of recipient cells was previously shown to be the specific receptor for the seven PilV adhesins. To identify the specific receptor structures of LPS for various PilV adhesins, R64 liquid matings were carried out with recipient cells consisting of various S. enterica serovar Typhimurium LT2 and E. coli K-12 waa mutants and their derivatives carrying various waa genes of different origins. From the mating experiments, including inhibition experiments, we propose that the GlcNAc(α1-2)Glc and Glc(α1-2)Gal structures of the LPS core of S. enterica serovar Typhimurium LT2 function as receptors for the PilVB' and PilVC' adhesins, respectively, while the PilVC' receptor in the wild-type LT2 LPS core may be masked. We further propose that the GlcNAc(β1-7)Hep and Glc(α1-2)Glc structures of the LPS core of E. coli K-12 function as receptors for the PilVC and PilVC' adhesins, respectively.
Lipopolysaccharide, genetic, lipopolysaccharides, LPS, structure, core, Bacterial Proteins, expression, gene, Bacterial, genetics, metabolism, DNA, Support, molecule, Escherichia, Escherichia coli, type, wild type, specific, mutant, mutants, specificity, Salmonella, plasmid, Salmonella enterica, surface, Salmonella typhimurium, sequence, function, inhibition, virology, recombination, rearrangement, adhesin, LPS core, Typhimurium, receptors, Bacteriophages, Conjugation, Fimbriae, origin, physiology, Plasmids, receptor
NCBI PubMed ID: 12923092Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Correspondence: komano-teruya@c.metro-u.ac.jp
Institutions: Department of Biology, Tokyo Metropolitan University, Minamiohsawa, Hachioji, Tokyo 192-0397, Japan
Methods: SDS-PAGE
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15. Compound ID: 2427
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a-D-Galp-(1-6)-+
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a-D-GlcpNAc-(1-2)-a-D-Glcp-(1-2)-a-D-Galp-(1-3)-a-D-Glcp-(1-3)-D-gro-a-D-manHepp-(1--/Kdo-Lipid A/ |
Show graphically |
Structure type: oligomer
Aglycon: Kdo-Lipid A
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130693,IEDB_136906,IEDB_137472,IEDB_140529,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_2189046,IEDB_983931,SB_192,SB_7
The structure is contained in the following publication(s):
- Article ID: 807
Heinrichs DE, Monteiro MA, Perry MB, Whitfield C "The assembly system for the lipopolysaccharide R2 core-type of Escherichia coli is a hybrid of those found in Escherichia coli K-12 and Salmonella enterica. Structure and function of the r2 waak and waal homologs" -
Journal of Biological Chemistry 273(15) (1998) 8849-8859
In Escherichia coli F632, the 14-kilobase pair chromosomal region located between waaC (formerly rfaC) and waaA (kdtA) contains genes encoding enzymes required for the synthesis of the type R2 core oligosaccharide portion of lipopolysaccharide. Ten of the 13 open reading frames encode predicted products sharing greater than 90% total similarity with homologs in E. coli K-12. However, the products of waaK (rfaK) and waaL (rfaL) each resemble homologs in Salmonella enterica serovar Typhimurium but share little similarity with E. coli K-12. The F632 WaaK and WaaL proteins therefore define differences between the type R2 and K-12 outer core oligosaccharides of E. coli lipopolysaccharides. Based on the chemical structure of the core oligosaccharide of an E. coli F632 waaK::aacC1 mutant and in vitro glycosyltransferase analyses, waaK encodes UDP-N-acetylglucosamine:(glucose) lipopolysaccharide a1,2-N-acetylglucosaminyltransferase. The WaaK enzyme adds a terminal GlcNAc side branch substituent that is crucial for the recognition of core oligosaccharide acceptor by the O-polysaccharide ligase, WaaL. Results of complementation analyses of E. coli K-12 and F632 waaL mutants suggest that structural differences between the WaaL proteins play a role in recognition of, and interaction with, terminal lipopolysaccharide core moieties.
Lipopolysaccharide, biosynthesis, structure, core, Escherichia, Escherichia coli, Salmonella, assembly, homolog, Salmonella enterica, function, hybrid
NCBI PubMed ID: 9535865Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: cwhitfie@uoguelph.ca
Institutions: Department of Microbiology, University of Guelph, Guelph, Ontario, Canada N1G 2W1, Institute for Biological Sciences, National Research Council, Ottawa, Ontario, Canada K1A OR6
Methods: methylation, PCR, DNA sequencing, FAB-MS, NMR, SDS-PAGE, enzymatic digestion, DNA restriction, endonuclease ligation
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Next 15 structure(s)
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Total list of corresponding CSDB IDs (record IDs):
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