Found 100 structures.
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1. Compound ID: 83
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Subst-(1-5)-+
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?%a-Kdop-(2-4)-+ |
| |
/Variants 0/-a-Kdop-(2-4)-a-Kdop-(2--/lipid A/
/Variants 0/ is:
EtN-(1-0)-?%P-?)-
OR (exclusively)
?%Rhap-(1-?)-
Subst = core oligosaccharide |
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Structure type: oligomer
Aglycon: lipid A
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130659,IEDB_136105,IEDB_137777,IEDB_137778,IEDB_1394181,IEDB_150901,IEDB_225177,IEDB_885823
The structure is contained in the following publication(s):
- Article ID: 17
Bode CE, Brabetz W, Brade H "Cloning and characterization of 3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) transferase genes (kdtA) from Acinetobacter baumannii and Acinetobacter haemolyticus" -
European Journal of Biochemistry 254(2) (1998) 404-412
3-Deoxy-D-manno-oct-2-ulosonic acid (Kdo) transferases (KdtA) are multifunctional glycosyltransferases with primary structures of low similarity. Totally degenerated primers were deduced from two stretches of identical amino acids between known KdtA sequences and used to amplify by PCR a kdtA-specific fragment from Acinetobacter baumannii ATCC 15308 DNA which was then applied as a probe for the cloning and sequencing of the complete Kdo transferase gene. With conserved PCR primers for this structural gene from A. baumannii ATCC 15308, also kdtA genes of A. baumannii ATCC 19606 and A. haemolyticus ATCC 17906 were obtained, cloned from the chromosome and sequenced. The genes coded for proteins with similarities to known Kdo transferases. Within the genus Acinetobacter, the identity and similarity of the deduced amino acid sequences were 71% and 84.5%, respectively. The kdtA sequences of both A. baumannii strains were identical and possessed a TTG start codon, whereas ATG was found in the case of A. haemolyticus. The genes from Acinetobacter and kdtA from Escherichia coli K-12 were expressed in the Gram-positive bacterium Corynebacterium glutamicum. In vitro tests confirmed the function of the gene products as Kdo transferases, which transferred mainly two Kdo residues to a synthetic lipid A precursor of E. coli. Also, no differences between the cloned kdtA genes from A. baumanniii, A. haemnolyticus and E. coli were observed when tetraacyl or hexaacyl lipid A were tested, since all transferases acted more efficiently on the former. With limiting amounts of acceptor, all Kdo transferases were able to transfer a third Kdo residue with varying efficiency
gene, characterization, 3-deoxy-D-manno-oct-2-ulosonic acid, acid, Acinetobacter, Acinetobacter baumannii, Acinetobacter haemolyticus, cloning, Kdo, lipopolysaccharide biosynthesis, shuttle plasmid, transferase
NCBI PubMed ID: 9660198Publication DOI: 10.1046/j.1432-1327.1998.2540404.xJournal NLM ID: 0107600Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
Correspondence: hbrade@fz-borstel.de
Institutions: Division of Medical and Biochemical Microbiology, Research Center Borstel, Center for Medicine and Biosciences, Borstel, Germany
Methods: PCR, DNA sequencing, DNA cloning
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2. Compound ID: 111
Structure type: oligomer
Aglycon: BSA or allyl
Compound class: neoglycoconjugate
Contained glycoepitopes: IEDB_130650,IEDB_130659,IEDB_150901
The structure is contained in the following publication(s):
- Article ID: 21
Brade L, Rozalski A, Kosma P, Brade H "A monoclonal antibody recognizing the 3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) trisaccharide a-Kdop(2→4)-a-Kdop(2→4)-a-Kdo of Chlamydophila psittaci 6BC lipopolysaccharide" -
Journal of Endotoxin Research 6(5) (2000) 361-368
A monoclonal antibody (mAb) S45-18 was generated against a synthetic neoglycoconjugate containing the trisaccharide αXKdop(2→4)αXKdop(2→4)αKdo (Kdo, 3-deoxy-D-manno-oct-2-ulopyranosonic acid) which represents a structure of the lipopolysaccharide (LPS) from Chlamydophila psittaci 6BC. The antibody was characterized by binding and inhibition assays in ELISA using: (i) the immunizing antigen and chemically synthesized derivatives thereof; (ii) chlamydial elementary bodies (EB); and (iii) LPS of Chl. psittaci 6BC and Chlamydia trachomatis L2. The specificity was determined in comparison to that of mAb S25-23 recognizing the αXKdop(2→8)αXKdop(2→4)αKdo trisaccharide which represents an epitope shared by all species of the family. MAb S45-18 bound to an epitope of the structure αXKdop(2→4)αXKdop(2→4)αKdo, with lower reactivity with the (2→8)-(2→4)-linked analog. Using chlamydial EB or LPS, mAb S45-18 bound preferentially to LPS and EB of Chl. psittaci. Therefore, Chl. psittaci LPS contains, in addition to the known genus-specific epitope, a species-specific epitope
lipopolysaccharides, 3-deoxy-D-manno-oct-2-ulosonic acid, antibody specificity, Chlamydia, Chlamydia trachomatis, Chlamydophila psittaci, epitopes, glycoconjugates, MAb
NCBI PubMed ID: 11521056Journal NLM ID: 9433350Publisher: Maney Publishing
Correspondence: hbrade@fz-borstel.de
Institutions: Division of Medical and Biochemical Microbiology, Research Center Borstel, Center for Medicine and Biosciences, Borstel, Germany
Methods: ELISA
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3. Compound ID: 112
Structure type: oligomer
Aglycon: BSA
Compound class: neoglycoconjugate
Contained glycoepitopes: IEDB_130650,IEDB_130659,IEDB_130662,IEDB_135813,IEDB_137340,IEDB_141807,IEDB_150901,IEDB_151531
The structure is contained in the following publication(s):
- Article ID: 21
Brade L, Rozalski A, Kosma P, Brade H "A monoclonal antibody recognizing the 3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) trisaccharide a-Kdop(2→4)-a-Kdop(2→4)-a-Kdo of Chlamydophila psittaci 6BC lipopolysaccharide" -
Journal of Endotoxin Research 6(5) (2000) 361-368
A monoclonal antibody (mAb) S45-18 was generated against a synthetic neoglycoconjugate containing the trisaccharide αXKdop(2→4)αXKdop(2→4)αKdo (Kdo, 3-deoxy-D-manno-oct-2-ulopyranosonic acid) which represents a structure of the lipopolysaccharide (LPS) from Chlamydophila psittaci 6BC. The antibody was characterized by binding and inhibition assays in ELISA using: (i) the immunizing antigen and chemically synthesized derivatives thereof; (ii) chlamydial elementary bodies (EB); and (iii) LPS of Chl. psittaci 6BC and Chlamydia trachomatis L2. The specificity was determined in comparison to that of mAb S25-23 recognizing the αXKdop(2→8)αXKdop(2→4)αKdo trisaccharide which represents an epitope shared by all species of the family. MAb S45-18 bound to an epitope of the structure αXKdop(2→4)αXKdop(2→4)αKdo, with lower reactivity with the (2→8)-(2→4)-linked analog. Using chlamydial EB or LPS, mAb S45-18 bound preferentially to LPS and EB of Chl. psittaci. Therefore, Chl. psittaci LPS contains, in addition to the known genus-specific epitope, a species-specific epitope
lipopolysaccharides, 3-deoxy-D-manno-oct-2-ulosonic acid, antibody specificity, Chlamydia, Chlamydia trachomatis, Chlamydophila psittaci, epitopes, glycoconjugates, MAb
NCBI PubMed ID: 11521056Journal NLM ID: 9433350Publisher: Maney Publishing
Correspondence: hbrade@fz-borstel.de
Institutions: Division of Medical and Biochemical Microbiology, Research Center Borstel, Center for Medicine and Biosciences, Borstel, Germany
Methods: ELISA
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4. Compound ID: 305
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a-L-Rhap-(1-5)-+
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EtN-(1--P--7)--a-Kdop-(2-4)-+
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a-Kdop-(2-4)-+ |
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L-gro-a-D-manHepp-(1-7)-+ |
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a-D-Galp-(1-6)-+ | P-4)-+ |
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L-gro-a-D-manHepp-(1-6)-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--/lipid A/
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P-4)-+ |
Show graphically |
Structure type: oligomer
Aglycon: lipid A
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130659,IEDB_130670,IEDB_133751,IEDB_136105,IEDB_136906,IEDB_137472,IEDB_140088,IEDB_140529,IEDB_141794,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_150901,IEDB_151528,IEDB_190606,IEDB_2189047,IEDB_225177,IEDB_226811,IEDB_232584,IEDB_885823,IEDB_983931,SB_192,SB_7
The structure is contained in the following publication(s):
- Article ID: 81
Frirdich E, Lindner B, Holst O, Whitfield C "Overexpression of the waaZ gene leads to modification of the structure of the inner core region of Escherichia coli lipopolysaccharide, truncation of the outer core, and reduction of the amount of O polysaccharide on the cell surface" -
Journal of Bacteriology 185(5) (2003) 1659-1671
The waa gene cluster is responsible for the biosynthesis of the lipopolysaccharide (LPS) core region in Escherichia coli and Salmonella: Homologs of the waaZ gene product are encoded by the waa gene clusters of Salmonella enterica and E. coli strains with the K-12 and R2 core types. Overexpression of WaaZ in E. coli and S. enterica led to a modified LPS structure showing core truncations and (where relevant) to a reduction in the amount of O-polysaccharide side chains. Mass spectrometry and nuclear magnetic resonance spectroscopy were used to determine the predominant LPS structures in an E. coli isolate with an R1 core (waaZ is lacking from the type R1 waa gene cluster) with a copy of the waaZ gene added on a plasmid. Novel truncated LPS structures, lacking up to 3 hexoses from the outer core, resulted from WaaZ overexpression. The truncated molecules also contained a KdoIII residue not normally found in the R1 core
Lipopolysaccharide, biosynthesis, LPS, structure, core, gene, isolate, microbiology, strain, polysaccharide, cell, chain, molecule, Research, side chain, Escherichia, Escherichia coli, type, predominant, cluster, gene cluster, O-polysaccharide, O polysaccharide, spectrometry, Salmonella, core region, region, mass spectrometry, reduction, biochemistry, biophysics, hexose, Hexoses, homolog, inner core, lead, Magnetic Resonance Spectroscopy, medicine, modification, modified, nuclear, nuclear magnetic resonance, nuclear magnetic resonance spectroscopy, plasmid, resonance, Salmonella enterica, spectroscopy, surface
NCBI PubMed ID: 12591884Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Correspondence: cwhitfie@uoguelph.ca
Institutions: Department of Microbiology, University of Guelph, Guelph, Ontario N1G 2W1, Canada. Biophysics. Analytical Biochemistry, Research Center Borstel, Center for Medicine and Biosciences, D-23845 Borstel, Germany
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5. Compound ID: 307
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a-L-Rhap-(1-5)-+
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EtN-(1--P--7)--a-Kdop-(2-4)-+
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a-Kdop-(2-4)-+ |
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EtN-(1---P---P---4)-+ |
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a-D-Galp-(1-6)-+ | P-4)-+ |
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Hepp-(1-6)-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--/lipid A/
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L-gro-a-D-manHepp-(1-7)-+ |
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Structure type: oligomer
Aglycon: lipid A
Trivial name: core oligosaccharide
Compound class: LPS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130659,IEDB_130670,IEDB_133751,IEDB_136105,IEDB_136906,IEDB_137472,IEDB_140088,IEDB_140529,IEDB_141794,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_150901,IEDB_151528,IEDB_190606,IEDB_2189047,IEDB_225177,IEDB_226811,IEDB_232584,IEDB_885823,IEDB_983931,SB_192,SB_7
The structure is contained in the following publication(s):
- Article ID: 81
Frirdich E, Lindner B, Holst O, Whitfield C "Overexpression of the waaZ gene leads to modification of the structure of the inner core region of Escherichia coli lipopolysaccharide, truncation of the outer core, and reduction of the amount of O polysaccharide on the cell surface" -
Journal of Bacteriology 185(5) (2003) 1659-1671
The waa gene cluster is responsible for the biosynthesis of the lipopolysaccharide (LPS) core region in Escherichia coli and Salmonella: Homologs of the waaZ gene product are encoded by the waa gene clusters of Salmonella enterica and E. coli strains with the K-12 and R2 core types. Overexpression of WaaZ in E. coli and S. enterica led to a modified LPS structure showing core truncations and (where relevant) to a reduction in the amount of O-polysaccharide side chains. Mass spectrometry and nuclear magnetic resonance spectroscopy were used to determine the predominant LPS structures in an E. coli isolate with an R1 core (waaZ is lacking from the type R1 waa gene cluster) with a copy of the waaZ gene added on a plasmid. Novel truncated LPS structures, lacking up to 3 hexoses from the outer core, resulted from WaaZ overexpression. The truncated molecules also contained a KdoIII residue not normally found in the R1 core
Lipopolysaccharide, biosynthesis, LPS, structure, core, gene, isolate, microbiology, strain, polysaccharide, cell, chain, molecule, Research, side chain, Escherichia, Escherichia coli, type, predominant, cluster, gene cluster, O-polysaccharide, O polysaccharide, spectrometry, Salmonella, core region, region, mass spectrometry, reduction, biochemistry, biophysics, hexose, Hexoses, homolog, inner core, lead, Magnetic Resonance Spectroscopy, medicine, modification, modified, nuclear, nuclear magnetic resonance, nuclear magnetic resonance spectroscopy, plasmid, resonance, Salmonella enterica, spectroscopy, surface
NCBI PubMed ID: 12591884Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Correspondence: cwhitfie@uoguelph.ca
Institutions: Department of Microbiology, University of Guelph, Guelph, Ontario N1G 2W1, Canada. Biophysics. Analytical Biochemistry, Research Center Borstel, Center for Medicine and Biosciences, D-23845 Borstel, Germany
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6. Compound ID: 355
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a-Kdop-(2-4)-a-Kdop-(2-4)-+
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a-D-Manp-(1-4)-+ |
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a-D-Manp-(1-2)-D-gro-a-D-manHepp-(1-3)-D-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/ |
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Structure type: oligomer
Aglycon: lipid A
Trivial name: LPS II
Compound class: LPS
Contained glycoepitopes: IEDB_130650,IEDB_130659,IEDB_130701,IEDB_144983,IEDB_150901,IEDB_152206,IEDB_2189046,IEDB_983930,SB_44,SB_67,SB_72
The structure is contained in the following publication(s):
- Article ID: 102
Toman R, Skultety L "Structural study on a lipopolysaccharide from Coxiella burnetii strain Nine Mile in avirulent phase II" -
Carbohydrate Research 283 (1996) 175-185
A lipopolysaccharide isolated from Coxiella burnetii strain Nine Mile in avirulent phase II contains in the lipid A proximal region D-mannose, D-glycero-D-manno-heptose, and 3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) in the molar ratio 2:2:3. The primary structure 1 of the heptasaccharide was determined by glycose analysis, methylation analysis, ESI-MS, and FABMS. [sequence: see text]
Lipopolysaccharide, LPS, core, phase, strain, structural, D-mannose, Kdo, avirulent, Coxiella burnetii, D-glycero-D-manno-heptose, phase II, structural studies, strain Nine Mile
NCBI PubMed ID: 8901269Journal NLM ID: 0043535Publisher: Elsevier
Institutions: Institute of Virology, Slovak Academy of Sciences, Dubravska cesta 9, 842 46 Bratislava, Slovak Republic
Methods: methylation, FAB-MS, ESI-MS
- Article ID: 4830
Narasaki CT, Toman R "Lipopolysaccharide of Coxiella burnetii" -
Book: Coxiella burnetii: Recent Advances and New Perspectives in Research of the Q Fever Bacterium (series: Advances in Experimental Medicine and Biology) (2012) Vol. 984, 65-90
A lipopolysaccharide (LPS) is considered to be one of the major determinants of virulence expression and infection of virulent Coxiella burnetii. The LPSs from virulent phase I (LPS I) and from avirulent phase II (LPS II) bacteria were investigated for their chemical composition, structure and biological properties. LPS II is of rough (R) type in contrast to LPS I, which is phenotypically smooth (S) and contains a noticeable amount of two sugars virenose (Vir) and dihydrohydroxystreptose (Strep), which have not been found in other LPSs and can be considered as unique biomarkers of the bacterium. Both sugars were suggested to be located mostly in terminal positions of the O-specific chain of LPS I (O-PS I) and to be involved in the immunobiology of Q fever. There is a need to establish a more detailed chemical structure of LPS I in connection with prospective, deeper studies on mechanisms of pathogenesis and immunity of Q fever, its early and reliable diagnosis, and effective prophylaxis against the disease. This will also help to better understanding of host-pathogen interactions and contribute to improved modulation of pathological reactions which in turn are prerequisite for research and development of vaccines of new type. A fundamental understanding of C. burnetii LPS biosynthesis is still lacking. The intracellular nature of the bacterium, lack of genetic tools and its status as a selected agent have made elucidating basic physiological mechanisms challenging. The GDP-β-D-Vir biosynthetic pathway proposed most recently is an important initial step in this endeavour. The current advanced technologies providing the genetic tools necessary to screen C. burnetii mutants and propagate isogenic mutants might speed the discovery process.
Lipopolysaccharide, biosynthesis, structure, Coxiella burnetii, function, Q fever, Coxiella
NCBI PubMed ID: 22711627Publication DOI: 10.1007/978-94-007-4315-1_4Publisher: New York: Springer.
Correspondence: Rudolf.Toman@savba.sk
Editors: Toman R, Heinzen RA, Samuel JE, Mege J-L
Institutions: Center Department of Microbial and Molecular Pathogenesis, Texas A&M University Health Science, College Station, TX 77843, USA
- Article ID: 5643
Toman R, Vadovic P "Lipopolysaccharides of Coxiella burnetii: chemical composition and structure, and their role in diagnosis of Q fever" -
Book: BSL3 and BSL4 Agents: Proteomics, Glycomics, and Antigenicity (2011) Chapter 10, 115-123
Publication DOI: 10.1002/9783527638192.ch10Publisher: New York: J. Wiley & Sons Ltd
Correspondence: Toman R
Editors: Stulik J, Toman R, Butaye P, Ulrich RG
Institutions: Laboratory for Diagnosis and Prevention of Rickettsial and Chlamydial Infections, Institute of Virology, SAS, Bratislava, Slovakia
Methods: methylation, FAB-MS, ESI-MS, MALDI-MS, electrophoresis
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7. Compound ID: 905
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?%a-Kdop-(2-4)-a-Kdop-(2-4)-+
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?%b-D-GalpA-(1-6)-b-D-Glcp-(1-4)-+ |
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L-gro-a-D-manHepp-(1-7)-+ | |
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?%D-gro-a-D-manHepp-(1-2)-D-gro-a-D-manHepp-(1-2)-D-gro-a-D-manHepp-(1-2)-?%D-gro-a-D-manHepp-(1-6)-a-D-GlcpN-(1-4)-a-D-GalpA-(1-3)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/ |
Show graphically |
Structure type: oligomer
Aglycon: lipid A
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130650,IEDB_130659,IEDB_130670,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_150901,IEDB_151531,IEDB_2189046,IEDB_2189047,IEDB_226811,IEDB_983931,SB_192
The structure is contained in the following publication(s):
- Article ID: 261
Holst O "On the occurrence of D-glycero-D-manno-heptose in lipopolysaccharides" -
Polish Journal of Chemistry 73 (1999) 1055-1067
Lipopolysaccharides (LPS) consist of three regions, i.e. the lipid A, the core region, and the O-specific polysaccharide. The core region and the lipid A represent a common structural unit occurring in all LPS. The structures of the core region of various bacteria have been investigated intensively for the past ten years, and several core regions containing D-glycero-D-manno-heptose which is the biosynthetic precursor of the common core constituent L-glycero-D-manno-heptose have been identified. In this review, these core structures are summarized and briefly discussed.
Lipopolysaccharide, lipopolysaccharides, core, D-glycero-D-manno-heptose, composition, occurrence
Journal NLM ID: 7901356WWW link: http://www.ichf.edu.pl/pjch/pj-1999/pj0799.htm#1055Publisher: Państwowe Wydawnictwo Naukowe
Institutions: Research Center Borstel, Center for Medicine and Biosciences, 23845 Borstel, Germany
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8. Compound ID: 920
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a-Kdop-(2-4)-a-Kdop-(2-4)-+
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a-D-Manp-(1-?)-+ |
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a-D-Manp-(1-2)-D-gro-a-D-manHepp-(1-?)-D-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/ |
Show graphically |
Structure type: fragment of a bigger structure
Aglycon: lipid A
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130650,IEDB_130659,IEDB_130701,IEDB_144983,IEDB_150901,IEDB_152206,IEDB_2189046,IEDB_983930,SB_44,SB_67,SB_72
The structure is contained in the following publication(s):
- Article ID: 261
Holst O "On the occurrence of D-glycero-D-manno-heptose in lipopolysaccharides" -
Polish Journal of Chemistry 73 (1999) 1055-1067
Lipopolysaccharides (LPS) consist of three regions, i.e. the lipid A, the core region, and the O-specific polysaccharide. The core region and the lipid A represent a common structural unit occurring in all LPS. The structures of the core region of various bacteria have been investigated intensively for the past ten years, and several core regions containing D-glycero-D-manno-heptose which is the biosynthetic precursor of the common core constituent L-glycero-D-manno-heptose have been identified. In this review, these core structures are summarized and briefly discussed.
Lipopolysaccharide, lipopolysaccharides, core, D-glycero-D-manno-heptose, composition, occurrence
Journal NLM ID: 7901356WWW link: http://www.ichf.edu.pl/pjch/pj-1999/pj0799.htm#1055Publisher: Państwowe Wydawnictwo Naukowe
Institutions: Research Center Borstel, Center for Medicine and Biosciences, 23845 Borstel, Germany
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9. 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)-+ | |
| | |
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 |
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_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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10. Compound ID: 953
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?%a-Kdop-(2-4)-+
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EtN-(1--P--7)--a-Kdop-(2-4)-+
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EtN-(1-0)-?%P-0)-?%P-4)-+ |
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a-D-GlcpN-(1-7)-L-gro-a-D-manHepp-(1-7)-+ | |
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a-D-GlcpNAc-(1-3)-+ | | |
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a-D-Glcp-(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/
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?%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_130659,IEDB_130670,IEDB_133751,IEDB_136906,IEDB_137472,IEDB_140088,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_150901,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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11. 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)-+ |
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L-gro-a-D-manHepp-(1-7)-+ | |
| | |
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-(1-3)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/
|
?%P-4)-+ |
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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_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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12. Compound ID: 957
|
?%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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a-D-Glcp-(1-3)-+ | |
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?%L-gro-a-D-manHepp-(1-7)-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: core oligosaccharide with O-unit
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130659,IEDB_130670,IEDB_140088,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_150901,IEDB_2189047,IEDB_226811,IEDB_983931,SB_192
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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13. Compound ID: 1062
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a-D-GlcpNAc-(1-7)-L-gro-a-D-manHepp-(1-7)-+
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a-D-GlcpNAc-(1-3)-+ | a-Kdop-(2-4)-a-Kdop-(2-4)-+
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a-D-Glcp-(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 |
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Structure type: oligomer
Trivial name: R3 core oligosaccharide
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130650,IEDB_130659,IEDB_130670,IEDB_136906,IEDB_137472,IEDB_140088,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_150901,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: 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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14. 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)-+
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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-(1-3)-L-gro-a-D-manHepp-(1-5)-Kdo |
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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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15. Compound ID: 2381
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P-4)-+
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a-Kdop-(2-4)-a-Kdop-(2-4)-a-Kdop-(2-6)-b-D-GlcpN-(1-6)-a-D-GlcpN-(1-P |
Show graphically |
Structure type: oligomer
Trivial name: core-lipid A carbohydrate backbone, epitope I
Compound class: core oligosaccharide, LPS
Contained glycoepitopes: IEDB_130650,IEDB_130659,IEDB_135394,IEDB_137340,IEDB_140092,IEDB_141807,IEDB_150901,IEDB_150908,IEDB_151531
The structure is contained in the following publication(s):
- Article ID: 814
Holst O, Bock K, Brade L, Brade H "The structures of oligosaccharide bisphosphates isolated from the lipopolysaccharide of a recombinant Escherichia coli strain expressing the gene gseA [3-deoxy-D-manno-octulopyranosonic acid (Kdo) transferase] of Chlamydia psittaci 6BC" -
European Journal of Biochemistry 229 (1995) 194-200
The lipopolysaccharide from the recombinant strain Escherichia coli F515-140 containing the cloned gene gseA [3-deoxy-D-manno-octulopyranosonic acid (Kdo) transferase] from Chlamydia psittaci 6BC was isolated and sequentially de-O-acylated and de-N-acylated. The products were separated by high-performance anion-exchange chromatography into three fractions, two of which contained a single compound. Their structures were elucidated by high-field NMR spectroscopy as α-Kdo-(2→4)-α-Kdo-(2→6)-β-D-GlcN-(1→6)-α-D-GlcN 1,4'-P2 (compound 1) (tetrasaccharide bisphosphate) [Holst, O., Broer, W., Thomas-Oates, J. E., Mamat, U. & Brade, H. (1993) Eur. J. Biochem. 214, 703-710] and α-Kdo-(2→4)-[α-Kdo-(2→8)-]-α-Kdo-(2→4)-α-Kdo-(2→6)-β-D-GlcN-(1→6)-α-D-GlcN 1,4'-P2 (compound 4) (hexasaccharide bisphosphate). The third fraction comprised two pentasaccharide bisphosphates, which could be separated by affinity chromatography using an immobilized monoclonal antibody specific for the trisaccharide α-Kdo-(2→8)-α-Kdo-(2→4)-α-Kdo. The bound fraction was identified as α-Kdo-(2→8)-α-Kdo-(2→4)-α-Kdo-(2→6)-β-D-GlcN-(1→6)-α-D-GlcN 1,4'-P2 (compound 2) [Holst, O., Broer, W., Thomas-Oates, J. E., Mamat, U. & Brade, H. (1993) Eur. J. Biochem. 214, 703-710], whereas the unbound fraction was identified as α-Kdo-(2→4)-α-Kdo-(2→4)-α-Kdo-(2→6)-β-D-GlcN-(1→6)-α-D-GlcN 1,4'-P2 (compound 3). This novel Kdo tetrasaccharide extends our knowledge on multifunctional Kdo transferases.
Lipopolysaccharide, LPS, oligosaccharide, structure, core, gene, strain, Escherichia, Escherichia coli, acid, Kdo, transferase, phosphate, Chlamydia, recombinant, bisphosphate, Chlamydia psittaci, gseA, HPLC
NCBI PubMed ID: 7744029Publication DOI: 10.1111/j.1432-1033.1995.0194l.xJournal NLM ID: 0107600Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
Correspondence: oholst@fz-borstel.de
Institutions: Division of Biochemical Microbiology, Forschungsinstitut Borstel, Germany, Division of Biochemical Microbiology, Institut fur Experimentelle Biologie und Medizin, Forschungsinstitut Borstel, Germany, Department of Chemistry, Carisberg Laboratory, Copenhagen, Denmark
Methods: 13C NMR, 1H NMR, GLC-MS, 31P NMR, HPAEC, affinity chromatography
- Article ID: 1157
Rund S, Lindner B, Brade H, Holst O "Structural analysis of the lipopolysaccharide from Chlamydophila psittaci strain 6BC" -
European Journal of Biochemistry 267(18) (2000) 5717-5726
The lipopolysaccaride of Chlamydophila psittaci 6BC was isolated from tissue culture-grown elementary bodies using a modified phenol/water procedure followed by extraction with phenol/chloroform/light petroleum. Compositional analyses indicated the presence of 3-deoxy-Dmanno-oct-2-ulosonic acid, GlcN, organic bound phosphate and fatty acids in a molar ratio of approximately 3. 3 : 2 : 1.8 : 4.6. Deacylated lipopolysaccharide was obtained after successive microscale treatment with hydrazine and potassium hydroxide, and was then separated by high performance anion-exchange chromatography into two major fractions, the structures of which were determined by 600 MHz NMR spectroscopy as α-Kdo-(2→8)-α-Kdo-(2→4)-α-Kdo-(2→6)-β-D-GlcpN-(1→6)-α-D-GlcpN 1,4'-bisphosphate and α-Kdo-(2→4)-[α-Kdo-(2→8)]-α-Kdo-(2→4)-α-Kdo-(2→6)-β-D-GlcpN-(1→6)-α-D-GlcpN 1,4'-bisphosphate. The distribution of fatty acids in lipid A was determined by compositional analyses andmatrix-assisted laser desorption/ionization time-of-flight mass spectrometry experiments on lipid A and de-O-acylated lipid A. It was shown that the carbohydrate backbone of lipid A is replaced by a complex mixture of fatty acids, including long-chain and branched (R)-configured 3-hydroxy fatty acids, the latter being exclusively present in an amide linkage
Lipopolysaccharide, strain, structural, serotype, analysis, structural analysis, Chlamydophila psittaci, NMR spectroscopy, mass spectrometry
NCBI PubMed ID: 10971582Journal NLM ID: 0107600Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
Correspondence: oholst@fz-borstel.de
Institutions: Divisions of Medical and Biochemical Microbiology and Biophysics, Research Center Borstel, Center for Medicine and Biosciences, Germany
Methods: 13C NMR, 1H NMR, NMR-2D, MALDI-TOF MS
- Article ID: 1386
Brabetz W, Lindner B, Brade H "Comparative analyses of secondary gene products of 3-deoxy-D-manno-oct-2-ulosonic acid transferases from Chlamydiaceae in Escherichia coli K-12" -
European Journal of Biochemistry 267(17) (2000) 5458-5465
The waaA gene encoding the essential, lipopolysaccharide (LPS)-specific 3-deoxy-Dmanno-oct-2-ulosonic acid (Kdo) transferase was inactivated in the chromosome of a heptosyltransferase I and II deficient Escherichia coli K-12 strain by insertion of gene expression cassettes encoding the waaA genes of Chlamydia trachomatis, Chlamydophila pneumoniae or Chlamydophila psittaci. The three chlamydial Kdo transferases were able to complement the knockout mutation without changing the growth or multiplication behaviour. The LPS of the mutants were serologically and structurally characterized in comparison to the LPS of the parent strain using compositional analyses, high performance anion exchange chromatography, matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and specific monoclonal antibodies. The data show that chlamydial Kdo transferases can replace in E. coli K-12 the host's Kdo transferase and retain the product specificities described in their natural background. In addition, we unequivocally proved that WaaA from C. psittaci transfers predominantly four Kdo residues to lipid A, forming a branched tetrasaccharide with the structure α-Kdo-(2→8)-[α-Kdo-(2→4)]-α-Kdo-(2→4)-α-Kdo.
Lipopolysaccharide, LPS, gene, Escherichia, Escherichia coli, 3-deoxy-D-manno-oct-2-ulosonic acid, acid, Kdo, transferase, transferases, Chlamydiaceae, genetic complementation, multifunctional 3-deoxy-D-manno-oct-2, product specificity, ulosonic acid transferases
NCBI PubMed ID: 10951204Journal NLM ID: 0107600Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
Correspondence: wbrabetz@fz-borstel.de
Institutions: Division of Medical and Biochemical Microbiology, Research Center Borstel, Center for Medicine and Biosciences, Borstel, Germany, Divizion of Medical and Biochemical Microbiology, Research Centre Borstel, Centre for Medicine and Biosciences,Borstel,Germany
- Article ID: 3825
Brooks CL, Müller-Loennies S, Borisova SN, Brade L, Kosma P, Hirama T, MacKenzie CR, Brade H, Evans SV "Antibodies raised against chlamydial lipopolysaccharide antigens reveal convergence in germline gene usage and differential epitope recognition" -
Biochemistry 49(3) (2010) 570-581
The structures of antigen-binding fragments from two related monoclonal antibodies have been determined to high resolution in the presence of several carbohydrate antigens raised against chlamydial lipopolysaccharide. With the exception of CDR H3, antibodies S54-10 and S73-2 are both derived from the same set of germline gene segments as the previously reported structures S25-2 and S45-18. Despite this similarity, the antibodies differ in specificity and the mechanism by which they recognize their cognate antigen. S54-10 uses an unrelated CDR H3 to recognize its antigen in a fashion analogous to S45-18; however, S73-2 recognizes the same antigen as S45-18 and S54-10 in a wholly unrelated manner. Together, these antibody-antigen structures provide snapshots into how the immune system uses the same set of inherited germline gene segments to generate multiple possible specificities that allow for differential recognition of epitopes and how unrelated CDR H3 sequences can result in convergent binding of clinically relevant bacterial antigens.
antibodies, epitope, recognition, antigens, Chlamydia, binding
NCBI PubMed ID: 20000757Journal NLM ID: 0370623Publisher: American Chemical Society
Correspondence: hebra@fz-borstel.de; svevans@uvic.ca
Institutions: University of Victoria, Department of Biochemistry and Microbiology, PO Box 3055 STN CSC, Victoria, BC, Canada V8P 3P6
Methods: ELISA, serological methods, genetic methods, crystallization, surface plasmon resonance (SPR)
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