Found 22 structures.
Displayed structures from 1 to 15
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1. Compound ID: 5989
|
a-L-Fucp2Me-(1-6)-+
|
dPam-(1-2)-b-D-GlcpN-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcNAc |
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Structure type: oligomer
; 1388 [M+H]+
Trivial name: NodBj-V (C16:1, MeFuc)
Contained glycoepitopes: IEDB_135813,IEDB_136045,IEDB_137340,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_151531,IEDB_152214,IEDB_153212,IEDB_174333,IEDB_241099,SB_74,SB_85,SB_86
The structure is contained in the following publication(s):
- Article ID: 2669
Carlson RW, Sanjuan J, Bhat UR, Glushka J, Spaink HP, Wijfjes AHM, Van Brussel AAN, Stokkermans TJW, Peters NK, Stacey G "The structures and biological activities of the lipo-oligosaccharide nodulation signals produced by type I and II strains of Bradyrhizobium japonicum" -
Journal of Biological Chemistry 268 (1993) 18372-18381
Bradyrhizobium japonicum produces lipo-oligosaccharide signal molecules that induce deformation of root hairs and meristematic activity on soybeans. B. japonicum USDA135 (a Type I strain) produces modified chitin pentasaccharide molecules with either a terminal N-C16:0- or N-C18:1-glucosamine with and without an O-acetyl group at C-6 and with 2-O-methylfucose linked to C-6 of the reducing N-acetylglucosamine. An additional molecule has N-C16:1-glucosamine and no O-acetyl group. All of these molecules cause root hair deformation on Vicia sativa and Glycine soja. The C18:1-containing molecules were tested and found to induce meristem formation on G. soja. USDA61 (a Type II strain) produces eight additional molecules. Five have a carbamoyl group on the terminal N-acylglucosamine. Six have chitin tetrasaccharide backbones. Three have a terminal N-acyl-N-methylglucosaminosyl residue. In four molecules, the reducing-end N-acetylglucosamine is glycosidically linked to glycerol and has a branching fucosyl, rather than a 2-O-methylfucosyl, residue. One molecule has a terminal N-acylglucosamine that has both acetyl and carbamoyl groups (one each).
NCBI PubMed ID: 8349712Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Institutions: Complex Carbohydrate Research Center, University of Georgia, Athens 30602-4712, Department of Microbiology and the Center for Legume Research, University of Tennessee, Knoxville, lknnessee 37996, Institute of Molecular Plant Sciences, Leiden University, 2311 VJ Leiden, The Netherlands, Ohio State Biotechnology Center, Ohio State University, Columbus, Ohio 43210
Methods: 1H NMR, NMR-2D, FAB-MS, GC-MS, TLC, biological assays, composition analysis, NMR-1D
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2. Compound ID: 8803
|
Lau-(1-3)-3HOMyr-(1-2)-+ 3HOMyr-(1-2)-+
| |
dPam-(1-3)-3HOMyr-(1-3)-b-D-GlcpN-(1-6)-a-D-GlcpN-(1---P-P
| |
b-L-Arap4N-(1--P--4)--+ 3HOMyr-(1-3)-+ |
Show graphically |
Structure type: oligomer
Compound class: lipid A
Contained glycoepitopes: IEDB_135394,IEDB_135515,IEDB_141807,IEDB_151531,IEDB_534864
The structure is contained in the following publication(s):
- Article ID: 3813
Anisimov AP, Dentovskaya SV, Kondakova AN, Lindner B, Shaikhutdinova RZ, Kocharova NA, Senchenkova SN, Knirel YA "Yersinia pestis lipopolysaccharide in host-pathogen interactions" -
Book: The Challenge of Highly Pathogenic Microorganisms - Mechanism of Virulence and Novel Medical Countermeasures (2010) Chapter 8, 77-87
Analysis of bacterial genomes revealed the phylogenetic proximity of predicted enzymes responsible for biosynthesis of lipopolysaccharide (LPS) of Yersinia pestis, the cause of plague, to homologous proteins of Yersinia spp. and some distantly related bacteria (Serratia proteamaculans, Erwinia carotovora, Burkholderia dolosa, Photorhabdus luminescens and others). Isogenic Y.pestis strains with single or double mutations in 14 genes of LPS biosynthetic pathways were constructed. Using high-resolution electrospray ionization mass spectrometry, the full LPS structures were elucidated in each mutant, and the sequence of monosaccharide transfers in the assembly of the LPS core was inferred. Truncation of the core decreased significantly the resistance of bacteria to normal human serum (NHS) and polymyxin B. Impairing of LPS biosynthesis resulted also in reduction of LPS-dependent enzymatic activities of plasminogen activator. A gradual truncation of the LPS core was accompanied by a decrease of bacterial virulence in mice and guinea pigs. However, the reduction in virulence remained behind the decrease of bacterial resistance to innate immunity factors. For instance, waaQ mutant deficient in HepIII transferase was highly susceptible to polymyxin B and NHS but was as virulent as the parental strain for both animals. Y.pestis mutants with two or less sugar residues in the LPS core were not only susceptible to antimicrobial cationic peptides and NHS but also avirulent in animal infection models. This finding demonstrated that the LPS structure is critical for the lethality of plague infection, and waaC, hldE and waaA or their protein products can be considered as promising candidates for targeting Y.pestis virulence using specific inhibitors. As the identities of the corresponding enzymes to non-yersiniae protein homologs are less than 90%, it seems possible to fit an inhibitor to each of the targets that will not affect normal commensal microflora in mammalian host.
Lipopolysaccharide, Yersinia pestis, host-pathogen interactions
Publication DOI: 10.1007/978-90-481-9054-6_8Publisher: Springer
Correspondence: a-p-anisimov@yandex.ru
Editors: Schafferman A, Ordentlich A
Institutions: State Research Center for Applied Microbiology and Biotechnology, Obolensk, 142279, Moscow Region, Russia, N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, 47, Leninskii Prospect, Moscow, Russia, Research Center Borstel, D-23457, Borstel, Germany
Methods: ESI-MS, mild acid hydrolysis, serological methods
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3. Compound ID: 9165
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P-4)-+ 3HOMyr-(1-2)-+
| |
dPam-(1-3)-3HOMyr-(1-2)-b-D-GlcpN-(1-6)-a-D-GlcpN-(1-P
|
3HOMyr-(1-3)-+ |
Show graphically |
Structure type: oligomer
; 1414
Compound class: lipid A
Contained glycoepitopes: IEDB_135394,IEDB_141807,IEDB_151531
The structure is contained in the following publication(s):
- Article ID: 3928
Pérez-Gutiérrez C, Llobet E, Llompart CM, Reinés M, Bengoechea JA "Role of lipid A acylation in Yersinia enterocolitica virulence" -
Infection and Immunity 78(6) (2010) 2768-2781
Yersinia enterocolitica is an important human pathogen. Y. enterocolitica must adapt to the host environment, and temperature is an important cue regulating the expression of most Yersinia virulence factors. Here, we report that Y. enterocolitica 8081 serotype O:8 synthesized tetra-acylated lipid A at 37 degrees C but that hexa-acylated lipid A predominated at 21 degrees C. By mass spectrometry and genetic methods, we have shown that the Y. enterocolitica msbB, htrB, and lpxP homologues encode the acyltransferases responsible for the addition of C(12), C(14) and C(16:1), respectively, to lipid A. The expression levels of the acyltransferases were temperature regulated. Levels of expression of msbB and lpxP were higher at 21 degrees C than at 37 degrees C, whereas the level of expression of htrB was higher at 37 degrees C. At 21 degrees C, an lpxP mutant was the strain most susceptible to polymyxin B, whereas at 37 degrees C, an htrB mutant was the most susceptible. We present evidence that the lipid A acylation status affects the expression of Yersinia virulence factors. Thus, expression of flhDC, the flagellar master regulatory operon, was downregulated in msbB and lpxP mutants, with a concomitant decrease in motility. Expression of the phospholipase yplA was also downregulated in both mutants. inv expression was downregulated in msbB and htrB mutants, and consistent with this finding, invasion of HeLa cells was diminished. However, the expression of rovA, the positive regulator of inv, was not affected in the mutants. The levels of pYV-encoded virulence factors Yops and YadA in the acyltransferase mutants were not affected. Finally, we show that only the htrB mutant was attenuated in vivo.
lipid A, Yersinia enterocolitica, virulence factor, acylation
NCBI PubMed ID: 20385763Journal NLM ID: 0246127Publisher: American Society for Microbiology
Correspondence: bengoechea@caubet-cimera.es
Institutions: Fundació Caubet- CIMERA Illes Balears, Recinto Hospital Joan March, Carretera Soller km 12, 07110 Bunyola, Spain, Área de Microbiología, Facultad Biología, Universitat Illes Balears, Palma Mallorca, Consejo Superior de Investigaciones Científicas (CSIC), Madrid, Spain
Methods: virulence assays, PCR, SDS-PAGE, MALDI-TOF MS, biological assays, genetic methods, statistical analysis
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4. Compound ID: 9166
|
Lau-(1-3)-3HOMyr-(1-3)-+ 3HOMyr-(1-2)-+
| |
dPam-(1-3)-3HOMyr-(1-2)-b-D-GlcpN-(1-6)-a-D-GlcpN-(1-P
| |
P-4)-+ 3HOMyr-(1-3)-+ |
Show graphically |
Structure type: oligomer
; 1824
Compound class: lipid A
Contained glycoepitopes: IEDB_135394,IEDB_135515,IEDB_141807,IEDB_151531,IEDB_534864
The structure is contained in the following publication(s):
- Article ID: 3928
Pérez-Gutiérrez C, Llobet E, Llompart CM, Reinés M, Bengoechea JA "Role of lipid A acylation in Yersinia enterocolitica virulence" -
Infection and Immunity 78(6) (2010) 2768-2781
Yersinia enterocolitica is an important human pathogen. Y. enterocolitica must adapt to the host environment, and temperature is an important cue regulating the expression of most Yersinia virulence factors. Here, we report that Y. enterocolitica 8081 serotype O:8 synthesized tetra-acylated lipid A at 37 degrees C but that hexa-acylated lipid A predominated at 21 degrees C. By mass spectrometry and genetic methods, we have shown that the Y. enterocolitica msbB, htrB, and lpxP homologues encode the acyltransferases responsible for the addition of C(12), C(14) and C(16:1), respectively, to lipid A. The expression levels of the acyltransferases were temperature regulated. Levels of expression of msbB and lpxP were higher at 21 degrees C than at 37 degrees C, whereas the level of expression of htrB was higher at 37 degrees C. At 21 degrees C, an lpxP mutant was the strain most susceptible to polymyxin B, whereas at 37 degrees C, an htrB mutant was the most susceptible. We present evidence that the lipid A acylation status affects the expression of Yersinia virulence factors. Thus, expression of flhDC, the flagellar master regulatory operon, was downregulated in msbB and lpxP mutants, with a concomitant decrease in motility. Expression of the phospholipase yplA was also downregulated in both mutants. inv expression was downregulated in msbB and htrB mutants, and consistent with this finding, invasion of HeLa cells was diminished. However, the expression of rovA, the positive regulator of inv, was not affected in the mutants. The levels of pYV-encoded virulence factors Yops and YadA in the acyltransferase mutants were not affected. Finally, we show that only the htrB mutant was attenuated in vivo.
lipid A, Yersinia enterocolitica, virulence factor, acylation
NCBI PubMed ID: 20385763Journal NLM ID: 0246127Publisher: American Society for Microbiology
Correspondence: bengoechea@caubet-cimera.es
Institutions: Fundació Caubet- CIMERA Illes Balears, Recinto Hospital Joan March, Carretera Soller km 12, 07110 Bunyola, Spain, Área de Microbiología, Facultad Biología, Universitat Illes Balears, Palma Mallorca, Consejo Superior de Investigaciones Científicas (CSIC), Madrid, Spain
Methods: virulence assays, PCR, SDS-PAGE, MALDI-TOF MS, biological assays, genetic methods, statistical analysis
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5. Compound ID: 9431
|
Lau-(1-3)-3HOMyr-(1-3)-+ 3HOMyr-(1-2)-+
| |
dPam-(1-3)-3HOMyr-(1-2)-b-D-GlcpN-(1-6)-a-D-GlcpN-(1---P-P
| |
b-L-Arap4N-(1--P--4)--+ 3HOMyr-(1-3)-+ |
Show graphically |
Structure type: fragment of a bigger structure
Compound class: lipid A
Contained glycoepitopes: IEDB_135394,IEDB_135515,IEDB_141807,IEDB_151531,IEDB_534864
The structure is contained in the following publication(s):
- Article ID: 4011
Dentovskaya SV, Anisimov AP, Kondakova AN, Bystrova OV, Lindner B, Svetoch TE, Shaikhutdinova RZ, Ivanov SA, Bakhteeva IV, Titareva GM, Knirel YA "Functional characterization and biological significance of Yersinia pestis lipopolysaccharide biosynthesis genes" -
Biochemistry (Moscow) 76(7) (2011) 808-822
In silico analysis of available bacterial genomes revealed the phylogenetic proximity levels of enzymes responsible for biosynthesis of lipopolysaccharide (LPS) of Yersinia pestis, the cause of plague, to homologous proteins of closely related Yersinia spp. and some other bacteria (Serratia proteamaculans, Erwinia carotovora, Burkholderia dolosa, Photorhabdus luminescens and others). Isogenic Y. pestis mutants with single or double mutations in 14 genes of LPS biosynthetic pathways were constructed by site-directed mutagenesis on the base of the virulent strain 231 and its attenuated derivative. Using high-resolution electrospray ionization mass spectrometry, the full LPS structures were elucidated in each mutant, and the sequence of monosaccharide transfers in the assembly of the LPS core was inferred. Truncation of the core decreased significantly the resistance of bacteria to normal human serum and polymyxin B, the latter probably as a result of a less efficient incorporation of 4-amino-4-deoxyarabinose into lipid A. Impairing of LPS biosynthesis resulted also in reduction of LPS-dependent enzymatic activities of plasminogen activator and elevation of LD(50) and average survival time in mice and guinea pigs infected with experimental plague. Unraveling correlations between biological properties of bacteria and particular LPS structures may help a better understanding of pathogenesis of plague and implication of appropriate genes as potential molecular targets for treatment of plague.
virulence, lipopolysaccharide biosynthesis, serum resistance, Yersinia pestis, antimicrobial-peptide resistance, fibrinolytic activity, coagulase activity
NCBI PubMed ID: 21999543Publication DOI: 10.1134/S0006297911070121Journal NLM ID: 0376536Publisher: Nauka/Interperiodica
Correspondence: annakond@gmail.com
Institutions: Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, State Research Center for Applied Microbiology and Biotechnology, 142279, Obolensk, Moscow Region, Russia, Research Center Borstel, Center for Medicine and Biosciences, Parkallee 22, D-23485, Borstel, Germany
Methods: PCR, SDS-PAGE, DNA techniques, ESI-MS, serological methods, genetic methods
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6. Compound ID: 9432
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3HOMyr-(1-2)-+
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b-L-Arap4N-(1--P--4)--+ |
| |
dPam-(1-3)-3HOMyr-(1-2)-+ | |
| | |
EtN-(1--P--7)--/Variants 0/-+ | | |
| | | |
?%b-D-GlcpNAc-(1-3)-+ b-D-Glcp-(1-4)-+ | | | |
| | | | | |
/Variants 1/-L-gro-a-D-manHepp-(1-7)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2-6)-b-D-GlcpN-(1-6)-a-D-GlcpN-(1---P-P
| |
Lau-(1-3)-3HOMyr-(1-3)-+ 3HOMyr-(1-3)-+
/Variants 0/ is:
a-Kop-(2-4)-
OR (exclusively)
a-Kdop-(2-4)-
/Variants 1/ is:
b-D-Galp-(1-7)-
OR (exclusively)
D-gro-a-D-manHepp-(1-7)- |
Show graphically |
Structure type: oligomer
Compound class: LPS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130659,IEDB_130670,IEDB_135394,IEDB_135515,IEDB_135607,IEDB_135609,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_150908,IEDB_151531,IEDB_190606,IEDB_2189046,IEDB_2189047,IEDB_226811,IEDB_534864,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 4011
Dentovskaya SV, Anisimov AP, Kondakova AN, Bystrova OV, Lindner B, Svetoch TE, Shaikhutdinova RZ, Ivanov SA, Bakhteeva IV, Titareva GM, Knirel YA "Functional characterization and biological significance of Yersinia pestis lipopolysaccharide biosynthesis genes" -
Biochemistry (Moscow) 76(7) (2011) 808-822
In silico analysis of available bacterial genomes revealed the phylogenetic proximity levels of enzymes responsible for biosynthesis of lipopolysaccharide (LPS) of Yersinia pestis, the cause of plague, to homologous proteins of closely related Yersinia spp. and some other bacteria (Serratia proteamaculans, Erwinia carotovora, Burkholderia dolosa, Photorhabdus luminescens and others). Isogenic Y. pestis mutants with single or double mutations in 14 genes of LPS biosynthetic pathways were constructed by site-directed mutagenesis on the base of the virulent strain 231 and its attenuated derivative. Using high-resolution electrospray ionization mass spectrometry, the full LPS structures were elucidated in each mutant, and the sequence of monosaccharide transfers in the assembly of the LPS core was inferred. Truncation of the core decreased significantly the resistance of bacteria to normal human serum and polymyxin B, the latter probably as a result of a less efficient incorporation of 4-amino-4-deoxyarabinose into lipid A. Impairing of LPS biosynthesis resulted also in reduction of LPS-dependent enzymatic activities of plasminogen activator and elevation of LD(50) and average survival time in mice and guinea pigs infected with experimental plague. Unraveling correlations between biological properties of bacteria and particular LPS structures may help a better understanding of pathogenesis of plague and implication of appropriate genes as potential molecular targets for treatment of plague.
virulence, lipopolysaccharide biosynthesis, serum resistance, Yersinia pestis, antimicrobial-peptide resistance, fibrinolytic activity, coagulase activity
NCBI PubMed ID: 21999543Publication DOI: 10.1134/S0006297911070121Journal NLM ID: 0376536Publisher: Nauka/Interperiodica
Correspondence: annakond@gmail.com
Institutions: Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, State Research Center for Applied Microbiology and Biotechnology, 142279, Obolensk, Moscow Region, Russia, Research Center Borstel, Center for Medicine and Biosciences, Parkallee 22, D-23485, Borstel, Germany
Methods: PCR, SDS-PAGE, DNA techniques, ESI-MS, serological methods, genetic methods
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7. Compound ID: 9433
|
3HOMyr-(1-2)-+
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?%b-L-Arap4N-(1--P--4)--+ |
| |
?%dPam-(1-3)-3HOMyr-(1-2)-+ | |
| | |
EtN-(1--P--7)--/Variants 0/-+ | | |
| | | |
?%b-D-GlcpNAc-(1-3)-+ b-D-Glcp-(1-4)-+ | | | |
| | | | | |
/Variants 1/-L-gro-a-D-manHepp-(1-7)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2-6)-b-D-GlcpN-(1-6)-a-D-GlcpN-(1---P-P
| |
?%Lau-(1-3)-3HOMyr-(1-3)-+ 3HOMyr-(1-3)-+
/Variants 0/ is:
a-Kop-(2-4)-
OR (exclusively)
a-Kdop-(2-4)-
/Variants 1/ is:
b-D-Galp-(1-7)-
OR (exclusively)
D-gro-a-D-manHepp-(1-7)- |
Show graphically |
Structure type: oligomer
Compound class: LPS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130659,IEDB_130670,IEDB_135394,IEDB_135515,IEDB_135607,IEDB_135609,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_150908,IEDB_151531,IEDB_190606,IEDB_2189046,IEDB_2189047,IEDB_226811,IEDB_534864,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 4011
Dentovskaya SV, Anisimov AP, Kondakova AN, Bystrova OV, Lindner B, Svetoch TE, Shaikhutdinova RZ, Ivanov SA, Bakhteeva IV, Titareva GM, Knirel YA "Functional characterization and biological significance of Yersinia pestis lipopolysaccharide biosynthesis genes" -
Biochemistry (Moscow) 76(7) (2011) 808-822
In silico analysis of available bacterial genomes revealed the phylogenetic proximity levels of enzymes responsible for biosynthesis of lipopolysaccharide (LPS) of Yersinia pestis, the cause of plague, to homologous proteins of closely related Yersinia spp. and some other bacteria (Serratia proteamaculans, Erwinia carotovora, Burkholderia dolosa, Photorhabdus luminescens and others). Isogenic Y. pestis mutants with single or double mutations in 14 genes of LPS biosynthetic pathways were constructed by site-directed mutagenesis on the base of the virulent strain 231 and its attenuated derivative. Using high-resolution electrospray ionization mass spectrometry, the full LPS structures were elucidated in each mutant, and the sequence of monosaccharide transfers in the assembly of the LPS core was inferred. Truncation of the core decreased significantly the resistance of bacteria to normal human serum and polymyxin B, the latter probably as a result of a less efficient incorporation of 4-amino-4-deoxyarabinose into lipid A. Impairing of LPS biosynthesis resulted also in reduction of LPS-dependent enzymatic activities of plasminogen activator and elevation of LD(50) and average survival time in mice and guinea pigs infected with experimental plague. Unraveling correlations between biological properties of bacteria and particular LPS structures may help a better understanding of pathogenesis of plague and implication of appropriate genes as potential molecular targets for treatment of plague.
virulence, lipopolysaccharide biosynthesis, serum resistance, Yersinia pestis, antimicrobial-peptide resistance, fibrinolytic activity, coagulase activity
NCBI PubMed ID: 21999543Publication DOI: 10.1134/S0006297911070121Journal NLM ID: 0376536Publisher: Nauka/Interperiodica
Correspondence: annakond@gmail.com
Institutions: Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, State Research Center for Applied Microbiology and Biotechnology, 142279, Obolensk, Moscow Region, Russia, Research Center Borstel, Center for Medicine and Biosciences, Parkallee 22, D-23485, Borstel, Germany
Methods: PCR, SDS-PAGE, DNA techniques, ESI-MS, serological methods, genetic methods
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8. Compound ID: 10199
|
/Variants 0/-+
|
a-D-S6Quip-(1-3)-D-Gro
|
Subst-(1-1)-+
/Variants 0/ is:
54%dPam-(1-2)-
OR (exclusively)
24%Pam-(1-2)-
OR (exclusively)
22%Myr-(1-2)-
Subst = thioacyl |
Show graphically |
Structure type: oligomer
Trivial name: 3'-(6-Sulfoquinovosyl)-2'-O-acyl-l'-O-thioacyl-sn-Gro
Compound class: thionsulfonolipid
Contained glycoepitopes: IEDB_141181,IEDB_176772
The structure is contained in the following publication(s):
- Article ID: 4236
Ishizuka I "Chemistry and functional distribution of sulfoglycolipids" -
Progress in Lipid Research 36 (1997) 245-319
No abstract
NCBI PubMed ID: 9640458Publication DOI: 10.1016/S0163-7827(97)00011-8Journal NLM ID: 7900832Publisher: Oxford; Elmsford, NY, Pergamon Press
Institutions: Teikyo University School of Medicine, Tokyo, Japan
Methods: 1H NMR, IR, FAB-MS, Azure A assay
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9. Compound ID: 10609
|
?%Lau-(1-3)-3HOMyr-(1-3)-+ 3HOMyr-(1-2)-+
| |
?%dPam-(1-3)-3HOMyr-(1-2)-b-D-GlcpN-(1-6)-a-D-GlcpN-(1--P--1)--b-L-Arap4N
| |
b-L-Arap4N-(1--P--4)--+ 3HOMyr-(1-3)-+ |
Show graphically |
Structure type: oligomer
Compound class: lipid A
Contained glycoepitopes: IEDB_135394,IEDB_135515,IEDB_141807,IEDB_151531,IEDB_534864
The structure is contained in the following publication(s):
- Article ID: 4330
Knirel YA, Anisimov AP "Lipopolysaccharide of Yersinia pestis, the cause of plague: structure, genetics, biological properties" -
Acta Naturae 4(3) (2012) 46-58
The present review summarizes data pertaining to the composition and structure of the carbohydrate moiety (core oligosaccharide) and lipid component (lipid A) of the various forms of lipopolysaccharide (LPS), one of the major pathogenicity factors ofYersinia pestis, the cause of plague. The review addresses the functions and the biological significance of genes for the biosynthesis of LPS, as well as the biological properties of LPS in strains from various intraspecies groups ofY. pestis and their mutants, including the contribution of LPS to the resistance of bacteria to factors of the innate immunity of both insect-vectors and mammal-hosts. Special attention is paid to temperature-dependent variations in the LPS structure, their genetic control and roles in the pathogenesis of plague. The evolutionary aspect is considered based on a comparison of the structure and genetics of the LPS ofY. pestis and other enteric bacteria, including otherYersinia species. The prospects of development of live plague vaccines created on the basis ofY. pestis strains with the genetically modified LPS are discussed.
Lipopolysaccharide, lipid A, immune response, Yersinia pestis, Plague, antibiotic resistance
NCBI PubMed ID: 23150803Journal NLM ID: 101525823Publisher: Moscow: Park Media Ltd
Correspondence: knirel@ioc.ac.ru
Institutions: Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia
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10. Compound ID: 10610
|
P-4)-+ 3HOMyr-(1-2)-+
| |
dPam-(1-3)-3HOMyr-(1-2)-b-D-GlcpN-(1-6)-a-D-GlcpN-(1-P
|
3HOMyr-(1-3)-+ |
Show graphically |
Structure type: oligomer
Compound class: lipid A
Contained glycoepitopes: IEDB_135394,IEDB_141807,IEDB_151531
The structure is contained in the following publication(s):
- Article ID: 4330
Knirel YA, Anisimov AP "Lipopolysaccharide of Yersinia pestis, the cause of plague: structure, genetics, biological properties" -
Acta Naturae 4(3) (2012) 46-58
The present review summarizes data pertaining to the composition and structure of the carbohydrate moiety (core oligosaccharide) and lipid component (lipid A) of the various forms of lipopolysaccharide (LPS), one of the major pathogenicity factors ofYersinia pestis, the cause of plague. The review addresses the functions and the biological significance of genes for the biosynthesis of LPS, as well as the biological properties of LPS in strains from various intraspecies groups ofY. pestis and their mutants, including the contribution of LPS to the resistance of bacteria to factors of the innate immunity of both insect-vectors and mammal-hosts. Special attention is paid to temperature-dependent variations in the LPS structure, their genetic control and roles in the pathogenesis of plague. The evolutionary aspect is considered based on a comparison of the structure and genetics of the LPS ofY. pestis and other enteric bacteria, including otherYersinia species. The prospects of development of live plague vaccines created on the basis ofY. pestis strains with the genetically modified LPS are discussed.
Lipopolysaccharide, lipid A, immune response, Yersinia pestis, Plague, antibiotic resistance
NCBI PubMed ID: 23150803Journal NLM ID: 101525823Publisher: Moscow: Park Media Ltd
Correspondence: knirel@ioc.ac.ru
Institutions: Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia
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11. Compound ID: 10963
|
/Variants 0/-a-D-Lyxp-(1-3)-b-D-Glcp6Me-(1-3)-b-D-Manp-(1-3)-b-D-Lyxp
/Variants 0/ is:
4%Pam-(1-3)-
OR (exclusively)
36%dPam-(1-3)-
OR (exclusively)
22%10b1C19-(1-3)-
OR (exclusively)
20%C18={?}-(1-3)-
OR (exclusively)
18%Ste-(1-3)- |
Show graphically |
Structure type: oligomer
Trivial name: oligosaccharide fragment from glycolipid
Contained glycoepitopes: IEDB_137485,IEDB_141181,IEDB_142488,IEDB_144983,IEDB_146664,IEDB_152206,IEDB_534865,IEDB_983930,IEDB_983931,SB_192,SB_44,SB_72
The structure is contained in the following publication(s):
- Article ID: 4445
Khoo KH, Suzuki R, Dell A, Morris HR, McNeil MR, Brennan PJ, Besra GS "Chemistry of the lyxose-containing mycobacteriophage receptors of Mycobacterium phlei/Mycobacterium smegmatis" -
Biochemistry 35(36) (1996) 11812-11819
Mycobacterium phlei (strain Timothy) (Mycobacterium smegmatis ATCC 19249) is characterized by the presence of a family of alkali-labile glycolipids, reminiscent of the trehalose-containing lipooligosaccharide class of antigens but lacking the nonreducing trehalose core. Through a combination of methylation analyses, 1H and 13C NMR, two-dimensional 1H/1H and 1H/13C NMR, fast atom bombardment-mass spectrometry, gas chromatography-mass spectrometry, and other analytical techniques, these new structures were shown to possess three distinct features. Firstly, they contained the pentose D-lyxose (Lyx), rarely found in biology, but an epimer of D-arabinose, a key component of the mycobacterial cell wall arabinogalactan and lipoarabinomannnan. Thus, it was apparent that these glycolipids are the same as those described by Bisso et al. and attributed with phage receptor properties [Bisso, G., Castelnuovo, G., Nardelli, M.-G., Orefici, G., Arancia, G., Laneelle, G., Asselineau, C., & Asselineau, J. (1976) Biochemie 58, 87-97]. Secondly, the complex oligosaccharides within the glycolipids contain the repeating units Lyxn(6-O-CH3-Glc)m and Lyxn(6-O-CH3-Glc)mMan1, where n+m equal to approximately 16 glycosyl residues. Thirdly, the M. phlei glycolipids were found to be heavily O-acylated, such that every D-Lyx residue invariably possesses an acyl function at position -2 and, in some instances, at both positions -2 and -4. The chemical characterization of these glycolipids, not feasible 20 years ago, clearly demonstrates that they are distinct from the type- and species-specific glycopeptidolipids, lipooligosaccharides, phenolic glycolipids, and the genus-specific phosphatidylinositol-based lipoglycans of mycobacteria. This present and previous studies begin to define the precise structural requirements responsible for the attachment of mycobacteriophage to the host cell wall.
cell wall, glycolipids, receptors, attachment, D-lyxose, Mycobacteriophages, Mycobacterium phlei Mycobacterium smegmatis
NCBI PubMed ID: 8794763Publication DOI: 10.1021/bi961055+Journal NLM ID: 0370623Publisher: American Chemical Society
Institutions: Department of Microbiology, Colorado State University, Fort Collins 80523, USA
Methods: 13C NMR, 1H NMR, methylation, NMR-2D, FAB-MS, GC-MS, de-O-acylation, sugar analysis, GC, HPLC
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12. Compound ID: 10964
|
/Variants 0/-a-D-Lyxp-(1-3)-b-D-Glcp6Me-(1-3)-b-D-Lyxp
/Variants 0/ is:
4%Pam-(1-3)-
OR (exclusively)
36%dPam-(1-3)-
OR (exclusively)
22%10b1C19-(1-3)-
OR (exclusively)
20%C18={?}-(1-3)-
OR (exclusively)
18%Ste-(1-3)- |
Show graphically |
Structure type: oligomer
Trivial name: oligosaccharide fragment from glycolipid
Contained glycoepitopes: IEDB_141181,IEDB_142488,IEDB_146664,IEDB_534865,IEDB_983931,SB_192
The structure is contained in the following publication(s):
- Article ID: 4445
Khoo KH, Suzuki R, Dell A, Morris HR, McNeil MR, Brennan PJ, Besra GS "Chemistry of the lyxose-containing mycobacteriophage receptors of Mycobacterium phlei/Mycobacterium smegmatis" -
Biochemistry 35(36) (1996) 11812-11819
Mycobacterium phlei (strain Timothy) (Mycobacterium smegmatis ATCC 19249) is characterized by the presence of a family of alkali-labile glycolipids, reminiscent of the trehalose-containing lipooligosaccharide class of antigens but lacking the nonreducing trehalose core. Through a combination of methylation analyses, 1H and 13C NMR, two-dimensional 1H/1H and 1H/13C NMR, fast atom bombardment-mass spectrometry, gas chromatography-mass spectrometry, and other analytical techniques, these new structures were shown to possess three distinct features. Firstly, they contained the pentose D-lyxose (Lyx), rarely found in biology, but an epimer of D-arabinose, a key component of the mycobacterial cell wall arabinogalactan and lipoarabinomannnan. Thus, it was apparent that these glycolipids are the same as those described by Bisso et al. and attributed with phage receptor properties [Bisso, G., Castelnuovo, G., Nardelli, M.-G., Orefici, G., Arancia, G., Laneelle, G., Asselineau, C., & Asselineau, J. (1976) Biochemie 58, 87-97]. Secondly, the complex oligosaccharides within the glycolipids contain the repeating units Lyxn(6-O-CH3-Glc)m and Lyxn(6-O-CH3-Glc)mMan1, where n+m equal to approximately 16 glycosyl residues. Thirdly, the M. phlei glycolipids were found to be heavily O-acylated, such that every D-Lyx residue invariably possesses an acyl function at position -2 and, in some instances, at both positions -2 and -4. The chemical characterization of these glycolipids, not feasible 20 years ago, clearly demonstrates that they are distinct from the type- and species-specific glycopeptidolipids, lipooligosaccharides, phenolic glycolipids, and the genus-specific phosphatidylinositol-based lipoglycans of mycobacteria. This present and previous studies begin to define the precise structural requirements responsible for the attachment of mycobacteriophage to the host cell wall.
cell wall, glycolipids, receptors, attachment, D-lyxose, Mycobacteriophages, Mycobacterium phlei Mycobacterium smegmatis
NCBI PubMed ID: 8794763Publication DOI: 10.1021/bi961055+Journal NLM ID: 0370623Publisher: American Chemical Society
Institutions: Department of Microbiology, Colorado State University, Fort Collins 80523, USA
Methods: 13C NMR, 1H NMR, methylation, NMR-2D, FAB-MS, GC-MS, de-O-acylation, sugar analysis, GC, HPLC
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13. Compound ID: 11341
|
3HOMyr-(1-2)-+
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Subst-(2-6)-+ |
| |
?%Lau-(1-3)-3HOMyr-(1-3)-+ | |
| | |
?%dPam-(1-3)-3HOMyr-(1-2)-b-D-GlcpN-(1-6)-a-D-GlcpN-(1-P
| |
?%b-L-Arap4N-(1--P--4)--+ 3HOMyr-(1-3)-+
Subst = core oligosaccharide |
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Structure type: oligomer
Compound class: lipid A
Contained glycoepitopes: IEDB_135394,IEDB_135515,IEDB_141807,IEDB_151531,IEDB_534864
The structure is contained in the following publication(s):
- Article ID: 4575
Matsuura M "Structural Modifications of Bacterial Lipopolysaccharide that Facilitate Gram-Negative Bacteria Evasion of Host Innate Immunity" -
Frontiers in Microbiology 4 (2013) 109
Bacterial lipopolysaccharide (LPS), a cell wall component characteristic of Gram-negative bacteria, is a representative pathogen-associated molecular pattern that allows mammalian cells to recognize bacterial invasion and trigger innate immune responses. The polysaccharide moiety of LPS primary plays protective roles for bacteria such as prevention from complement attacks or camouflage with common host carbohydrate residues. The lipid moiety, termed lipid A, is recognized by the Toll-like receptor 4 (TLR4)/MD-2 complex, which transduces signals for activation of host innate immunity. The basic structure of lipid A is a glucosamine disaccharide substituted by phosphate groups and acyl groups. Lipid A with six acyl groups (hexa-acylated form) has been indicated to be a strong stimulator of the TLR4/MD-2 complex. This type of lipid A is conserved among a wide variety of Gram-negative bacteria, and those bacteria are easily recognized by host cells for activation of defensive innate immune responses. Modifications of the lipid A structure to less-acylated forms have been observed in some bacterial species, and those forms are poor stimulators of the TLR4/MD-2 complex. Such modifications are thought to facilitate bacterial evasion of host innate immunity, thereby enhancing pathogenicity. This hypothesis is supported by studies of Yersinia pestis LPS, which contains hexa-acylated lipid A when the bacterium grows at 27 degrees C (the temperature of the vector flea), and shifts to contain less-acylated forms when grown at the human body temperature of 37 degrees C. This alteration of lipid A forms following transmission of Y. pestis from fleas to humans contributes predominantly to the virulence of this bacterium over other virulence factors. A similar role for less-acylated lipid A forms has been indicated in some other bacterial species, such as Francisella tularensis, Helicobacter pylori, and Porphyromonas gingivalis, and further studies to explore this concept are expected.
innate immunity, modification of lipopolysaccharide, less-acylated lipid A, immune evasion
NCBI PubMed ID: 23745121Publication DOI: 10.3389/fimmu.2013.00109Journal NLM ID: 101548977Publisher: Lausanne: Frontiers Research Foundation
Correspondence: mmatsuur@mb.med.kyoto-u.ac.jp
Institutions: Department of Microbiology, Graduate School of Medicine, Kyoto University Kyoto, Japan
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14. Compound ID: 11643
|
Lau-(1-3)-3HOMyr-(1-3)-+ 3HOMyr-(1-2)-+
| |
dPam-(1-3)-3HOMyr-(1-2)-b-D-GlcpN-(1-6)-a-D-GlcpN-(1--P--1)--b-L-Arap4N
| |
b-L-Arap4N-(1--P--4)--+ 3HOMyr-(1-3)-+ |
Show graphically |
Structure type: oligomer
Compound class: lipid A
Contained glycoepitopes: IEDB_135394,IEDB_135515,IEDB_141807,IEDB_151531,IEDB_534864
The structure is contained in the following publication(s):
- Article ID: 4694
Korneev KV, Kondakova AN, Arbatsky NP, Novototskaya-Vlasova KA, Rivkina EM, Anisimov AP, Kruglov AA, Kuprash DV, Nedospasov SA, Knirel YA, Drutskaya MS "Distinct biological activity of lipopolysaccharides with different lipid A acylation status from mutant strains of Yersinia pestis and some members of genus Psychrobacter" -
Biochemistry (Moscow) 79(12) (2014) 1333-1338
Correlation between the chemical structure of lipid A from various Gramnegative bacteria and biological activity of their lipopolysaccharide (LPS) as an agonist of the innate immune receptor Tolllike receptor 4 was investigated. Purified LPS species were quantitatively evaluated by their ability to activate the production of tumor necrosis factor (TNF) by murine bone marrowderived macrophages in vitro. Wildtype LPS from plaguecausing bacteria Yersinia pestis was compared to LPS from mutant strains with defects in acyltransferase genes (lpxM, lpxP) responsible for the attachment of secondary fatty acid residues (12:0 and 16:1) to lipid A. Lipid A of Y. pestis double ΔlpxM/ΔlpxP mutant was found to have the chemical structure that was predicted based on the known functions of the respective acyltransferases. The structures of lipid A from two members of the ancient psychrotrophic bacteria of the genus Psychrobacter were established for the first time, and biological activity of LPS from these bacteria containing lipid A fatty acids with shorter acyl chains (C10C12) than those in lipid A from LPS of Y. pestis or E. coli (C12C16) was determined. The data revealed a correlation between the ability of LPS to activate TNF production by bone marrowderived macrophages with the number and the length of acyl chains within lipid A.
Lipopolysaccharide, lipopolysaccharides, chemistry, strain, molecular, lipid, lipid A, mutant, biological, activity, biological activity, biology, genus, Yersinia, organic, acylation, Yersinia pestis, tumor necrosis factor, molecular biology, Toll-like receptor 4, Russia, Psychrobacter, Science, Psychrobacter spp.
Publication DOI: 10.1134/S0006297914120062Journal NLM ID: 0376536Publisher: Nauka/Interperiodica
Correspondence: yknirel@gmail.com; marinadru@gmail.com
Institutions: Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, ul. Vavilova 32, Moscow, Russia, fax: (499) 1351405, Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, fax: (499) 1355328
Methods: mild acid hydrolysis, biological assays, MS, statistical analysis
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15. Compound ID: 12821
|
dPam-(1-3)-Gro-(1--P--3)--R-3HOLau-(1-3)-+
|
R-3HOLau-(1-3)-+ |
| |
Myr-(1-3)-R-3HOC14={c4}-(1-2)-b-D-GlcpN-(1-6)-a-D-GlcpN
| |
P-4)-+ |
|
R-3HOMyr-(1-2)-+ |
Show graphically |
Structure type: oligomer
Compound class: lipid A
Contained glycoepitopes: IEDB_130695,IEDB_141807,IEDB_151531,IEDB_167835,IEDB_176772
The structure is contained in the following publication(s):
- Article ID: 5099
Scott AJ, Oyler BL, Goodlett DR, Ernst RK "Lipid A structural modifications in extreme conditions and identification of unique modifying enzymes to define the Toll-like receptor 4 structure-activity relationship" -
Biochimica et Biophysica Acta: Molecular and Cell Biology of Lipids 1862(11) (2017) 1439-1450
Strategies utilizing Toll-like receptor 4 (TLR4) agonists for treatment of cancer, infectious diseases, and other targets report promising results. Potent TLR4 antagonists are also gaining attention as therapeutic leads. Though some principles for TLR4 modulation by lipid A have been described, a thorough understanding of the structure-activity relationship (SAR) is lacking. Only through a complete definition of lipid A-TLR4 SAR is it possible to predict TLR4 signaling effects of discrete lipid A structures, rendering them more pharmacologically relevant. A limited 'toolbox' of lipid A-modifying enzymes has been defined and is largely composed of enzymes from mesophile human and zoonotic pathogens. Expansion of this 'toolbox' will result from extending the search into lipid A biosynthesis and modification by bacteria living at the extremes. Here, we review the fundamentals of lipid A structure, advances in lipid A uses in TLR4 modulation, and the search for novel lipid A-modifying systems in extremophile bacteria. This article is part of a Special Issue entitled: Bacterial Lipids edited by Russell E. Bishop.
lipid A structure, Marine bacteria, TLR4 agonists, TLR4 antagonists, TLR4 immunomodulation, Lipid A modifying enzymes
NCBI PubMed ID: 28108356Publication DOI: 10.1016/j.bbalip.2017.01.004Journal NLM ID: 0217513Publisher: Elsevier
Correspondence: rkernst@umaryland.edu
Institutions: Institute of Marine & Environmental Technology, University of Maryland Center for Environmental Science, Baltimore, MD 21202, United States, Department of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore, MD 21201, United States, Department of Microbial Pathogenesis, School of Dentistry, University of Maryland, Baltimore, MD 21201, United States
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