Found 3 structures.
Displayed structures from 1 to 3
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1. Compound ID: 3392
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b-D-Glcp-(1-2)-+
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a-D-Galp-(1-2)-+ |
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a-Neup5Ac-(2-3)-+ | | EtN-(1--P--6)--+ a-Kdop-(2-4)-+
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b-D-Galp-(1-3)-b-D-GalpNAc-(1-4)-b-D-Galp-(1-3)-b-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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b-D-Glcp-(1-4)-+ |
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Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130648,IEDB_130650,IEDB_130659,IEDB_131186,IEDB_1335895,IEDB_134627,IEDB_135818,IEDB_136044,IEDB_136794,IEDB_136906,IEDB_137472,IEDB_137473,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141794,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_147450,IEDB_147451,IEDB_149174,IEDB_150933,IEDB_151528,IEDB_167072,IEDB_190606,IEDB_2189047,IEDB_742245,IEDB_983931,SB_116,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_192,SB_195,SB_23,SB_24,SB_25,SB_39,SB_68,SB_7,SB_8,SB_84,SB_88,SB_96
The structure is contained in the following publication(s):
- Article ID: 1281
Szymanski CM, Michael FS, Jarell HC, Li J, Gilbert M, Larocque S, Vinogradov E, Brisson JR "Detection of conserved N-linked glycans and phase-variable lipooligosaccharides and capsules from campylobacter cells by mass spectrometry and high resolution magic angle spinning NMR spectroscopy" -
Journal of Biological Chemistry 278(27) (2003) 24509-24520
Glycomics, the study of microbial polysaccharides and genes responsible for their formation, requires the continuous development of rapid and sensitive methods for the identification of glycan structures. In this study, methods for the direct analysis of sugars from 108 to 1010 cells are outlined using the human gastrointestinal pathogen, Campylobacter jejuni. Using capillary-electrophoresis coupled with sensitive electrospray mass spectrometry, we demonstrate variability in the lipid A component of C. jejuni lipooligosaccharides (LOSs). In addition, these sensitive methods have permitted the detection of phase-variable LOS core structures that were not observed previously. High resolution magic angle spinning (HR-MAS) NMR was used to examine capsular polysaccharides directly from campylobacter cells and showed profiles similar to those observed for purified polysaccharides analyzed by solution NMR. This method also exhibited the feasibility of campylobacter serotyping, mutant verification, and preliminary sugar analysis. HR-MAS NMR examination of growth from individual colonies of C. jejuni NCTC11168 indicated that the capsular glycan modifications are also phase-variable. These variants show different staining patterns on deoxycholate-PAGE and reactivity with immune sera. One of the identified modifications was a novel -OP=O(NH2)OMe phosphoramide, not observed previously in nature. In addition, HR-MAS NMR detected the N-linked glycan, GalNAc-α1,4-GalNAc-α1,4-[Glc-β1,3-]GalNAc-α1,4-GalNAc-α 1,4-GalNAc-α1,3-Bac, where Bac is 2,4-diacetamido-2,4,6-trideoxy-d-glucopyranose, in C. jejuni and Campylobacter coli. The presence of this common heptasaccharide in multiple campylobacter isolates demonstrates the conservation of the N-linked protein glycosylation pathway in this organism
Lipooligosaccharide, capsular polysaccharide, Campylobacter, NMR spectroscopy, mass spectrometry, magic angle
NCBI PubMed ID: 12716884Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: jean-robert.brisson+AEA-nrc-cnrc.gc.ca
Institutions: Institute for Biological Sciences, National Research Council of Canada, Ottawa, Ontario KlA ORB, Canada
Methods: NMR-2D, NMR, ESI-MS, HR-MAS NMR
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2. Compound ID: 11252
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b-D-Glcp-(1-2)-+
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a-D-Galp-(1-2)-+ |
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a-Neup5Ac-(2-3)-+ | | /Variants 0/-+ Kdop-(2-?)-+
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b-D-Galp-(1-3)-b-D-GalpNAc-(1-4)-b-D-Galp-(1-3)-b-D-Galp-(1-3)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-Kdop-(2--/lipid A/
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b-D-Glcp-(1-4)-+
/Variants 0/ is:
P-6)-
OR (exclusively)
EtN-(1--P--6)-- |
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Structure type: oligomer
Aglycon: lipid A
Compound class: LOS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130648,IEDB_130650,IEDB_130658,IEDB_130659,IEDB_131186,IEDB_1335895,IEDB_134627,IEDB_135818,IEDB_136044,IEDB_136794,IEDB_136906,IEDB_137472,IEDB_137473,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141794,IEDB_142488,IEDB_146100,IEDB_146664,IEDB_147450,IEDB_147451,IEDB_149174,IEDB_150933,IEDB_151528,IEDB_167072,IEDB_190606,IEDB_2189047,IEDB_742245,IEDB_983931,SB_116,SB_165,SB_166,SB_170,SB_171,SB_172,SB_187,SB_192,SB_195,SB_23,SB_24,SB_25,SB_39,SB_68,SB_7,SB_8,SB_84,SB_88,SB_96
The structure is contained in the following publication(s):
- Article ID: 4537
Iwata T, Chiku K, Amano K, Kusumoto M, Ohnishi-Kameyama M, Ono H, Akiba M "Effects of lipooligosaccharide inner core truncation on bile resistance and chick colonization by Campylobacter jejuni" -
PLoS One 8(2) (2013) e56900
Campylobacter jejuni is the most common bacterium that causes diarrhea worldwide, and chickens are considered the main reservoir of this pathogen. This study investigated the effects of serial truncation of lipooligosaccharide (LOS), a major component of the outer membrane of C. jejuni, on its bile resistance and intestinal colonization ability in chickens. Genes encoding manno-heptose synthetases or glycosyltransferases were inactivated to generate isogenic mutants. Serial truncation of the LOS core oligosaccharide caused a stepwise increase in susceptibilities of two C. jejuni strains, NCTC 11168 and 81-176, to bile acids. Inactivation of hldE, hldD, or waaC caused severe truncation of the core oligosaccharide, which greatly increased the susceptibility to bile acids. Both wild-type strains grew normally in chicken intestinal extracts, whereas the mutants with severe oligosaccharide truncation were not detected 12 h after inoculation. These mutants attained viable bacterial counts in the bile acid-free extracts 24 h after inoculation. The wild-type strain 11-164 was present in the cecal contents at >10(7) CFU/g on 5 days after challenge infection and after this time period, whereas its hldD mutant was present at <10(3) CFU/g throughout the experimental period. Trans-complementation of the hldD mutant with the wild-type hldD allele completely restored the in vivo colonization level to that of the wild-type strain. Mutants with a shorter LOS had higher hydrophobicities. Thus, the length of the LOS core oligosaccharide affected the surface hydrophobicity and bile resistance of C. jejuni as well as its ability to colonize chicken intestines.
Lipooligosaccharide, Campylobacter jejuni, Genes, glycosyltransferases, inner core, outer membrane
NCBI PubMed ID: 23437265Publication DOI: 10.1371/journal.pone.0056900Journal NLM ID: 101285081Publisher: San Francisco, CA: Public Library of Science
Correspondence: akiba@affrc.go.jp
Institutions: Bacterial and Parasitic Disease Research Division, National Institute of Animal Health, Tsukuba, Japan, Analytical Science Division, National Food Research Institute, Tsukuba, Japan, Bioscience Research Education Center, Akita University, Akita, Akita, Japan, Graduate School of Life and Environmental Sciences, Osaka Prefecture University, Izumisano, Osaka, Japan
Methods: PCR, GC-MS, MALDI-TOF MS, genetic methods, SDS-Tricine-PAGE
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3. Compound ID: 11254
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b-D-Galp-(1-3)-+ /Variants 0/-+ Kdop-(2-?)-+
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b-D-Glcp-(1-2)-L-gro-a-D-manHepp-(1-3)-L-gro-a-D-manHepp-(1-5)-Kdop
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b-D-Glcp-(1-4)-+
/Variants 0/ is:
P-6)-
OR (exclusively)
EtN-(1--P--6)-- |
Show graphically |
Structure type: oligomer
Compound class: LOS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130650,IEDB_130658,IEDB_130659,IEDB_1335895,IEDB_136044,IEDB_137472,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141794,IEDB_142488,IEDB_146664,IEDB_190606,IEDB_2189047,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: 4537
Iwata T, Chiku K, Amano K, Kusumoto M, Ohnishi-Kameyama M, Ono H, Akiba M "Effects of lipooligosaccharide inner core truncation on bile resistance and chick colonization by Campylobacter jejuni" -
PLoS One 8(2) (2013) e56900
Campylobacter jejuni is the most common bacterium that causes diarrhea worldwide, and chickens are considered the main reservoir of this pathogen. This study investigated the effects of serial truncation of lipooligosaccharide (LOS), a major component of the outer membrane of C. jejuni, on its bile resistance and intestinal colonization ability in chickens. Genes encoding manno-heptose synthetases or glycosyltransferases were inactivated to generate isogenic mutants. Serial truncation of the LOS core oligosaccharide caused a stepwise increase in susceptibilities of two C. jejuni strains, NCTC 11168 and 81-176, to bile acids. Inactivation of hldE, hldD, or waaC caused severe truncation of the core oligosaccharide, which greatly increased the susceptibility to bile acids. Both wild-type strains grew normally in chicken intestinal extracts, whereas the mutants with severe oligosaccharide truncation were not detected 12 h after inoculation. These mutants attained viable bacterial counts in the bile acid-free extracts 24 h after inoculation. The wild-type strain 11-164 was present in the cecal contents at >10(7) CFU/g on 5 days after challenge infection and after this time period, whereas its hldD mutant was present at <10(3) CFU/g throughout the experimental period. Trans-complementation of the hldD mutant with the wild-type hldD allele completely restored the in vivo colonization level to that of the wild-type strain. Mutants with a shorter LOS had higher hydrophobicities. Thus, the length of the LOS core oligosaccharide affected the surface hydrophobicity and bile resistance of C. jejuni as well as its ability to colonize chicken intestines.
Lipooligosaccharide, Campylobacter jejuni, Genes, glycosyltransferases, inner core, outer membrane
NCBI PubMed ID: 23437265Publication DOI: 10.1371/journal.pone.0056900Journal NLM ID: 101285081Publisher: San Francisco, CA: Public Library of Science
Correspondence: akiba@affrc.go.jp
Institutions: Bacterial and Parasitic Disease Research Division, National Institute of Animal Health, Tsukuba, Japan, Analytical Science Division, National Food Research Institute, Tsukuba, Japan, Bioscience Research Education Center, Akita University, Akita, Akita, Japan, Graduate School of Life and Environmental Sciences, Osaka Prefecture University, Izumisano, Osaka, Japan
Methods: PCR, GC-MS, MALDI-TOF MS, genetic methods, SDS-Tricine-PAGE
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