Found 4 structures.
Displayed structures from 1 to 4
Expand all compounds
Collapse all compounds
Show all as text (SweetDB notation)
Show all graphically (SNFG notation)
1. Compound ID: 13070
|
b-D-GalpNAc-(1-3)-b-D-Galp-(1-3)-D-GlcpNAc-(1-?)-b-D-Galp-(1-4)-D-GlcpNAc-(1--/core-Trio(GlcNAc-Fuc-Hep)/ |
Show graphically |
Structure type: fragment of a bigger structure
Aglycon: core-Trio(GlcNAc-Fuc-Hep)
Trivial name: type 2 LacNAc-type 1 A blood group
Compound class: LPS
Contained glycoepitopes: IEDB_130646,IEDB_130648,IEDB_135813,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137473,IEDB_1391962,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_143794,IEDB_150899,IEDB_151531,IEDB_157001,IEDB_157003,IEDB_1635950,IEDB_190606,IEDB_241103,IEDB_241107,IEDB_489984,IEDB_885811,IEDB_885816,SB_137,SB_156,SB_165,SB_166,SB_173,SB_187,SB_195,SB_21,SB_29,SB_30,SB_7,SB_88
The structure is contained in the following publication(s):
- Article ID: 5179
Li H, Tang H, Debowski AW, Stubbs KA, Marshall BJ, Benghezal M "Lipopolysaccharide Structural Differences between Western and Asian Helicobacter pylori Strains" -
Toxins 10(9) (2018) 364
Recent structural analysis of the lipopolysaccharide (LPS) isolated from Helicobacter pylori G27 wild-type and O-antigen ligase mutant resulted in the redefinition of the core-oligosaccharide and O-antigen domains. The short core-oligosaccharide (Glc-Gal-Hep-III-Hep-II-Hep-I-KDO) and its attached trisaccharide (Trio, GlcNAc-Fuc-Hep) appear to be highly conserved structures among H. pylori strains. The G27 LPS contains a linear glucan?heptan linker between the core-Trio and distal Lewis antigens. This linker domain was commonly identified in Western strains. In contrast, out of 12 partial LPS structures of Asian strains, none displayed the heptan moiety, despite the presence of Lewis antigens. This raises the question of how Lewis antigens are attached to the Trio, and whether the LPS structure of Asian strains contain another linker. Of note, a riban was identified as a linker in LPS of the mouse-adapted SS1 strain, suggesting that alternative linker structures can occur. In summary, additional full structural analyses of LPS in Asian strains are required to assess the presence or absence of an alternative linker in these strains. It will also be interesting to study the glucan-heptan linker moieties in pathogenesis as H. pylori infections in Asia are usually more symptomatic than the ones presented in the Western world.
Lipopolysaccharide, structure, Helicobacter pylori
NCBI PubMed ID: 30205541Publication DOI: 10.3390/toxins10090364Journal NLM ID: 101530765Publisher: Basel: MDPI
Correspondence: H.T.
; M.B.
Institutions: West China Marshall Research Center for Infectious Diseases, Center of Infectious Diseases, West China Hospital of Sichuan University, Chengdu 610041, China, Helicobacter pylori Research Laboratory, School of Biomedical Sciences, Marshall Centre for Infectious Disease Research and Training, University of Western Australia, Nedlands, WA 6009, Australia, School of Molecular Sciences, University of Western Australia, Crawley, WA 6009, Australia
Expand this compound
Collapse this compound
2. Compound ID: 15358
|
a-D-Galp-(1-3)-a-D-Manp-(1-2)-+
|
b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+ |
| |
b-D-Galp-(1-?)-b-D-GlcpNAc-(1-?)-b-D-Galp-(1-3)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-3)-a-D-Galp-(1-3)-a-D-Manp-(1-6)-a-D-Manp-(1-4)-a-D-GlcpN |
Show graphically |
Structure type: structural motif or average structure
Trivial name: procyclin glycoprotein
Compound class: GPI-anchor
Contained glycoepitopes: IEDB_130646,IEDB_130697,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_136104,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391962,IEDB_140108,IEDB_140116,IEDB_140122,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_141829,IEDB_142078,IEDB_143632,IEDB_143794,IEDB_144983,IEDB_150899,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_153529,IEDB_157001,IEDB_157003,IEDB_158533,IEDB_190606,IEDB_983930,SB_136,SB_137,SB_156,SB_165,SB_166,SB_173,SB_187,SB_191,SB_195,SB_196,SB_198,SB_29,SB_30,SB_44,SB_67,SB_7,SB_72,SB_88
The structure is contained in the following publication(s):
- Article ID: 5949
Jenni A, Knüsel S, Nagar R, Benninger M, Häner R, Ferguson MAJ, Roditi AK, Butikofer P "Elimination of GPI2 suppresses glycosylphosphatidylinositol GlcNAc transferase activity and alters GPI glycan modification in Trypanosoma brucei" -
Journal of Biological Chemistry 297(2) (2021) 100977
Many eukaryotic cell-surface proteins are post-translationally modified by a glycosylphosphatidylinositol (GPI) moiety that anchors them to the cell membrane. The biosynthesis of GPI anchors is initiated in the endoplasmic reticulum by transfer of GlcNAc from UDP-GlcNAc to phosphatidylinositol. This reaction is catalyzed by GPI GlcNAc transferase, a multisubunit complex comprising the catalytic subunit Gpi3/PIG-A as well as at least five other subunits, including the hydrophobic protein Gpi2, which is essential for the activity of the complex in yeast and mammals, but the function of which is not known. To investigate the role of Gpi2, we exploited Trypanosoma brucei (Tb), an early diverging eukaryote and important model organism that initially provided the first insights into GPI structure and biosynthesis. We generated insect-stage (procyclic) trypanosomes that lack TbGPI2 and found that in TbGPI2-null parasites, (i) GPI GlcNAc transferase activity is reduced, but not lost, in contrast with yeast and human cells, (ii) the GPI GlcNAc transferase complex persists, but its architecture is affected, with loss of at least the TbGPI1 subunit, and (iii) the GPI anchors of procyclins, the major surface proteins, are underglycosylated when compared with their WT counterparts, indicating the importance of TbGPI2 for reactions that occur in the Golgi apparatus. Immunofluorescence microscopy localized TbGPI2 not only to the endoplasmic reticulum but also to the Golgi apparatus, suggesting that in addition to its expected function as a subunit of the GPI GlcNAc transferase complex, TbGPI2 may have an enigmatic noncanonical role in Golgi-localized GPI anchor modification in trypanosomes.
glycosyltransferase, Trypanosoma brucei, GPI anchor, procyclin
NCBI PubMed ID: 34284059Publication DOI: 10.1016/j.jbc.2021.100977Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: peter.buetikofer@ibmm.unibe.ch
Institutions: Wellcome Centre for Anti-Infectives Research, School of Life Sciences, University of Dundee, Dundee, United Kingdom, Institute of Biochemistry and Molecular Medicine, University of Bern, Bern, Switzerland, Graduate School for Chemical and Biomedical Sciences, University of Bern, Bern, Switzerland, Institute of Cell Biology, University of Bern, Bern, Switzerland, Department for Chemistry and Biochemistry, University of Bern, Bern, Switzerland, Department of Biochemistry, Weill Cornell Medical College, New York, New York, USA
Methods: PCR, GC-MS, SDS-PAGE, TLC, ESI-MS, MS/MS, radiolabeling, genetic methods, Southern blotting, permethylation, immunofluorescence microscopy, flow cytometry analysis, Northern blotting
Expand this compound
Collapse this compound
3. Compound ID: 15359
|
a-D-Galp-(1-3)-a-D-Manp-(1-2)-+
|
a-Neup5Ac-(2-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-+ |
| |
b-D-Galp-(1-?)-b-D-GlcpNAc-(1-?)-b-D-Galp-(1-3)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-3)-a-D-Galp-(1-3)-a-D-Manp-(1-6)-a-D-Manp-(1-4)-a-D-GlcpN |
Show graphically |
Structure type: structural motif or average structure
Trivial name: procyclin glycoprotein
Compound class: GPI-anchor
Contained glycoepitopes: IEDB_130646,IEDB_130697,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_136104,IEDB_136794,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391962,IEDB_140108,IEDB_140116,IEDB_140122,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_141829,IEDB_142078,IEDB_143632,IEDB_143794,IEDB_144983,IEDB_146100,IEDB_149174,IEDB_150899,IEDB_150933,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_153529,IEDB_157001,IEDB_157003,IEDB_158533,IEDB_190606,IEDB_423120,IEDB_983930,SB_115,SB_116,SB_131,SB_136,SB_137,SB_156,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_187,SB_191,SB_195,SB_196,SB_198,SB_29,SB_30,SB_39,SB_44,SB_67,SB_68,SB_7,SB_72,SB_84,SB_88
The structure is contained in the following publication(s):
- Article ID: 5949
Jenni A, Knüsel S, Nagar R, Benninger M, Häner R, Ferguson MAJ, Roditi AK, Butikofer P "Elimination of GPI2 suppresses glycosylphosphatidylinositol GlcNAc transferase activity and alters GPI glycan modification in Trypanosoma brucei" -
Journal of Biological Chemistry 297(2) (2021) 100977
Many eukaryotic cell-surface proteins are post-translationally modified by a glycosylphosphatidylinositol (GPI) moiety that anchors them to the cell membrane. The biosynthesis of GPI anchors is initiated in the endoplasmic reticulum by transfer of GlcNAc from UDP-GlcNAc to phosphatidylinositol. This reaction is catalyzed by GPI GlcNAc transferase, a multisubunit complex comprising the catalytic subunit Gpi3/PIG-A as well as at least five other subunits, including the hydrophobic protein Gpi2, which is essential for the activity of the complex in yeast and mammals, but the function of which is not known. To investigate the role of Gpi2, we exploited Trypanosoma brucei (Tb), an early diverging eukaryote and important model organism that initially provided the first insights into GPI structure and biosynthesis. We generated insect-stage (procyclic) trypanosomes that lack TbGPI2 and found that in TbGPI2-null parasites, (i) GPI GlcNAc transferase activity is reduced, but not lost, in contrast with yeast and human cells, (ii) the GPI GlcNAc transferase complex persists, but its architecture is affected, with loss of at least the TbGPI1 subunit, and (iii) the GPI anchors of procyclins, the major surface proteins, are underglycosylated when compared with their WT counterparts, indicating the importance of TbGPI2 for reactions that occur in the Golgi apparatus. Immunofluorescence microscopy localized TbGPI2 not only to the endoplasmic reticulum but also to the Golgi apparatus, suggesting that in addition to its expected function as a subunit of the GPI GlcNAc transferase complex, TbGPI2 may have an enigmatic noncanonical role in Golgi-localized GPI anchor modification in trypanosomes.
glycosyltransferase, Trypanosoma brucei, GPI anchor, procyclin
NCBI PubMed ID: 34284059Publication DOI: 10.1016/j.jbc.2021.100977Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: peter.buetikofer@ibmm.unibe.ch
Institutions: Wellcome Centre for Anti-Infectives Research, School of Life Sciences, University of Dundee, Dundee, United Kingdom, Institute of Biochemistry and Molecular Medicine, University of Bern, Bern, Switzerland, Graduate School for Chemical and Biomedical Sciences, University of Bern, Bern, Switzerland, Institute of Cell Biology, University of Bern, Bern, Switzerland, Department for Chemistry and Biochemistry, University of Bern, Bern, Switzerland, Department of Biochemistry, Weill Cornell Medical College, New York, New York, USA
Methods: PCR, GC-MS, SDS-PAGE, TLC, ESI-MS, MS/MS, radiolabeling, genetic methods, Southern blotting, permethylation, immunofluorescence microscopy, flow cytometry analysis, Northern blotting
Expand this compound
Collapse this compound
4. Compound ID: 15360
|
a-D-Galp-(1-3)-a-D-Manp-(1-2)-+
|
b-D-Galp-(1-?)-b-D-GlcpNAc-(1-?)-b-D-Galp-(1-3)-b-D-GlcpNAc-(1-3)-+ |
| |
a-Neup5Ac-(2-3)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-4)-b-D-GlcpNAc-(1-6)-b-D-Galp-(1-3)-a-D-Galp-(1-3)-a-D-Manp-(1-6)-a-D-Manp-(1-4)-a-D-GlcpN |
Show graphically |
Structure type: structural motif or average structure
Trivial name: procyclin glycoprotein
Compound class: GPI-anchor
Contained glycoepitopes: IEDB_130646,IEDB_130697,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_136104,IEDB_136794,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391962,IEDB_140108,IEDB_140116,IEDB_140122,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_141829,IEDB_142078,IEDB_143632,IEDB_143794,IEDB_144983,IEDB_146100,IEDB_149174,IEDB_150899,IEDB_150933,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_153529,IEDB_157001,IEDB_157003,IEDB_158533,IEDB_190606,IEDB_423120,IEDB_983930,SB_115,SB_116,SB_131,SB_136,SB_137,SB_156,SB_165,SB_166,SB_170,SB_171,SB_172,SB_173,SB_187,SB_191,SB_195,SB_196,SB_198,SB_29,SB_30,SB_39,SB_44,SB_67,SB_68,SB_7,SB_72,SB_84,SB_88
The structure is contained in the following publication(s):
- Article ID: 5949
Jenni A, Knüsel S, Nagar R, Benninger M, Häner R, Ferguson MAJ, Roditi AK, Butikofer P "Elimination of GPI2 suppresses glycosylphosphatidylinositol GlcNAc transferase activity and alters GPI glycan modification in Trypanosoma brucei" -
Journal of Biological Chemistry 297(2) (2021) 100977
Many eukaryotic cell-surface proteins are post-translationally modified by a glycosylphosphatidylinositol (GPI) moiety that anchors them to the cell membrane. The biosynthesis of GPI anchors is initiated in the endoplasmic reticulum by transfer of GlcNAc from UDP-GlcNAc to phosphatidylinositol. This reaction is catalyzed by GPI GlcNAc transferase, a multisubunit complex comprising the catalytic subunit Gpi3/PIG-A as well as at least five other subunits, including the hydrophobic protein Gpi2, which is essential for the activity of the complex in yeast and mammals, but the function of which is not known. To investigate the role of Gpi2, we exploited Trypanosoma brucei (Tb), an early diverging eukaryote and important model organism that initially provided the first insights into GPI structure and biosynthesis. We generated insect-stage (procyclic) trypanosomes that lack TbGPI2 and found that in TbGPI2-null parasites, (i) GPI GlcNAc transferase activity is reduced, but not lost, in contrast with yeast and human cells, (ii) the GPI GlcNAc transferase complex persists, but its architecture is affected, with loss of at least the TbGPI1 subunit, and (iii) the GPI anchors of procyclins, the major surface proteins, are underglycosylated when compared with their WT counterparts, indicating the importance of TbGPI2 for reactions that occur in the Golgi apparatus. Immunofluorescence microscopy localized TbGPI2 not only to the endoplasmic reticulum but also to the Golgi apparatus, suggesting that in addition to its expected function as a subunit of the GPI GlcNAc transferase complex, TbGPI2 may have an enigmatic noncanonical role in Golgi-localized GPI anchor modification in trypanosomes.
glycosyltransferase, Trypanosoma brucei, GPI anchor, procyclin
NCBI PubMed ID: 34284059Publication DOI: 10.1016/j.jbc.2021.100977Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: peter.buetikofer@ibmm.unibe.ch
Institutions: Wellcome Centre for Anti-Infectives Research, School of Life Sciences, University of Dundee, Dundee, United Kingdom, Institute of Biochemistry and Molecular Medicine, University of Bern, Bern, Switzerland, Graduate School for Chemical and Biomedical Sciences, University of Bern, Bern, Switzerland, Institute of Cell Biology, University of Bern, Bern, Switzerland, Department for Chemistry and Biochemistry, University of Bern, Bern, Switzerland, Department of Biochemistry, Weill Cornell Medical College, New York, New York, USA
Methods: PCR, GC-MS, SDS-PAGE, TLC, ESI-MS, MS/MS, radiolabeling, genetic methods, Southern blotting, permethylation, immunofluorescence microscopy, flow cytometry analysis, Northern blotting
Expand this compound
Collapse this compound
Total list of structure IDs on all result pages of the current query:
Total list of corresponding CSDB IDs (record IDs):
Execution: 2 sec