Found 5 structures.
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1. Compound ID: 1357
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Subst-(1-4)-+
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b-D-Glcp-(1-3)-a-D-FucpNAc4N-(1-4)-a-D-GalpNAc-(1-3)-D-GalNAc
Subst = 9-fluorenylmethoxycarbonyl (Fmoc) = SMILES O={1}C(O)OCC1C2=C(C3=C1C=CC=C3)C=CC=C2 |
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Structure type: oligomer
Contained glycoepitopes: IEDB_130648,IEDB_137473,IEDB_1391961,IEDB_141582,IEDB_141584,IEDB_142488,IEDB_146664,IEDB_153207,IEDB_1635955,IEDB_885821,IEDB_885822,IEDB_983931,SB_192
The structure is contained in the following publication(s):
- Article ID: 429
Yother J, Leopold K, White J, Fischer W "Generation and properties of a Streptococcus pneumoniae mutant which does not require choline or analogs for growth" -
Journal of Bacteriology 180(8) (1998) 2093-2101
A mutant (JY2190) of Streptococcus pneumoniae Rx1 which had acquired the ability to grow in the absence of choline and analogs was isolated. Lipoteichoic acid (LTA) and wall teichoic acid (TA) isolated from the mutant were free of phosphocholine and other phosphorylated amino alcohols. Both polymers showed an unaltered chain structure and, in the case of LTA, an unchanged glycolipid anchor. The cell wall composition was also not altered except that, due to the lack of phosphocholine, the phosphate content of cell walls was half that of the parent strain. Isolated cell walls of the mutant were resistant to hydrolysis by pneumococcal autolysin (N-acetylmuramyl-L-alanine amidase) but were cleaved by the muramidases CPL and cellosyl. The lack of active autolysin in the mutant cells became apparent by impaired cell separation at the end of cell division and by resistance against stationary-phase and penicillin-induced lysis. As a result of the absence of choline in the LTA, pneumococcal surface protein A (PspA) was no longer retained on the cytoplasmic membrane. During growth in the presence of choline, which was incorporated as phosphocholine into LTA and TA, the mutant cells separated normally, did not release PspA, and became penicillin sensitive. However, even under these conditions, they did not lyse in the stationary phase, and they showed poor reactivity with antibody to phosphocholine and an increased release of C-polysaccharide from the cell. In contrast to ethanolamine-grown parent cells (A. Tomasz, Proc. Natl. Acad. Sci. USA 59:86-93, 1968), the choline-free mutant cells retained the capability to undergo genetic transformation but, compared to Rx1, with lower frequency and at an earlier stage of growth. The properties of the mutant could be transferred to the parent strain by DNA of the mutant
Streptococcus pneumoniae, teichoic acid, C polysaccharide, choline, lipoteichoic acid
NCBI PubMed ID: 9555891Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Correspondence: jyother@uab.edu
Institutions: Department of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294, Institut Biochemie, Universitat Erlangen-Nurnberg, D-91054 Erlangen, Germany
Methods: GLC, HPLC, immunoblotting, microscopy, periodate oxidation
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2. Compound ID: 3299
Structure type: oligomer
Contained glycoepitopes: IEDB_130648,IEDB_137473,IEDB_1391961,IEDB_141582,IEDB_141584,IEDB_142488,IEDB_146664,IEDB_153207,IEDB_1635955,IEDB_885821,IEDB_885822,IEDB_983931,SB_192
The structure is contained in the following publication(s):
- Article ID: 1217
Shashkov AS, Tul'skaya EM, Grachev AA, Evtushenko LI, Bueva OV, Naumova IB "Structure of cell-wall teichoic acid of Streptomyces sparsogenes VKM Ac-1744T" -
Biochemistry (Moscow) 63 (1998)
structure, cell, polymer, acidic, acid, bacteria, cell wall, 13C NMR, function, teichoic acid, Streptomyces, Gram-positive, anionic, taxonomy
Journal NLM ID: 0376536Publisher: Nauka/Interperiodica
Institutions: Institute of biochemistry and Physiology of Microorganisms,Russian Academy of Sciences,Pushchino,Russia
Methods: NMR
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3. Compound ID: 4556
Structure type: oligomer
Contained glycoepitopes: IEDB_130648,IEDB_137473,IEDB_1391961,IEDB_141582,IEDB_141584,IEDB_153207,IEDB_1635955,IEDB_885821,IEDB_885822
The structure is contained in the following publication(s):
- Article ID: 1750
Jennings HJ, Lugowski C, Young NM "Structure of the complex polysaccharide C-substance from Streptococcus pneumoniae type 1" -
Biochemistry 19 (1980) 4712-4719
The complex cell-wall polysaccharide, C-substance, was isolated from Streptococcus pneumoniae type 1 and purified by DEAE-cellulose (HCO3(-) form) and Sephadex column chromatography. The complete structure of this antigen was obtained by the application of methylation and 1H NMR and 13C NMR spectroscopic techniques to a series of oligosaccharide fragments obtained by the selective degradation of the N-acetylated antigen. Native C-substance is composed of the following repeating unit: β-D-Glup-1→3-α-AAT-Galp-1→4-α-D-GalNAcp-1→3-β-D-GalNH2p-1→1'-ribitol-5-phosphate where AATGal is 2-acetamido-4-amino-2,4,6-trideoxygalactose. Phosphocholine substituents are situated at O(6) of the unacetylated galactosamine residues, and the repeating units are linked through a diphosphate ester from ribitol to O(6) of the β-D-glucopyranose residue. This structure has also been shown to be common to C-substances prepared from a number of other pneumococcal types based on the criterion of their identical 13C NMR spectra.
NCBI PubMed ID: 7426624Publication DOI: 10.1021/bi00561a026 ·Journal NLM ID: 0370623Publisher: American Chemical Society
Institutions: Division of Biological Sciences, National Research Council of Canada, Ottawa, Ontario, Canada K1A OR6
Methods: 13C NMR
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4. Compound ID: 4557
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b-D-Glcp-(1-3)-a-D-FucpNAc4NAc-(1-4)-a-D-GalpNAc-(1-3)-D-GalNAc |
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Structure type: oligomer
Contained glycoepitopes: IEDB_130648,IEDB_137473,IEDB_1391961,IEDB_141582,IEDB_141584,IEDB_142488,IEDB_146664,IEDB_153207,IEDB_1635955,IEDB_885821,IEDB_885822,IEDB_983931,SB_192
The structure is contained in the following publication(s):
- Article ID: 1750
Jennings HJ, Lugowski C, Young NM "Structure of the complex polysaccharide C-substance from Streptococcus pneumoniae type 1" -
Biochemistry 19 (1980) 4712-4719
The complex cell-wall polysaccharide, C-substance, was isolated from Streptococcus pneumoniae type 1 and purified by DEAE-cellulose (HCO3(-) form) and Sephadex column chromatography. The complete structure of this antigen was obtained by the application of methylation and 1H NMR and 13C NMR spectroscopic techniques to a series of oligosaccharide fragments obtained by the selective degradation of the N-acetylated antigen. Native C-substance is composed of the following repeating unit: β-D-Glup-1→3-α-AAT-Galp-1→4-α-D-GalNAcp-1→3-β-D-GalNH2p-1→1'-ribitol-5-phosphate where AATGal is 2-acetamido-4-amino-2,4,6-trideoxygalactose. Phosphocholine substituents are situated at O(6) of the unacetylated galactosamine residues, and the repeating units are linked through a diphosphate ester from ribitol to O(6) of the β-D-glucopyranose residue. This structure has also been shown to be common to C-substances prepared from a number of other pneumococcal types based on the criterion of their identical 13C NMR spectra.
NCBI PubMed ID: 7426624Publication DOI: 10.1021/bi00561a026 ·Journal NLM ID: 0370623Publisher: American Chemical Society
Institutions: Division of Biological Sciences, National Research Council of Canada, Ottawa, Ontario, Canada K1A OR6
Methods: 13C NMR
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5. Compound ID: 10197
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Galf-(1-3)-+
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GalA3Me-(1-6)-+ |
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-3)-GalNAc-(1-4)-GlcNAc-(1-4)-GalA-(1-3)-GalNAc-(1- |
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Structure type: polymer biological repeating unit
; n=10
Compound class: N-glycan
Contained glycoepitopes: IEDB_130648,IEDB_135813,IEDB_136095,IEDB_137340,IEDB_137472,IEDB_137473,IEDB_1391961,IEDB_141582,IEDB_141584,IEDB_141807,IEDB_149155,IEDB_151531,IEDB_152216,IEDB_153207,IEDB_1635955,IEDB_190606,IEDB_2218588,IEDB_885821,IEDB_885822
The structure is contained in the following publication(s):
- Article ID: 2450
Lis H, Sharon N "Protein glycosylation. Structural and functional aspects" -
European Journal of Biochemistry 218 (1993) 1-27
During the last decade, there have been enormous advances in our knowledge of glycoproteins and the stage has been set for the biotechnological production of many of them for therapeutic use. These advances are reviewed, with special emphasis on the structure and function of the glycoproteins (excluding the proteoglycans). Current methods for structural analysis of glycoproteins are surveyed, as are novel carbohydrate-peptide linking groups, and mono- and oligo-saccharide constituents found in these macromolecules. The possible roles of the carbohydrate units in modulating the physicochemical and biological properties of the parent proteins are discussed, and evidence is presented on their roles as recognition determinants between molecules and cells, or cell and cells. Finally, examples are given of changes that occur in the carbohydrates of soluble and cell-surface glycoproteins during differentiation, growth and malignancy, which further highlight the important role of these substances in health and disease.
NCBI PubMed ID: 8243456Journal NLM ID: 0107600Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
Institutions: Department of Membrane Research and Biophysics, Weizmann Institute of Science, Rehovot, Israel
- Article ID: 4237
Paul G, Wieland F "Sequence of the halobacterial glycosaminoglycan" -
Journal of Biological Chemistry 262 (1987) 9587-9593
The cell-surface glycoprotein of halobacterium contains a sulfated repeating unit saccharide chain, similar to the mammalian glycosaminoglycans. The composition of a presumptive repeating pentasaccharide unit of this glycosaminoglycan is 1 GlcNAc, 1 GalNAc, 1 Gal, 1 GalA (where GalA represents galacturonic acid), 1 3-O-methyl-GalA, and 2 SO42-. Linkage to protein of this glycoconjugate involves the hitherto unique unit Asn-GalNAc, with the N-linked asparagine residue being the second NH2-terminal amino acid and part of the common N-linked glycosyl acceptor sequence Asn-X-Thr(Ser). Transfer of the completed, sulfated glycosaminoglycan from its lipid precursor to the protein occurs at the cell surface, and the presence of this sulfated saccharide chain in the cell-surface glycoprotein seems to be required to maintain the structural integrity of the rod-shaped halobacteria. In this paper, we report the complete saccharide structure of this N-linked glycosaminoglycan. This structure is deduced from chemical analyses of fragments that were isolated after hydrazinolysis and subsequent nitrous acid deamination or after mild acidic hydrolysis of purified Pronase-derived glycosaminoglycan-peptides. The halobacterial glycosaminoglycan consists, on the average, of 10 repeating pentasaccharide units of the following structure. (formula: see text) The reducing end N-acetylgalactosamine residue is linked directly to the asparagine, without a special saccharide linker region.
NCBI PubMed ID: 3597425Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Methods: gel filtration, GLC-MS, partial acid hydrolysis, acid hydrolysis, GLC, deamination, methanolysis, desulfation, hydrazinolysis, reduction, permethylation analysis
- Article ID: 4241
Wieland F "Structure and biosynthesis of prokaryotic glycoproteins" -
Biochimie 70 (1988) 1493-1504
Glycoproteins as components of cell surfaces are not restricted to eukaryotes. The prokaryotic glycoprotein studied in greatest detail so far is the cell surface glycoprotein of the archaebacterium Halobacterium halobium. This bacterial glycoprotein contains 3 different types of glycoconjugates, and each type of glycoconjugate involves a different carbohydrate-protein linkage unit: 1) One glycosaminoglycan chain, constructed from a repeating sulfated pentasaccharide block, is linked to one protein molecule via the novel N-glycosyl linkage unit asparaginyl-N-acetylgalactosamine. 2) Ten sulfated oligosaccharides that contain glucose, glucuronic acid and iduronic acid are bound to the protein via the hitherto unknown N-glycosyl linkage unit asparaginylglucose. 3) About 15 disaccharides, glucosylgalactose, are O-glycosyl-linked to a cluster of threonine residues close to the C-terminus of the core protein. The overall structure of the cell surface glycoprotein of halobacteria is thus reminiscent of animal proteoglycans and a functional role of the glycosaminoglycan chain in maintaining the rod shape of halobacteria is discussed. Biosynthesis of the two N-glycosyl linkage units involves dolichol monophosphate and dolicholdiphosphate-linked saccharide precursors. Sulfation and epimerization of the glycoconjugates occur at the lipid-linked level and the mature saccharides are transferred to the protein core on the cell surface. The sulfated oligosaccharides that finally become bound to asparagine via glucose are transiently methylated at their lipid-linked stage and this transient chemical modification seems to be required for the biosynthesis of the corresponding N-glycosyl bond.
NCBI PubMed ID: 3149518Publication DOI: 10.1016/0300-9084(88)90286-6Journal NLM ID: 1264604Publisher: Paris: Editions Scientifiques Elsevier
Institutions: Institut für Biochemie I, Heidelberg, F.R.G
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