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1. Compound ID: 1470
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GroA-(2--P--4)--b-D-ManpNAc-(1-4)-+
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a-D-Glcp-(1-6)-+ |
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{{{-b-D-Galp-(1-4)-b-D-ManpNAc-(1-3)-}}}/n=21/-a-L-Rhap-(1-3)-a-L-Rhap-(1-3)-a-L-Rhap-(1-3)-b-D-Galp-(1-7)-Tyr |
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Structure type: oligomer
Compound class: S-layer glycoprotein
Contained glycoepitopes: IEDB_136044,IEDB_136105,IEDB_137472,IEDB_141794,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_190606,IEDB_225177,IEDB_885813,IEDB_885823,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: 468
Schäffer C, Messner P "Surface-layer glycoproteins: an example for the diversity of bacterial glycosylation with promising impacts on nanobiotechnology" -
Glycobiology 14(8) (2004) 31R-42R
Bacterial cell surface layers, referred to simply as S-layers, have been described for all major phylogenetic groups of bacteria, which may indicate their pivotal role for a bacterium in its natural habitat. They have the unique ability to assemble into two-dimensional crystalline arrays that completely cover the bacterial cells. Glycosylation represents the most frequent modification of S-layer proteins. S-layer glycoproteins constitute a class of glycoconjugates first isolated in the mid-1970s, but S-layer glycoprotein research is still being regarded as an 'exotic field of glycobiology,' possibly because of its 'noneukaryotic' character. Extensive work over the past 30 years provided evidence of an enormous diversity of S-layer glycoproteins that have been created in nature over 3 billion years of prokaryotic evolution. These glycoconjugates are substantially different from eukaryotic glycoproteins, with regard to both composition and structure; nevertheless, some general structural concepts may be deduced. The awareness of the high application potential of S-layer glycoproteins, especially in combination with their intrinsic cell surface display feature, in the field of modern nanobiotechnology as a base for glycoengineering has recently led to the investigation of the S-layer protein glycosylation process at the molecular level, which has lagged behind the structural studies due to the lack of suitable molecular tools. From that work an even more interesting picture of this class of glycoconjugates is emerging. The availability of purified enzymes from S-layer glycan biosynthesis pathways exhibiting increased stabilities and/or rare sugar specificities in conjunction with preliminary genomic data on S-layer glycan biosynthesis clusters will pave the way for the rational design of S-layer neoglycoproteins.
LPS, bacterial glycosylation, genomic glycosylation loci, glycan diversity, glycoengineering, S-layer nanoglycobiology
NCBI PubMed ID: 15044388Publication DOI: 10.1093/glycob/cwh064Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Correspondence: paul.messner@boka.ac.at
Institutions: Center for NanoBiotechnology, University of Applied Life Sciences and Natural Resources, Gregor-Mendel-Strasse 33, A-1180 Wien, Austria
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2. Compound ID: 1471
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Me-3)-{{{-a-L-Rhap-(1-4)-a-D-Manp-(1-3)-}}}/n=28/-a-L-Rhap-(1-3)-a-L-Rhap-(1-3)-a-L-Rhap-(1-3)-b-D-Galp-(1-7)-Tyr |
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Structure type: oligomer
Compound class: S-layer glycoprotein
Contained glycoepitopes: IEDB_130701,IEDB_136044,IEDB_136105,IEDB_137472,IEDB_137477,IEDB_141794,IEDB_144983,IEDB_152206,IEDB_190606,IEDB_225177,IEDB_885823,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_44,SB_67,SB_7,SB_72,SB_88
The structure is contained in the following publication(s):
- Article ID: 468
Schäffer C, Messner P "Surface-layer glycoproteins: an example for the diversity of bacterial glycosylation with promising impacts on nanobiotechnology" -
Glycobiology 14(8) (2004) 31R-42R
Bacterial cell surface layers, referred to simply as S-layers, have been described for all major phylogenetic groups of bacteria, which may indicate their pivotal role for a bacterium in its natural habitat. They have the unique ability to assemble into two-dimensional crystalline arrays that completely cover the bacterial cells. Glycosylation represents the most frequent modification of S-layer proteins. S-layer glycoproteins constitute a class of glycoconjugates first isolated in the mid-1970s, but S-layer glycoprotein research is still being regarded as an 'exotic field of glycobiology,' possibly because of its 'noneukaryotic' character. Extensive work over the past 30 years provided evidence of an enormous diversity of S-layer glycoproteins that have been created in nature over 3 billion years of prokaryotic evolution. These glycoconjugates are substantially different from eukaryotic glycoproteins, with regard to both composition and structure; nevertheless, some general structural concepts may be deduced. The awareness of the high application potential of S-layer glycoproteins, especially in combination with their intrinsic cell surface display feature, in the field of modern nanobiotechnology as a base for glycoengineering has recently led to the investigation of the S-layer protein glycosylation process at the molecular level, which has lagged behind the structural studies due to the lack of suitable molecular tools. From that work an even more interesting picture of this class of glycoconjugates is emerging. The availability of purified enzymes from S-layer glycan biosynthesis pathways exhibiting increased stabilities and/or rare sugar specificities in conjunction with preliminary genomic data on S-layer glycan biosynthesis clusters will pave the way for the rational design of S-layer neoglycoproteins.
LPS, bacterial glycosylation, genomic glycosylation loci, glycan diversity, glycoengineering, S-layer nanoglycobiology
NCBI PubMed ID: 15044388Publication DOI: 10.1093/glycob/cwh064Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Correspondence: paul.messner@boka.ac.at
Institutions: Center for NanoBiotechnology, University of Applied Life Sciences and Natural Resources, Gregor-Mendel-Strasse 33, A-1180 Wien, Austria
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3. Compound ID: 1472
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b-D-Galf-(1-3)-a-D-Galp-(1-2)-a-L-Rhap-(1-3)-a-D-Manp-(1-3)-a-L-Rhap-(1-3)-b-D-Glcp-(1-?)-Tyr |
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Structure type: oligomer
Compound class: S-layer glycoprotein
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_136105,IEDB_136906,IEDB_137472,IEDB_141794,IEDB_142488,IEDB_144983,IEDB_146664,IEDB_151528,IEDB_152206,IEDB_189517,IEDB_190606,IEDB_225177,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: 468
Schäffer C, Messner P "Surface-layer glycoproteins: an example for the diversity of bacterial glycosylation with promising impacts on nanobiotechnology" -
Glycobiology 14(8) (2004) 31R-42R
Bacterial cell surface layers, referred to simply as S-layers, have been described for all major phylogenetic groups of bacteria, which may indicate their pivotal role for a bacterium in its natural habitat. They have the unique ability to assemble into two-dimensional crystalline arrays that completely cover the bacterial cells. Glycosylation represents the most frequent modification of S-layer proteins. S-layer glycoproteins constitute a class of glycoconjugates first isolated in the mid-1970s, but S-layer glycoprotein research is still being regarded as an 'exotic field of glycobiology,' possibly because of its 'noneukaryotic' character. Extensive work over the past 30 years provided evidence of an enormous diversity of S-layer glycoproteins that have been created in nature over 3 billion years of prokaryotic evolution. These glycoconjugates are substantially different from eukaryotic glycoproteins, with regard to both composition and structure; nevertheless, some general structural concepts may be deduced. The awareness of the high application potential of S-layer glycoproteins, especially in combination with their intrinsic cell surface display feature, in the field of modern nanobiotechnology as a base for glycoengineering has recently led to the investigation of the S-layer protein glycosylation process at the molecular level, which has lagged behind the structural studies due to the lack of suitable molecular tools. From that work an even more interesting picture of this class of glycoconjugates is emerging. The availability of purified enzymes from S-layer glycan biosynthesis pathways exhibiting increased stabilities and/or rare sugar specificities in conjunction with preliminary genomic data on S-layer glycan biosynthesis clusters will pave the way for the rational design of S-layer neoglycoproteins.
LPS, bacterial glycosylation, genomic glycosylation loci, glycan diversity, glycoengineering, S-layer nanoglycobiology
NCBI PubMed ID: 15044388Publication DOI: 10.1093/glycob/cwh064Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Correspondence: paul.messner@boka.ac.at
Institutions: Center for NanoBiotechnology, University of Applied Life Sciences and Natural Resources, Gregor-Mendel-Strasse 33, A-1180 Wien, Austria
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4. Compound ID: 1474
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b-D-Glcp-(1-6)-+
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b-D-Glcp-(1-6)-+ |
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a-D-Galp-(1-2)-+ | a-D-Galp-(1-2)-+ |
| | | |
{{{-a-L-Rhap-(1-3)-a-D-Manp-(1-4)-b-L-Rhap-(1-3)-a-D-Glcp-(1-4)-}}}/n=4-11/-a-L-Rhap-(1-3)-a-D-Manp-(1-4)-b-L-Rhap-(1-3)-b-D-Glcp-(1-7)-Tyr |
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Structure type: oligomer
Compound class: S-layer glycoprotein
Contained glycoepitopes: IEDB_130701,IEDB_136105,IEDB_136906,IEDB_137472,IEDB_141794,IEDB_142488,IEDB_144983,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_152206,IEDB_190606,IEDB_225177,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: 468
Schäffer C, Messner P "Surface-layer glycoproteins: an example for the diversity of bacterial glycosylation with promising impacts on nanobiotechnology" -
Glycobiology 14(8) (2004) 31R-42R
Bacterial cell surface layers, referred to simply as S-layers, have been described for all major phylogenetic groups of bacteria, which may indicate their pivotal role for a bacterium in its natural habitat. They have the unique ability to assemble into two-dimensional crystalline arrays that completely cover the bacterial cells. Glycosylation represents the most frequent modification of S-layer proteins. S-layer glycoproteins constitute a class of glycoconjugates first isolated in the mid-1970s, but S-layer glycoprotein research is still being regarded as an 'exotic field of glycobiology,' possibly because of its 'noneukaryotic' character. Extensive work over the past 30 years provided evidence of an enormous diversity of S-layer glycoproteins that have been created in nature over 3 billion years of prokaryotic evolution. These glycoconjugates are substantially different from eukaryotic glycoproteins, with regard to both composition and structure; nevertheless, some general structural concepts may be deduced. The awareness of the high application potential of S-layer glycoproteins, especially in combination with their intrinsic cell surface display feature, in the field of modern nanobiotechnology as a base for glycoengineering has recently led to the investigation of the S-layer protein glycosylation process at the molecular level, which has lagged behind the structural studies due to the lack of suitable molecular tools. From that work an even more interesting picture of this class of glycoconjugates is emerging. The availability of purified enzymes from S-layer glycan biosynthesis pathways exhibiting increased stabilities and/or rare sugar specificities in conjunction with preliminary genomic data on S-layer glycan biosynthesis clusters will pave the way for the rational design of S-layer neoglycoproteins.
LPS, bacterial glycosylation, genomic glycosylation loci, glycan diversity, glycoengineering, S-layer nanoglycobiology
NCBI PubMed ID: 15044388Publication DOI: 10.1093/glycob/cwh064Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Correspondence: paul.messner@boka.ac.at
Institutions: Center for NanoBiotechnology, University of Applied Life Sciences and Natural Resources, Gregor-Mendel-Strasse 33, A-1180 Wien, Austria
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5. Compound ID: 3456
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a-D-Manp-(1-4)-+
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b-D-Glcp-(1-4)-b-D-S6Quip-(1-3)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc-(1-1)-Tyr-(2-1)-Asn
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a-D-Manp-(1-6)-+ |
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Structure type: oligomer
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_137340,IEDB_141807,IEDB_142488,IEDB_144983,IEDB_146664,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_983930,IEDB_983931,SB_192,SB_44,SB_67,SB_72,SB_74,SB_85
The structure is contained in the following publication(s):
- Article ID: 1312
Zähringer U, Moll H, Hettmann T, Knirel YA, Schafer G "Cytochrome b558/566 from the archaeon Sulfolobus acidocaldarius has a unique Asn-linked highly branched hexasaccharide chain containing 6-sulfoquinovose" -
European Journal of Biochemistry 267(13) (2000) 4144-4149
Cytochrome b558/566 from the archaeon Sulfolobus acidocaldarius (DSM 639) has been described as a novel highly glycosylated membrane-bound b-type hemoprotein [Hettmann, T., Schmidt, C. L., Anemuller, S., Zähringer, U., Moll, Haemophilus, Petersen, A. & Schafer, G. (1998) J. Biol. Chem. 273, 12032-12040]. The purified cytochrome b558/566 was characterized by MALDI MS as a 64-kDa (glyco)protein expressing 17% glycosylation. Detailed chemical studies showed that it was exclusively O-mannosylated with monosaccharides and N-glycosylated with at least seven hexasaccharide units having the same unique structure. The hexasaccharide was released by cleavage with peptide:N-glycosidase (PNGase) F and found to consist of two residues each of Man and GlcNAc and one residue each of Glc and 6-deoxy-6-sulfoglucose (6-sulfoquinovose). The last sugar has been known as a component of glycolipids of plants and some prokaryotes, but has not been hitherto found in bacterial glycoproteins. Digestion with trypsin/pronase gave a mixture of glycopeptides with the same Asn-linked hexasaccharide chain, from which an N-glycosylated Tyr-Asn dipeptide was purified by gel chromatography and anion-exchange HPLC. Studies of the degradation products using methylation analysis, ESI MS, MALDI MS, and 1H and 13C NMR spectroscopy, including 1H,13C HMQC and NOESY experiments, established the structure of the unique Asn-linked hexasaccharide chain of cytochrome b558/566
structure, branched, hexasaccharide, chain, glycopeptide, glycoprotein, Archaeon, 6-sulfoquinovose
NCBI PubMed ID: 10866817Journal NLM ID: 0107600Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
Correspondence: uzaehr@fz-borstel.de
Institutions: Forschungszentrum Borstel, Zentrum fur Medizin und Biowissenschaften, Borstel, Germany
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6. Compound ID: 5645
Structure type: oligomer
Compound class: O-glycoprotein
Contained glycoepitopes: IEDB_142488,IEDB_146664,IEDB_983931,SB_192
The structure is contained in the following publication(s):
- Article ID: 2451
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
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7. Compound ID: 5872
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b-D-Galf-(1-3)-a-D-Galp-(1-2)-a-L-Rhap-(1-3)-a-D-Manp-(1-3)-a-L-Rhap-(1-3)-b-D-Glcp-(1-7)-Tyr |
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Structure type: oligomer
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_136105,IEDB_136906,IEDB_137472,IEDB_141794,IEDB_142488,IEDB_144983,IEDB_146664,IEDB_151528,IEDB_152206,IEDB_189517,IEDB_190606,IEDB_225177,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: 2596
Messner P, Christian R, Kolbe J, Schulz G, Sleytr UB "Analysis of a novel linkage unit of O-linked carbohydrates from the crystalline surface layer glycoprotein of Clostridium thermohydrosulfuricum S102-70" -
Journal of Bacteriology 174 (1992) 2236-2240
Journal NLM ID: 2985120RPublisher: American Society for Microbiology
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8. Compound ID: 6121
Structure type: oligomer
Compound class: O-glycoprotein
Contained glycoepitopes: IEDB_130701,IEDB_136104,IEDB_143632,IEDB_144983,IEDB_152206,IEDB_983930,SB_136,SB_196,SB_44,SB_67,SB_72
The structure is contained in the following publication(s):
- Article ID: 2730
Herrmann GF, Wang P, Shen GJ, Garcia-Junceda E, Khan SH, Matta KL, Wong CH "Large scale production of recombinant a-1,2-mannosyltransferase from E. coli for the study of acceptor specificity and use of the recombinant whole cells in synthesis" -
Journal of Organic Chemistry 59 (1994) 6356-6362
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9. Compound ID: 6379
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GroA-(2--P--4)--b-D-ManpNAc-(1-4)-+
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a-D-Glcp-(1-6)-+ a-D-Glcp-(1-6)-+ a-D-Glcp-(1-6)-+ |
| | | |
b-D-Galp-(1-4)-b-D-ManpNAc-(1-3)-{{{-b-D-Galp-(1-4)-b-D-ManpNAc-(1-3)-}}}/n=20/-b-D-Galp-(1-4)-b-D-ManpNAc-(1-3)-a-L-Rhap-(1-3)-a-L-Rhap-(1-3)-a-L-Rhap-(1-3)-b-D-Galp-(1-1)-Tyr |
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Structure type: oligomer
Trivial name: O-linked glycoprotein
Contained glycoepitopes: IEDB_136044,IEDB_136105,IEDB_137472,IEDB_141794,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_190606,IEDB_225177,IEDB_885813,IEDB_885823,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: 2877
Messner P, Christian R, Neuninger C, Schulz G "Similarity of "core" structures in two different glycans of tyrosine-linked eubacterial S-layer glycoproteins" -
Journal of Bacteriology 177 (1995) 2188-2193
Previously, the repeating-unit structure of the S-layer glycoprotein from the eubacterium Bacillus alvei CCM 2051 has been determined to be [→3)-β-D-Galp-(1→4)-[α-D-Glcp-(1→6)-]-β-D-ManpNAc-(1→]n (E. Altman, J.-R. Brisson, P. Messner, and U. B. Sleytr, Biochem. Cell Biol. 69:72-78, 1991). Nuclear magnetic resonance spectroscopic reexamination of this glycan reveals that the O-antigen-like domain of the polysaccharide is [see text] connected with the S-layer polypeptide through the "core" structure →3)-α-L-Rhap-(1→3)-α-L-Rhap-(1→3)-α-L-Rhap-(1→3)-β-D-Galp-(1→O)-Tyr. Except for the substitution in position 4 of the nonreducing rhamnose with the modified glyceric acid phosphate residue GroA-2→OPO2→4-β-D-ManpNAc-(1→, this core is identical to the core of the tyrosine-linked glycan from the S-layer glycoprotein of Thermoanaerobacter thermohydrosulfuricus L111-69 (K. Bock, J. Schuster-Kolbe, E. Altman, G. Allmaier, B. Stahl, R. Christian, U. B. Sleytr, and P. Messner, J. Biol. Chem. 269:7137-7144, 1994).
NCBI PubMed ID: 7721708Publication DOI: 10.1128/jb.177.8.2188-2193.1995Journal NLM ID: 2985120RPublisher: American Society for Microbiology
Institutions: Zentrum für Ultrastrukturforschung, Universität für Bodenkultur, Vienna, Austria
Methods: 13C NMR, 1H NMR
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10. Compound ID: 7306
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Subst-(1-4)-a-D-Manp-(1-3)-a-L-Rhap-(1-3)-a-L-Rhap-(1-3)-a-L-Rhap-(1-3)-b-D-Galp-(1-7)-Tyr
Subst = glycan chain (ID 22503) |
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Structure type: oligomer
Trivial name: S-layer glycoprotein
Contained glycoepitopes: IEDB_130701,IEDB_136044,IEDB_136105,IEDB_137472,IEDB_141794,IEDB_144983,IEDB_152206,IEDB_190606,IEDB_225177,IEDB_885823,IEDB_983930,SB_165,SB_166,SB_187,SB_195,SB_44,SB_67,SB_7,SB_72,SB_88
The structure is contained in the following publication(s):
- Article ID: 3310
Bock K, Schuster-Kolbe J, Altman E, Allmaier G, Stahl B, Christian R, Sleytr UB, Messner P "Primary structure of the O-glycosidically linked glycan chain of the crystalline surface layer glycoprotein of Thermoanaerobacter thermohydrosulfuricus L111-69. Galactosyl tyrosine as a novel linkage unit" -
Journal of Biological Chemistry 269(10) (1994) 7137-7144
The products of Pronase digestion of the crystalline surface layer (S-layer) glycoproteins of Thermoanaerobacter thermohydrosulfuricus strains L111-69 and L110-69 were isolated by gel permeation chromatography, cation exchange chromatography, chromatofocusing, and reversed phase high performance liquid chromatography. Four compounds were obtained which were analyzed by monosaccharide analysis, one- and two-dimensional 500 and 600 MHz 1H and 13C NMR spectroscopy, methylation analysis, gas-liquid chromatography/mass spectrometry, and matrix-assisted laser desorption ionization mass spectrometry. For all glycopeptides we propose the following glycan structure with galactose as the linkage sugar. [formula: see text] The isolated glycopeptides resulted from Pronase cleavage at the glycosylated tyrosine residues. Tyrosine was found as the linkage amino acid in all fractions but the remaining amino acid sequences varied, indicating the presence of different glycosylation sites in the intact S-layer glycoprotein
NMR spectroscopy, amino acid, S-layer, Clostridium, glycoprotein, Pronase
NCBI PubMed ID: 8125923Journal NLM ID: 2985121RPublisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Institutions: Department of Chemistry, Carlsberg Laboratory, Valby, Copenhagen, Denmark
Methods: 13C NMR, 1H NMR, methylation, NMR-2D, mild acid hydrolysis, MALDI-MS, alkaline hydrolysis, analytical methods, enzymatic digestion
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11. Compound ID: 9308
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GroA-(2--P--4)--b-D-ManpNAc-(1-4)-+
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a-D-Glcp-(1-6)-+ |
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{{{-b-D-Galp-(1-4)-b-D-ManpNAc-(1-3)-}}}/n=24/-a-L-Rhap-(1-3)-a-L-Rhap-(1-3)-a-L-Rhap-(1-3)-b-D-Galp-(1-7)-Tyr-(?--/tyrosine residues of the S-layer protein backbone/ |
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Structure type: oligomer
Aglycon: tyrosine residues of the S-layer protein backbone
Trivial name: S-layer O-glycan
Compound class: S-layer glycoprotein
Contained glycoepitopes: IEDB_136044,IEDB_136105,IEDB_137472,IEDB_141794,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_190606,IEDB_225177,IEDB_885813,IEDB_885823,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: 3967
Zarschler K, Janesch B, Pabst M, Altmann F, Messner P, Schäffer C "Protein tyrosine O-glycosylation - A rather unexplored prokaryotic glycosylation system" -
Glycobiology 20(6) (2010) 787-798
lycosylation is a frequent and heterogeneous posttranslational protein modification occurring in all domains of life. While protein N-glycosylation at asparagine and O-glycosylation at serine, threonine or hydroxyproline residues have been studied in great detail, only few data are available on O-glycosidic attachment of glycans to the amino acid tyrosine. In this study, we describe the identification and characterization of a bacterial protein tyrosine O-glycosylation system. In the Gram-positive, mesophilic bacterium Paenibacillus alvei CCM 2051T, a polysaccharide consisting of [→3)-β-D-Galp-(1[α-D-Glcp-(1→6)] →4)-β-D-ManpNAc-(1→] repeating units is O-glycosidically linked via an adaptor with the structure -[GroA-2→OPO2→4-β-D-ManpNAc-(1→4)] →3)-α-L-Rhap-(1→3)-α-L-Rhap-(1→3)-α-L-Rhap-(1→3)-β-D-Galp-(1→ to specific tyrosine residues of the S-layer protein SpaA. A +AH4-24.3-kb S-layer glycosylation (slg) gene cluster encodes the information necessary for the biosynthesis of this glycan chain within 18 open reading frames (ORF). The corresponding translation products are involved in the biosynthesis of nucleotide-activated monosaccharides, assembly and export as well as in the transfer of the completed polysaccharide chain to the S-layer target protein. All ORFs of the cluster, except those encoding the nucleotide sugar biosynthesis enzymes and the ATP binding cassette (ABC) transporter integral transmembrane proteins, were disrupted by the insertion of the mobile group II intron Ll.LtrB, and S-layer glycoproteins produced in mutant backgrounds were analyzed by mass spectrometry. There is evidence that the glycan chain is synthesized in a process comparable to the ABC-transporter-dependent pathway of the lipopolysaccharide O-polysaccharide biosynthesis. Furthermore, with the protein WsfB, we have identified an O-oligosaccharyl:protein transferase required for the formation of the covalent β-D-Gal→Tyr linkage between the glycan chain and the S-layer protein.
S-layer, glycosylation gene cluster, Paenibacillus alvei, tyrosine O-glycosylation
NCBI PubMed ID: 20200052Publication DOI: 10.1093/glycob/cwq035Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Correspondence: paul.messner@boku.ac.at; christina.schae?er@boku.ac.at
Institutions: Department of NanoBiotechnology, Vienna Institute of BioTechnology, Universitat fur Bodenkultur Wien, A-1190 Vienna, Austria
Methods: PCR, SDS-PAGE, DNA techniques, ESI-MS, genetic methods, RT-PCR, LC-MS
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12. Compound ID: 14143
| Cyclic
Subst2-(1-2)-D-aThr-(1-2)-+ b-D-Manp-(1-3)-+
| |
-3)-Thr-(1-2)-Thr-(1-2)-D-Tyr-(1-2)-Subst-(1-2)-Gln-(1-2)-Gly-(1-2)-Thr2Me-(1-2)-Gln-(1-
Subst = (2Z)-2-aminobut-2-enoic acid = SMILES C/C={2}C(N)\{1}C(=O)O;
Subst2 = 2,3-dihydroxymyristic acid = SMILES CCCCCCCCCCCC(O)C(O){1}C(=O)O |
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Structure type: cyclic polymer repeating unit
; 1404.67572 [M+Na]+, n=1
C62H99N11O24
Trivial name: hassalidin A
Compound class: glycopeptide
Contained glycoepitopes: IEDB_137485,IEDB_144983,IEDB_152206,IEDB_983930,SB_44,SB_72
The structure is contained in the following publication(s):
- Article ID: 5580
Neuhof T, Schmieder P, Preussel K, Dieckmann R, Pham H, Bartl F, von Döhren H "Hassallidin A, a glycosylated lipopeptide with antifungal activity from the cyanobacterium Hassallia sp." -
Journal of Natural Products 68(5) (2005) 695-700
Hassallidin A (1), a new antifungal glycosylated lipopeptide, was isolated from an epilithic cyanobacterium collected in Bellano, Italy, identified as Tolypothrix (basionym Hassallia) species. Chemical, mass spectrometric, and spectroscopic analyses, including one- and two-dimensional NMR, were performed to determine an esterified eight-residue cyclic peptide linked with a carbohydrate and a fatty acid residue. Chiral GC-MS analysis revealed the occurrence of the nonproteinogenic amino acids D-allo-Thr, D-Thr, D-Tyr, D-Gln, and dehydroaminobutyric acid (Dhb) within the peptide moiety. The additional components of hassallidin A could be identified as alpha,beta-dihydroxytetradecanoic acid (Dht) and mannose. This is the first report on a cyclic peptide of cyanobacterial origin that contains both a fatty acid and a carbohydrate moiety. Compound 1 exhibits antifungal activity against Aspergillus fumigatus and Candida albicans with MIC values of 4.8 μg/mL for both test organisms
hassalidin A, antifungal activity, Tolypothrix, cyclic peptide
NCBI PubMed ID: 15921412Publication DOI: 10.1021/np049671rJournal NLM ID: 7906882Publisher: American Society of Pharmacognosy
Correspondence: doehren@chem.tu-berlin.de
Institutions: Institut für Chemie, Fak. II, Technische Universität Berlin, Berlin, Germany, Forschungsinstitut für Molekulare Pharmakologie, Berlin, Germany, Institut für Medizinische Physik und Biophysik, Charité-Universitätsmedizin Berlin, Humboldt-Universität, Berlin, Germany, Zentrum für Biophysik und Bioinformatik, Humboldt-Universität, Berlin, Germany
Methods: 13C NMR, 1H NMR, NMR-2D, IR, GC-MS, ESI-MS, acid hydrolysis, ESI-ICR-MS, amino acid analysis, MALDI-TOF MS, HPLC, UV, extraction, 15N NMR, cell growth, derivatization, evaporation, centrifugation, antifungal activity test, optical density measurement
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13. Compound ID: 14216
| Cyclic
a-D-Manp1N-(1-5)-+ iVl-(1-3)-a-D-Manp-(1-4)-a-D-Manp-(1-7)-+
| |
-2)-Subst-(1-2)-Subst-(1-2)-L-Ser-(1-2)-Gly-(1-2)-Subst2-(1-2)-D-Tyr-(1-
Subst = SMILES N=C1NCC([C@H](O){2}[C@@H](N){1}C(=O)O){5}N1;
Subst2 = SMILES C[C@@H](c1ccccc1){2}[C@H](N){1}C(=O)O |
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Structure type: cyclic polymer repeating unit
; n=1
Trivial name: mannopeptimycin δ
Compound class: glycopeptide
Contained glycoepitopes: IEDB_130701,IEDB_144983,IEDB_150900,IEDB_152206,IEDB_983930,SB_44,SB_67,SB_72
The structure is contained in the following publication(s):
- Article ID: 5599
Wu MC, Styles MQ, Law BJ, Struck AW, Nunns L, Micklefield J "Engineered biosynthesis of enduracidin lipoglycopeptide antibiotics using the ramoplanin mannosyltransferase Ram29" -
Microbiology 161(7) (2015) 1338-1347
The lipopeptides ramoplanin from Actinoplanes sp. ATCC 33076 and enduracidin produced by Streptomyces fungicidicus are effective antibiotics against a number of drug-resistant Gram-positive pathogens. While these two antibiotics share a similar cyclic peptide structure, comprising 17 amino acids with an N-terminal fatty acid side chain, ramoplanin has a di-mannose moiety that enduracidin lacks. The mannosyl substituents of ramoplanin enhance aqueous solubility, which was important in the development of ramoplanin as a potential treatment for Clostridium difficile infections. In this study we have determined the function of the putative mannosyltransferase encoded by ram29 from the ramoplanin biosynthetic gene cluster. Bioinformatics revealed that Ram29 is an integral membrane protein with a putative DxD motif that is suggested to bind to, and activate, a polyprenyl phosphomannose donor and an extracytoplasmic C-terminal domain that is predicted to bind the ramoplanin aglycone acceptor. The ram29 gene was cloned into the tetracycline inducible plasmid pMS17 and integrated into the genome of the enduracidin producer S. fungicidicus. Induction of ram29 expression in S. fungicidicus resulted in the production of monomannosylated enduracidin derivatives, which are not present in the WT strain. Tandem MS analysis showed that mannosylation occurs on the Hpg11 residue of enduracidin. In addition to confirming the function of Ram29, these findings demonstrate how the less common, membrane-associated, polyprenyl phosphosugar-dependent glycosyltransferases can be used in natural product glycodiversification. Such a strategy may be valuable in future biosynthetic engineering approaches aimed at improving the physico-chemical and biological properties of bioactive secondary metabolites including antibiotics
biosynthesis, antibiotics, nonribosomal peptides, lipoglycopeptides, mannosylation, glycodiversification
NCBI PubMed ID: 25878261Publication DOI: 10.1099/mic.0.000095Journal NLM ID: 0376646Publisher: Washington, DC: Kluwer Academic/Plenum Publishers
Correspondence: Jason.micklefield@manchester.ac.uk
Institutions: School of Chemistry and Manchester Institute of Biotechnology, The University of Manchester, Manchester, UK
Methods: PCR, DNA sequencing, DNA techniques, HPLC, UV, extraction, ESI-QTOF-MS/MS, LC-ESI-MS, cell growth, centrifugation
- Article ID: 5602
Singh MP, Petersen PJ, Weiss WJ, Janso JE, Luckman SW, Lenoy EB, Bradford PA, Testa RT, Greenstein M "Mannopeptimycins, new cyclic glycopeptide antibiotics produced by Streptomyces hygroscopicus LL-AC98: antibacterial and mechanistic activities" -
Antimicrobial Agents and Chemotherapy 47(1) (2003) 62-69
Mannopeptimycins alpha, beta, gamma, delta, and epsilon are new cyclic glycopeptide antibiotics produced by Streptomyces hygroscopicus LL-AC98. Mannopeptimycins gamma, delta, and epsilon, which have an isovaleryl substitution at various positions on the terminal mannose of the disaccharide moiety, demonstrated moderate to good antibacterial activities. Mannopeptimycin epsilon was the most active component against methicillin-resistant staphylococci and vancomycin-resistant enterococci (MICs, 2 to 4 μg/ml for staphylococci and streptococci and 4 to 32 μg/ml for enterococci), while mannopeptimycins gamma and delta were two- to fourfold less active. Mannopeptimycins alpha and beta, which lack the isovaleryl substitution and the disaccharide moiety, respectively, had poor antibacterial activities. The in vivo efficacies of the mannopeptimycins in Staphylococcus aureus mouse protection studies paralleled their in vitro activities. The median effective doses of mannopeptimycins gamma, delta, and epsilon were 3.8, 2.6, and 0.59 mg/kg of body weight, respectively. The mannopeptimycins were inactive against cell wall-deficient S. aureus and caused spheroplasting of Escherichia coli imp similar to that observed with penicillin G in an osmotically protective medium. Mannopeptimycin delta rapidly inhibited [(3)H]N-acetylglucosamine incorporation into peptidoglycan in Bacillus subtilis and had no effect on DNA, RNA, or protein biosynthesis. On the basis of the observations presented above, an effect on cell wall biosynthesis was suggested as the primary mode of action for mannopeptimycin delta. The mannopeptimycins were inactive against Candida albicans, did not initiate hemolysis of human erythrocytes, and did not promote potassium ion leakage from E. coli imp, suggesting a lack of membrane damage to prokaryotic or eukaryotic cells
glycopeptides, antibiotics, mannopeptimycins, Streptomyces hygroscopicus LL-AC98
NCBI PubMed ID: 12499170Publication DOI: 10.1128/aac.47.1.62-69.2003Journal NLM ID: 0315061Correspondence: singhm@wyeth.com
Institutions: Natural Products Microbiology, Wyeth Research, Pearl River, NY, USA, Antibacterial Research, Infectious Disease Section, Wyeth Research, Pearl River, NY, USA
Methods: biological assays, cell growth, antibacterial assay
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14. Compound ID: 14224
| Cyclic
a-D-Manp1N-(1-5)-+ a-D-Manp-(1-4)-a-D-Manp-(1-7)-+
| |
-2)-Subst-(1-2)-Subst-(1-2)-L-Ser-(1-2)-Gly-(1-2)-Subst2-(1-2)-D-Tyr-(1-
Subst = SMILES N=C1NCC([C@H](O){2}[C@@H](N){1}C(=O)O){5}N1;
Subst2 = SMILES C[C@@H](c1ccccc1){2}[C@H](N){1}C(=O)O |
Show graphically |
Structure type: cyclic polymer repeating unit
; n=1
Trivial name: mannopeptimycin α
Compound class: glycopeptide
Contained glycoepitopes: IEDB_130701,IEDB_144983,IEDB_150900,IEDB_152206,IEDB_983930,SB_44,SB_67,SB_72
The structure is contained in the following publication(s):
- Article ID: 5602
Singh MP, Petersen PJ, Weiss WJ, Janso JE, Luckman SW, Lenoy EB, Bradford PA, Testa RT, Greenstein M "Mannopeptimycins, new cyclic glycopeptide antibiotics produced by Streptomyces hygroscopicus LL-AC98: antibacterial and mechanistic activities" -
Antimicrobial Agents and Chemotherapy 47(1) (2003) 62-69
Mannopeptimycins alpha, beta, gamma, delta, and epsilon are new cyclic glycopeptide antibiotics produced by Streptomyces hygroscopicus LL-AC98. Mannopeptimycins gamma, delta, and epsilon, which have an isovaleryl substitution at various positions on the terminal mannose of the disaccharide moiety, demonstrated moderate to good antibacterial activities. Mannopeptimycin epsilon was the most active component against methicillin-resistant staphylococci and vancomycin-resistant enterococci (MICs, 2 to 4 μg/ml for staphylococci and streptococci and 4 to 32 μg/ml for enterococci), while mannopeptimycins gamma and delta were two- to fourfold less active. Mannopeptimycins alpha and beta, which lack the isovaleryl substitution and the disaccharide moiety, respectively, had poor antibacterial activities. The in vivo efficacies of the mannopeptimycins in Staphylococcus aureus mouse protection studies paralleled their in vitro activities. The median effective doses of mannopeptimycins gamma, delta, and epsilon were 3.8, 2.6, and 0.59 mg/kg of body weight, respectively. The mannopeptimycins were inactive against cell wall-deficient S. aureus and caused spheroplasting of Escherichia coli imp similar to that observed with penicillin G in an osmotically protective medium. Mannopeptimycin delta rapidly inhibited [(3)H]N-acetylglucosamine incorporation into peptidoglycan in Bacillus subtilis and had no effect on DNA, RNA, or protein biosynthesis. On the basis of the observations presented above, an effect on cell wall biosynthesis was suggested as the primary mode of action for mannopeptimycin delta. The mannopeptimycins were inactive against Candida albicans, did not initiate hemolysis of human erythrocytes, and did not promote potassium ion leakage from E. coli imp, suggesting a lack of membrane damage to prokaryotic or eukaryotic cells
glycopeptides, antibiotics, mannopeptimycins, Streptomyces hygroscopicus LL-AC98
NCBI PubMed ID: 12499170Publication DOI: 10.1128/aac.47.1.62-69.2003Journal NLM ID: 0315061Correspondence: singhm@wyeth.com
Institutions: Natural Products Microbiology, Wyeth Research, Pearl River, NY, USA, Antibacterial Research, Infectious Disease Section, Wyeth Research, Pearl River, NY, USA
Methods: biological assays, cell growth, antibacterial assay
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15. Compound ID: 14225
| Cyclic
a-D-Manp1N-(1-5)-+
|
-2)-Subst-(1-2)-Subst-(1-2)-L-Ser-(1-2)-Gly-(1-2)-Subst2-(1-2)-D-Tyr-(1-
Subst = SMILES N=C1NCC([C@H](O){2}[C@@H](N){1}C(=O)O){5}N1;
Subst2 = SMILES C[C@@H](c1ccccc1){2}[C@H](N){1}C(=O)O |
Show graphically |
Structure type: cyclic polymer repeating unit
; n=1
Trivial name: mannopeptimycin β
Compound class: glycopeptide
Contained glycoepitopes: IEDB_150900
The structure is contained in the following publication(s):
- Article ID: 5602
Singh MP, Petersen PJ, Weiss WJ, Janso JE, Luckman SW, Lenoy EB, Bradford PA, Testa RT, Greenstein M "Mannopeptimycins, new cyclic glycopeptide antibiotics produced by Streptomyces hygroscopicus LL-AC98: antibacterial and mechanistic activities" -
Antimicrobial Agents and Chemotherapy 47(1) (2003) 62-69
Mannopeptimycins alpha, beta, gamma, delta, and epsilon are new cyclic glycopeptide antibiotics produced by Streptomyces hygroscopicus LL-AC98. Mannopeptimycins gamma, delta, and epsilon, which have an isovaleryl substitution at various positions on the terminal mannose of the disaccharide moiety, demonstrated moderate to good antibacterial activities. Mannopeptimycin epsilon was the most active component against methicillin-resistant staphylococci and vancomycin-resistant enterococci (MICs, 2 to 4 μg/ml for staphylococci and streptococci and 4 to 32 μg/ml for enterococci), while mannopeptimycins gamma and delta were two- to fourfold less active. Mannopeptimycins alpha and beta, which lack the isovaleryl substitution and the disaccharide moiety, respectively, had poor antibacterial activities. The in vivo efficacies of the mannopeptimycins in Staphylococcus aureus mouse protection studies paralleled their in vitro activities. The median effective doses of mannopeptimycins gamma, delta, and epsilon were 3.8, 2.6, and 0.59 mg/kg of body weight, respectively. The mannopeptimycins were inactive against cell wall-deficient S. aureus and caused spheroplasting of Escherichia coli imp similar to that observed with penicillin G in an osmotically protective medium. Mannopeptimycin delta rapidly inhibited [(3)H]N-acetylglucosamine incorporation into peptidoglycan in Bacillus subtilis and had no effect on DNA, RNA, or protein biosynthesis. On the basis of the observations presented above, an effect on cell wall biosynthesis was suggested as the primary mode of action for mannopeptimycin delta. The mannopeptimycins were inactive against Candida albicans, did not initiate hemolysis of human erythrocytes, and did not promote potassium ion leakage from E. coli imp, suggesting a lack of membrane damage to prokaryotic or eukaryotic cells
glycopeptides, antibiotics, mannopeptimycins, Streptomyces hygroscopicus LL-AC98
NCBI PubMed ID: 12499170Publication DOI: 10.1128/aac.47.1.62-69.2003Journal NLM ID: 0315061Correspondence: singhm@wyeth.com
Institutions: Natural Products Microbiology, Wyeth Research, Pearl River, NY, USA, Antibacterial Research, Infectious Disease Section, Wyeth Research, Pearl River, NY, USA
Methods: biological assays, cell growth, antibacterial assay
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