Found 11 structures.
Displayed structures from 1 to 11
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1. Compound ID: 21766
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a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-3)-+
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a-D-Manp-(1-2)-a-D-Manp-(1-3)-+ |
| |
a-D-Manp-(1-2)-+ | |
| | |
EtN-(1--P--?)--a-D-Manp-(1-6)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcNAc-ol-(1-2)-Subst
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D-Galf-(1-?)-+
Subst = 2-aminopyridine = SMILES N{2}c1ccccn1 |
Show graphically |
Structure type: oligomer
; 2246 [M+H]+
Compound class: mannan
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130701,IEDB_135813,IEDB_136095,IEDB_136104,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_143632,IEDB_144983,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_190606,IEDB_429156,IEDB_474450,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_53,SB_67,SB_72,SB_73,SB_77
The structure is contained in the following publication(s):
- Article ID: 8775
Hykollari A, Eckmair B, Voglmeir J, Jin C, Yan S, Vanbeselaere J, Razzazi-Fazeli E, Wilson IB, Paschinger K "More than just oligomannose: an N-glycomic comparison of Penicillium species" -
Molecular and Cellular Proteomics 15(1) (2016) 73-92
N-glycosylation is an essential set of post-translational modifications of proteins; in the case of filamentous fungi, N-glycans are present on a range of secreted and cell wall proteins. In this study, we have compared the glycans released by peptide/N-glycosidase F from proteolysed cell pellets of three Penicillium species (P. dierckxii, P. nordicum and P. verrucosum that all belong to the Eurotiomycetes). Although the major structures are all within the range Hex(5-11)HexNAc(2) as shown by mass spectrometry, variations in reversed-phase chromatograms and MS/MS fragmentation patterns are indicative of differences in the actual structure. Hydrofluoric acid and mannosidase treatments revealed that the oligomannosidic glycans were not only in part modified with phosphoethanolamine residues and outer chain och1-dependent mannosylation, but that bisecting galactofuranose was present in a species-dependent manner. These data are the first to specifically show the modification of N-glycans in fungi with zwitterionic moieties. Furthermore, our results indicate that mere mass spectrometric screening is insufficient to reveal the subtly complex nature of N-glycosylation even within a single fungal genus.
mass spectrometry, N-glycan, Penicillium
NCBI PubMed ID: 26515459Publication DOI: 10.1074/mcp.M115.055061Journal NLM ID: 101125647Publisher: Bethesda, MD: ASBMB
Correspondence: Paschinger K
Institutions: Department für Chemie, Universität für Bodenkultur, Wien, Austria, Institutionen för Biomedicin, Göteborgs universitet, Göteborg, Sweden, VetOMICS Core Facility, Veterinärmedizinische Universität, Wien, Austria
Methods: HF hydrolysis, MALDI-TOF MS/MS, fluorescent labeling with 2-aminopyridine, PR-HPLC
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2. Compound ID: 21767
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a-D-Manp-(1-6)-+
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a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-3)-+
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a-D-Manp-(1-2)-a-D-Manp-(1-3)-+ |
| |
a-D-Manp-(1-2)-+ | |
| | |
EtN-(1--P--?)--a-D-Manp-(1-6)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcNAc-ol-(1-2)-Subst
|
D-Galf-(1-?)-+
Subst = 2-aminopyridine = SMILES N{2}c1ccccn1 |
Show graphically |
Structure type: oligomer
; 2409 [M+H]+
Compound class: mannan
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130701,IEDB_135813,IEDB_136095,IEDB_136104,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_143632,IEDB_144983,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_190606,IEDB_429156,IEDB_474450,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_53,SB_67,SB_72,SB_73,SB_77
The structure is contained in the following publication(s):
- Article ID: 8775
Hykollari A, Eckmair B, Voglmeir J, Jin C, Yan S, Vanbeselaere J, Razzazi-Fazeli E, Wilson IB, Paschinger K "More than just oligomannose: an N-glycomic comparison of Penicillium species" -
Molecular and Cellular Proteomics 15(1) (2016) 73-92
N-glycosylation is an essential set of post-translational modifications of proteins; in the case of filamentous fungi, N-glycans are present on a range of secreted and cell wall proteins. In this study, we have compared the glycans released by peptide/N-glycosidase F from proteolysed cell pellets of three Penicillium species (P. dierckxii, P. nordicum and P. verrucosum that all belong to the Eurotiomycetes). Although the major structures are all within the range Hex(5-11)HexNAc(2) as shown by mass spectrometry, variations in reversed-phase chromatograms and MS/MS fragmentation patterns are indicative of differences in the actual structure. Hydrofluoric acid and mannosidase treatments revealed that the oligomannosidic glycans were not only in part modified with phosphoethanolamine residues and outer chain och1-dependent mannosylation, but that bisecting galactofuranose was present in a species-dependent manner. These data are the first to specifically show the modification of N-glycans in fungi with zwitterionic moieties. Furthermore, our results indicate that mere mass spectrometric screening is insufficient to reveal the subtly complex nature of N-glycosylation even within a single fungal genus.
mass spectrometry, N-glycan, Penicillium
NCBI PubMed ID: 26515459Publication DOI: 10.1074/mcp.M115.055061Journal NLM ID: 101125647Publisher: Bethesda, MD: ASBMB
Correspondence: Paschinger K
Institutions: Department für Chemie, Universität für Bodenkultur, Wien, Austria, Institutionen för Biomedicin, Göteborgs universitet, Göteborg, Sweden, VetOMICS Core Facility, Veterinärmedizinische Universität, Wien, Austria
Methods: HF hydrolysis, MALDI-TOF MS/MS, fluorescent labeling with 2-aminopyridine, PR-HPLC
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3. Compound ID: 21770
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a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-3)-+
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a-D-Manp-(1-2)-a-D-Manp-(1-6)-+ |
| |
a-D-Manp-(1-2)-a-D-Manp-(1-3)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcNAc-ol-(1-2)-Subst
|
D-Galf-(1-?)-+
Subst = 2-aminopyridine = SMILES N{2}c1ccccn1 |
Show graphically |
Structure type: oligomer
; 2123.66 [M+H]+
Compound class: mannan
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_136095,IEDB_136104,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_143632,IEDB_144983,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_190606,IEDB_429156,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_53,SB_67,SB_72,SB_73,SB_77
The structure is contained in the following publication(s):
- Article ID: 8775
Hykollari A, Eckmair B, Voglmeir J, Jin C, Yan S, Vanbeselaere J, Razzazi-Fazeli E, Wilson IB, Paschinger K "More than just oligomannose: an N-glycomic comparison of Penicillium species" -
Molecular and Cellular Proteomics 15(1) (2016) 73-92
N-glycosylation is an essential set of post-translational modifications of proteins; in the case of filamentous fungi, N-glycans are present on a range of secreted and cell wall proteins. In this study, we have compared the glycans released by peptide/N-glycosidase F from proteolysed cell pellets of three Penicillium species (P. dierckxii, P. nordicum and P. verrucosum that all belong to the Eurotiomycetes). Although the major structures are all within the range Hex(5-11)HexNAc(2) as shown by mass spectrometry, variations in reversed-phase chromatograms and MS/MS fragmentation patterns are indicative of differences in the actual structure. Hydrofluoric acid and mannosidase treatments revealed that the oligomannosidic glycans were not only in part modified with phosphoethanolamine residues and outer chain och1-dependent mannosylation, but that bisecting galactofuranose was present in a species-dependent manner. These data are the first to specifically show the modification of N-glycans in fungi with zwitterionic moieties. Furthermore, our results indicate that mere mass spectrometric screening is insufficient to reveal the subtly complex nature of N-glycosylation even within a single fungal genus.
mass spectrometry, N-glycan, Penicillium
NCBI PubMed ID: 26515459Publication DOI: 10.1074/mcp.M115.055061Journal NLM ID: 101125647Publisher: Bethesda, MD: ASBMB
Correspondence: Paschinger K
Institutions: Department für Chemie, Universität für Bodenkultur, Wien, Austria, Institutionen för Biomedicin, Göteborgs universitet, Göteborg, Sweden, VetOMICS Core Facility, Veterinärmedizinische Universität, Wien, Austria
Methods: HF hydrolysis, MALDI-TOF MS/MS, fluorescent labeling with 2-aminopyridine, PR-HPLC
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4. Compound ID: 21771
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a-D-Manp-(1-2)-a-D-Manp-(1-3)-+
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a-D-Manp-(1-2)-a-D-Manp-(1-6)-+ |
| |
a-D-Manp-(1-2)-a-D-Manp-(1-3)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcNAc-ol-(1-2)-Subst
|
D-Galf-(1-?)-+
Subst = 2-aminopyridine = SMILES N{2}c1ccccn1 |
Show graphically |
Structure type: oligomer
; 1961 [M+H]+
Compound class: mannan
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_136095,IEDB_136104,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141831,IEDB_143632,IEDB_144983,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_190606,IEDB_429156,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_53,SB_67,SB_72,SB_73,SB_77
The structure is contained in the following publication(s):
- Article ID: 8775
Hykollari A, Eckmair B, Voglmeir J, Jin C, Yan S, Vanbeselaere J, Razzazi-Fazeli E, Wilson IB, Paschinger K "More than just oligomannose: an N-glycomic comparison of Penicillium species" -
Molecular and Cellular Proteomics 15(1) (2016) 73-92
N-glycosylation is an essential set of post-translational modifications of proteins; in the case of filamentous fungi, N-glycans are present on a range of secreted and cell wall proteins. In this study, we have compared the glycans released by peptide/N-glycosidase F from proteolysed cell pellets of three Penicillium species (P. dierckxii, P. nordicum and P. verrucosum that all belong to the Eurotiomycetes). Although the major structures are all within the range Hex(5-11)HexNAc(2) as shown by mass spectrometry, variations in reversed-phase chromatograms and MS/MS fragmentation patterns are indicative of differences in the actual structure. Hydrofluoric acid and mannosidase treatments revealed that the oligomannosidic glycans were not only in part modified with phosphoethanolamine residues and outer chain och1-dependent mannosylation, but that bisecting galactofuranose was present in a species-dependent manner. These data are the first to specifically show the modification of N-glycans in fungi with zwitterionic moieties. Furthermore, our results indicate that mere mass spectrometric screening is insufficient to reveal the subtly complex nature of N-glycosylation even within a single fungal genus.
mass spectrometry, N-glycan, Penicillium
NCBI PubMed ID: 26515459Publication DOI: 10.1074/mcp.M115.055061Journal NLM ID: 101125647Publisher: Bethesda, MD: ASBMB
Correspondence: Paschinger K
Institutions: Department für Chemie, Universität für Bodenkultur, Wien, Austria, Institutionen för Biomedicin, Göteborgs universitet, Göteborg, Sweden, VetOMICS Core Facility, Veterinärmedizinische Universität, Wien, Austria
Methods: HF hydrolysis, MALDI-TOF MS/MS, fluorescent labeling with 2-aminopyridine, PR-HPLC
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5. Compound ID: 21772
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a-D-Manp-(1-6)-+
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a-D-Manp-(1-2)-a-D-Manp-(1-2)-a-D-Manp-(1-3)-+
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a-D-Manp-(1-2)-a-D-Manp-(1-6)-+ |
| |
a-D-Manp-(1-2)-a-D-Manp-(1-3)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcNAc-ol-(1-2)-Subst
|
D-Galf-(1-?)-+
Subst = 2-aminopyridine = SMILES N{2}c1ccccn1 |
Show graphically |
Structure type: oligomer
; 2285 [M+H]+
Compound class: mannan
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_136095,IEDB_136104,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_143632,IEDB_144983,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_190606,IEDB_429156,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_53,SB_67,SB_72,SB_73,SB_77
The structure is contained in the following publication(s):
- Article ID: 8775
Hykollari A, Eckmair B, Voglmeir J, Jin C, Yan S, Vanbeselaere J, Razzazi-Fazeli E, Wilson IB, Paschinger K "More than just oligomannose: an N-glycomic comparison of Penicillium species" -
Molecular and Cellular Proteomics 15(1) (2016) 73-92
N-glycosylation is an essential set of post-translational modifications of proteins; in the case of filamentous fungi, N-glycans are present on a range of secreted and cell wall proteins. In this study, we have compared the glycans released by peptide/N-glycosidase F from proteolysed cell pellets of three Penicillium species (P. dierckxii, P. nordicum and P. verrucosum that all belong to the Eurotiomycetes). Although the major structures are all within the range Hex(5-11)HexNAc(2) as shown by mass spectrometry, variations in reversed-phase chromatograms and MS/MS fragmentation patterns are indicative of differences in the actual structure. Hydrofluoric acid and mannosidase treatments revealed that the oligomannosidic glycans were not only in part modified with phosphoethanolamine residues and outer chain och1-dependent mannosylation, but that bisecting galactofuranose was present in a species-dependent manner. These data are the first to specifically show the modification of N-glycans in fungi with zwitterionic moieties. Furthermore, our results indicate that mere mass spectrometric screening is insufficient to reveal the subtly complex nature of N-glycosylation even within a single fungal genus.
mass spectrometry, N-glycan, Penicillium
NCBI PubMed ID: 26515459Publication DOI: 10.1074/mcp.M115.055061Journal NLM ID: 101125647Publisher: Bethesda, MD: ASBMB
Correspondence: Paschinger K
Institutions: Department für Chemie, Universität für Bodenkultur, Wien, Austria, Institutionen för Biomedicin, Göteborgs universitet, Göteborg, Sweden, VetOMICS Core Facility, Veterinärmedizinische Universität, Wien, Austria
Methods: HF hydrolysis, MALDI-TOF MS/MS, fluorescent labeling with 2-aminopyridine, PR-HPLC
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6. Compound ID: 21773
|
a-D-Manp-(1-6)-+
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a-D-Manp-(1-2)-a-D-Manp-(1-3)-+
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a-D-Manp-(1-2)-a-D-Manp-(1-6)-+ |
| |
a-D-Manp-(1-2)-a-D-Manp-(1-3)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcNAc-ol-(1-2)-Subst
|
D-Galf-(1-?)-+
Subst = 2-aminopyridine = SMILES N{2}c1ccccn1 |
Show graphically |
Structure type: oligomer
; 2123.05 [M+H]+
Compound class: mannan
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_136095,IEDB_136104,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141831,IEDB_143632,IEDB_144983,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_190606,IEDB_429156,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_44,SB_53,SB_67,SB_72,SB_73,SB_77
The structure is contained in the following publication(s):
- Article ID: 8775
Hykollari A, Eckmair B, Voglmeir J, Jin C, Yan S, Vanbeselaere J, Razzazi-Fazeli E, Wilson IB, Paschinger K "More than just oligomannose: an N-glycomic comparison of Penicillium species" -
Molecular and Cellular Proteomics 15(1) (2016) 73-92
N-glycosylation is an essential set of post-translational modifications of proteins; in the case of filamentous fungi, N-glycans are present on a range of secreted and cell wall proteins. In this study, we have compared the glycans released by peptide/N-glycosidase F from proteolysed cell pellets of three Penicillium species (P. dierckxii, P. nordicum and P. verrucosum that all belong to the Eurotiomycetes). Although the major structures are all within the range Hex(5-11)HexNAc(2) as shown by mass spectrometry, variations in reversed-phase chromatograms and MS/MS fragmentation patterns are indicative of differences in the actual structure. Hydrofluoric acid and mannosidase treatments revealed that the oligomannosidic glycans were not only in part modified with phosphoethanolamine residues and outer chain och1-dependent mannosylation, but that bisecting galactofuranose was present in a species-dependent manner. These data are the first to specifically show the modification of N-glycans in fungi with zwitterionic moieties. Furthermore, our results indicate that mere mass spectrometric screening is insufficient to reveal the subtly complex nature of N-glycosylation even within a single fungal genus.
mass spectrometry, N-glycan, Penicillium
NCBI PubMed ID: 26515459Publication DOI: 10.1074/mcp.M115.055061Journal NLM ID: 101125647Publisher: Bethesda, MD: ASBMB
Correspondence: Paschinger K
Institutions: Department für Chemie, Universität für Bodenkultur, Wien, Austria, Institutionen för Biomedicin, Göteborgs universitet, Göteborg, Sweden, VetOMICS Core Facility, Veterinärmedizinische Universität, Wien, Austria
Methods: HF hydrolysis, MALDI-TOF MS/MS, fluorescent labeling with 2-aminopyridine, PR-HPLC
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7. Compound ID: 21774
|
a-D-Manp-(1-2)-a-D-Manp-(1-3)-+
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a-D-Manp-(1-6)-+ |
| |
a-D-Manp-(1-2)-a-D-Manp-(1-3)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcNAc-ol-(1-2)-Subst
|
D-Galf-(1-?)-+
Subst = 2-aminopyridine = SMILES N{2}c1ccccn1 |
Show graphically |
Structure type: oligomer
Compound class: mannan
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_136095,IEDB_136104,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_143632,IEDB_144983,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_190606,IEDB_429156,IEDB_857734,IEDB_983930,SB_136,SB_196,SB_197,SB_198,SB_44,SB_53,SB_67,SB_72,SB_73,SB_77
The structure is contained in the following publication(s):
- Article ID: 8775
Hykollari A, Eckmair B, Voglmeir J, Jin C, Yan S, Vanbeselaere J, Razzazi-Fazeli E, Wilson IB, Paschinger K "More than just oligomannose: an N-glycomic comparison of Penicillium species" -
Molecular and Cellular Proteomics 15(1) (2016) 73-92
N-glycosylation is an essential set of post-translational modifications of proteins; in the case of filamentous fungi, N-glycans are present on a range of secreted and cell wall proteins. In this study, we have compared the glycans released by peptide/N-glycosidase F from proteolysed cell pellets of three Penicillium species (P. dierckxii, P. nordicum and P. verrucosum that all belong to the Eurotiomycetes). Although the major structures are all within the range Hex(5-11)HexNAc(2) as shown by mass spectrometry, variations in reversed-phase chromatograms and MS/MS fragmentation patterns are indicative of differences in the actual structure. Hydrofluoric acid and mannosidase treatments revealed that the oligomannosidic glycans were not only in part modified with phosphoethanolamine residues and outer chain och1-dependent mannosylation, but that bisecting galactofuranose was present in a species-dependent manner. These data are the first to specifically show the modification of N-glycans in fungi with zwitterionic moieties. Furthermore, our results indicate that mere mass spectrometric screening is insufficient to reveal the subtly complex nature of N-glycosylation even within a single fungal genus.
mass spectrometry, N-glycan, Penicillium
NCBI PubMed ID: 26515459Publication DOI: 10.1074/mcp.M115.055061Journal NLM ID: 101125647Publisher: Bethesda, MD: ASBMB
Correspondence: Paschinger K
Institutions: Department für Chemie, Universität für Bodenkultur, Wien, Austria, Institutionen för Biomedicin, Göteborgs universitet, Göteborg, Sweden, VetOMICS Core Facility, Veterinärmedizinische Universität, Wien, Austria
Methods: HF hydrolysis, MALDI-TOF MS/MS, fluorescent labeling with 2-aminopyridine, PR-HPLC
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8. Compound ID: 21775
|
a-D-Manp-(1-3)-+
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a-D-Manp-(1-6)-+ |
| |
a-D-Manp-(1-3)-a-D-Manp-(1-6)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-D-GlcNAc-ol-(1-2)-Subst
|
D-Galf-(1-?)-+
Subst = 2-aminopyridine = SMILES N{2}c1ccccn1 |
Show graphically |
Structure type: oligomer
; 1475.59 [M+H]+
Compound class: mannan
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_136095,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140116,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_144983,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_164174,IEDB_190606,IEDB_429156,IEDB_857734,IEDB_983930,SB_197,SB_198,SB_44,SB_67,SB_72,SB_73,SB_77
The structure is contained in the following publication(s):
- Article ID: 8775
Hykollari A, Eckmair B, Voglmeir J, Jin C, Yan S, Vanbeselaere J, Razzazi-Fazeli E, Wilson IB, Paschinger K "More than just oligomannose: an N-glycomic comparison of Penicillium species" -
Molecular and Cellular Proteomics 15(1) (2016) 73-92
N-glycosylation is an essential set of post-translational modifications of proteins; in the case of filamentous fungi, N-glycans are present on a range of secreted and cell wall proteins. In this study, we have compared the glycans released by peptide/N-glycosidase F from proteolysed cell pellets of three Penicillium species (P. dierckxii, P. nordicum and P. verrucosum that all belong to the Eurotiomycetes). Although the major structures are all within the range Hex(5-11)HexNAc(2) as shown by mass spectrometry, variations in reversed-phase chromatograms and MS/MS fragmentation patterns are indicative of differences in the actual structure. Hydrofluoric acid and mannosidase treatments revealed that the oligomannosidic glycans were not only in part modified with phosphoethanolamine residues and outer chain och1-dependent mannosylation, but that bisecting galactofuranose was present in a species-dependent manner. These data are the first to specifically show the modification of N-glycans in fungi with zwitterionic moieties. Furthermore, our results indicate that mere mass spectrometric screening is insufficient to reveal the subtly complex nature of N-glycosylation even within a single fungal genus.
mass spectrometry, N-glycan, Penicillium
NCBI PubMed ID: 26515459Publication DOI: 10.1074/mcp.M115.055061Journal NLM ID: 101125647Publisher: Bethesda, MD: ASBMB
Correspondence: Paschinger K
Institutions: Department für Chemie, Universität für Bodenkultur, Wien, Austria, Institutionen för Biomedicin, Göteborgs universitet, Göteborg, Sweden, VetOMICS Core Facility, Veterinärmedizinische Universität, Wien, Austria
Methods: HF hydrolysis, MALDI-TOF MS/MS, fluorescent labeling with 2-aminopyridine, PR-HPLC
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9. Compound ID: 22078
|
a-D-Manp-(1-2)-a-D-Manp-(1-6)-+
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a-D-Manp-(1-2)-a-D-Manp-(1-3)-a-D-Manp-(1-6)-+
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D-Galf-(1-2)-+ a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ |
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{{{-a-D-Manp-(1-6)-}}}/n=5/-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc |
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Structure type: oligomer
Compound class: N-glycan
Contained glycoepitopes: IEDB_123886,IEDB_130701,IEDB_135813,IEDB_136095,IEDB_136104,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140116,IEDB_140942,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_143632,IEDB_144983,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153220,IEDB_153762,IEDB_153763,IEDB_164046,IEDB_164174,IEDB_187201,IEDB_187238,IEDB_187239,IEDB_187240,IEDB_190606,IEDB_429156,IEDB_540671,IEDB_548907,IEDB_76933,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_33,SB_44,SB_53,SB_67,SB_72,SB_73,SB_74,SB_77,SB_85
The structure is contained in the following publication(s):
- Article ID: 8939
Kar B, Patel P, Ao J, Free SJ "Neurospora crassa family GH72 glucanosyltransferases function to crosslink cell wall glycoprotein N-linked galactomannan to cell wall lichenin" -
Fungal Genetics and Biology 123 (2019) 60-69
The formation of a glucan/chitin/glycoprotein cell wall matrix is vital for fungal survival, growth, and morphogenesis. The cell wall proteins are important cell wall components and function in adhesion, signal transduction, and as cell wall structural elements. In this report we demonstrate that Neurospora crassa GH72 glucan transferases function to crosslink cell wall glycoproteins into the cell wall. With an in vitro assay, we show that the glucan transferases are able to attach lichenin, a cell wall glucan with a repeating β-1,4-glucose-β-1,4-glucose-β-1,3-glucose structure, to cell wall glycoproteins. We propose that the pathway for attachment of lichenin to the glycoprotein has four steps. First, N-linked oligosaccharides present on the glycoproteins are modified by the addition of a galactomannan. As part of our report we have characterized the structure of the galactomannan, which consists of an α-1,6-mannose backbone with galactofuranose side chains. In the second step, the galactomannan is processed by members of the GH76 α-1,6-mannanases. In the third step, the glucan transferases cleave the lichenin and create substrate-enzyme intermediates. In the final step, the transferases transfer the lichenin to the processed galactomannan. We demonstrate that the N. crassa glucan transferases have demonstrate specificity for the processed galactomannan and for lichenin. The energy from the cleaved glycosidic bond in lichenin is retained in the substrate-enzyme intermediate and used to create a new glycosidic bond between the lichenin and the processed galactomannan. The pathway effectively crosslinks glycoproteins into the fungal cell wall.
oligosaccharide, cell wall, glycosyltransferase, N-linked glycosylation, fungi, Neurospora, protein cross-linking
NCBI PubMed ID: 30503329Publication DOI: 10.1016/j.fgb.2018.11.007Journal NLM ID: 9607601Publisher: Orlando, FL : Academic Press / Elsevier
Correspondence: free@buffalo.edu
Institutions: Department of Biological Sciences, SUNY University at Buffalo, Buffalo, NY, USA
Methods: GC-MS, SDS-PAGE, Western blotting, enzymatic digestion, gel immunoprecipitation, cell growth, MALDI-TOF/TOF MS, enzymatic assay, precipitation, centrifugation
- Article ID: 8948
Patel PK, Free SJ "The genetics and biochemistry of cell wall structure and synthesis in Neurospora crassa, a model filamentous fungus" -
Frontiers in Microbiology 10 (2019) ID 2294
This review discusses the wealth of information available for the N. crassa cell wall. The basic organization and structure of the cell wall is presented and how the wall changes during the N. crassa life cycle is discussed. Over forty cell wall glycoproteins have been identified by proteomic analyses. Genetic and biochemical studies have identified many of the key enzymes needed for cell wall biogenesis, and the roles these enzymes play in cell wall biogenesis are discussed. The review includes a discussion of how the major cell wall components (chitin, β-1,3-glucan, mixed β-1,3-/β-1,4- glucans, glycoproteins, and melanin) are synthesized and incorporated into the cell wall. We present a four-step model for how cell wall glycoproteins are covalently incorporated into the cell wall. In N. crassa, the covalent incorporation of cell wall glycoproteins into the wall occurs through a glycosidic linkage between lichenin (a mixed β-1,3-/β-1,4- glucan) and a "processed" galactomannan that has been attached to the glycoprotein N-linked oligosaccharides. The first step is the addition of the galactomannan to the N-linked oligosaccharide. Mutants affected in galactomannan formation are unable to incorporate glycoproteins into their cell walls. The second step is carried out by the enzymes from the GH76 family of α-1,6-mannanases, which cleave the galactomannan to generate a processed galactomannan. The model suggests that the third and fourth steps are carried out by members of the GH72 family of glucanosyltransferases. In the third step the glucanosyltransferases cleave lichenin and generate enzyme/substrate intermediates in which the lichenin is covalently attached to the active site of the glucanosyltransferases. In the final step, the glucanosyltransferases attach the lichenin onto the processed galactomannans, which creates new glycosidic bonds and effectively incorporates the glycoproteins into the cross-linked cell wall glucan/chitin matrix.
cell wall, Galactomannan, glucan, filamentous fungi, melanin, Neurospora, glucanosyltransferase, mannanase
NCBI PubMed ID: 31649638Publication DOI: 10.3389/fmicb.2019.02294Journal NLM ID: 101548977Publisher: Lausanne: Frontiers Research Foundation
Correspondence: free@buffalo.edu
Institutions: Department of Biological Sciences, SUNY University at Buffalo, Buffalo, NY, USA
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10. Compound ID: 23310
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a-D-Manp-(1-2)-a-D-Manp-(1-6)-+
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a-D-Manp-(1-2)-a-D-Manp-(1-3)-a-D-Manp-(1-6)-+
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D-Galf-(1-2)-+ |
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D-Galf-(1-2)-+ | |
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D-Galf-(1-2)-+ | | |
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D-Galf-(1-2)-+ | | | a-D-Manp-(1-2)-a-D-Manp-(1-2)-+ |
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D-Galf-(1-2)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-6)-a-D-Manp-(1-3)-b-D-Manp-(1-4)-b-D-GlcpNAc-(1-4)-b-D-GlcpNAc |
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Structure type: oligomer
Trivial name: N-linked oligosaccharide, galactomannan
Compound class: glycoprotein
Contained glycoepitopes: IEDB_123886,IEDB_130701,IEDB_135813,IEDB_136095,IEDB_136104,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140116,IEDB_140942,IEDB_141793,IEDB_141807,IEDB_141828,IEDB_141829,IEDB_141830,IEDB_141831,IEDB_143632,IEDB_144983,IEDB_151079,IEDB_151531,IEDB_152206,IEDB_153212,IEDB_153220,IEDB_153762,IEDB_153763,IEDB_164046,IEDB_164174,IEDB_187201,IEDB_187238,IEDB_187239,IEDB_187240,IEDB_190606,IEDB_429156,IEDB_540671,IEDB_548907,IEDB_76933,IEDB_857734,IEDB_983930,SB_136,SB_191,SB_196,SB_197,SB_198,SB_33,SB_44,SB_53,SB_67,SB_72,SB_73,SB_74,SB_77,SB_85
The structure is contained in the following publication(s):
- Article ID: 9553
Patel PK, Tung SK, Porfirio S, Sonon R, Azadi P, Free SJ "Extracellular targeting of Neurospora crassa cell wall and secreted glycoproteins by DFG-5" -
Fungal Genetics and Biology 160 (2022) 103686
The formation of a cell wall is vital for the survival and growth of a fungal cell. Fungi express members of the GH76 family of α-1,6-mannanases which play an important role in cell wall biogenesis. In this report we characterize the Neurospora crassa DFG-5 α-1,6-mannanase and demonstrate that it binds to the α-1,6-mannose backbone of an N-linked galactomannan found on cell wall glycoproteins. We show that DFG-5 has an enzymatic activity and provide evidence that it processes the α-1,6-mannose backbone of the N-linked galactomannan. Site-directed mutagenesis and complementation experiments show that D116 and D117 are located at the DFG-5 active site. D76 and E130, which are located in a groove on the opposite side of the protein, are also important for enzyme function. Cell wall glycoproteins co-purify with DFG-5 demonstrating a specific association between DFG-5 and cell wall glycoproteins. DFG-5 is able to discriminate between cell wall and secreted glycoproteins, and does not bind to the N-linked galactomannans present on secreted glycoproteins. DFG-5 plays a key role in targeting extracellular glycoproteins to their final destinations. By processing the galactomannans on cell wall proteins, DFG-5 targets them for cell wall incorporation by lichenin transferases. The N-linked galactomannans on secreted proteins are not processed by DFG-5, which targets these proteins for release into the extracellular medium.
Galactomannan, protein secretion, cell wall biosynthesis, DFG5, Extracellular protein targeting, GH76 α-1, 6-mannanase
NCBI PubMed ID: 35306147Publication DOI: 10.1016/j.fgb.2022.103686Journal NLM ID: 9607601Publisher: Orlando, FL : Academic Press / Elsevier
Correspondence: S.J. Free
Institutions: Complex Carbohydrate Research Center, University of Georgia, Athens, GA, USA, Department of Biological Sciences, SUNY University at Buffalo, Buffalo, NY, USA
Methods: PCR, Western blotting, MALDI-TOF MS, enzymatic digestion, cloning, enzymatic assay, complementation, site-directed mutagenesis, co-purification experiments
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11. Compound ID: 27538
Structure type: polymer chemical repeating unit
Contained glycoepitopes: IEDB_136095,IEDB_137472,IEDB_190606
The structure is contained in the following publication(s):
- Article ID: 11056
El-Sayed MM "An arabinogalactan from the seeds of Psidium guava" -
Carbohydrate Research 98 (1981) 209-212
Journal NLM ID: 0043535Publisher: Elsevier
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Total list of structure IDs on all result pages of the current query:
Total list of corresponding CSDB IDs (permanent record IDs):
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