PubMed:23580777 JSON TXT

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Glycan-Motif

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":0,"end":8},"obj":"https://glytoucan.org/Structures/Glycans/G49108TO"},{"id":"T2","span":{"begin":0,"end":8},"obj":"https://glytoucan.org/Structures/Glycans/G89565QL"},{"id":"T3","span":{"begin":311,"end":319},"obj":"https://glytoucan.org/Structures/Glycans/G49108TO"},{"id":"T4","span":{"begin":311,"end":319},"obj":"https://glytoucan.org/Structures/Glycans/G89565QL"},{"id":"T5","span":{"begin":366,"end":374},"obj":"https://glytoucan.org/Structures/Glycans/G49108TO"},{"id":"T6","span":{"begin":366,"end":374},"obj":"https://glytoucan.org/Structures/Glycans/G89565QL"},{"id":"T7","span":{"begin":1018,"end":1026},"obj":"https://glytoucan.org/Structures/Glycans/G49108TO"},{"id":"T8","span":{"begin":1018,"end":1026},"obj":"https://glytoucan.org/Structures/Glycans/G89565QL"},{"id":"T9","span":{"begin":1152,"end":1160},"obj":"https://glytoucan.org/Structures/Glycans/G49108TO"},{"id":"T10","span":{"begin":1152,"end":1160},"obj":"https://glytoucan.org/Structures/Glycans/G89565QL"},{"id":"T11","span":{"begin":1404,"end":1412},"obj":"https://glytoucan.org/Structures/Glycans/G49108TO"},{"id":"T12","span":{"begin":1404,"end":1412},"obj":"https://glytoucan.org/Structures/Glycans/G89565QL"},{"id":"T13","span":{"begin":1476,"end":1484},"obj":"https://glytoucan.org/Structures/Glycans/G49108TO"},{"id":"T14","span":{"begin":1476,"end":1484},"obj":"https://glytoucan.org/Structures/Glycans/G89565QL"}],"text":"O-GlcNAc transferase inhibits KSHV propagation and modifies replication relevant viral proteins as detected by systematic O-GlcNAcylation analysis.\nO-GlcNAcylation is an inducible, highly dynamic and reversible post-translational modification, mediated by a unique enzyme named O-linked N-acetyl-d-glucosamine (O-GlcNAc) transferase (OGT). In response to nutrients, O-GlcNAc levels are differentially regulated on many cellular proteins involved in gene expression, translation, immune reactions, protein degradation, protein-protein interaction, apoptosis and signal transduction. In contrast to eukaryotic cells, little is known about the role of O-GlcNAcylation in the viral life cycle. Here, we show that the overexpression of the OGT reduces the replication efficiency of Kaposi's sarcoma-associated herpesvirus (KSHV) in a dose-dependent manner. In order to investigate the global impact of O-GlcNAcylation in the KSHV life cycle, we systematically analyzed the 85 annotated KSHV-encoded open reading frames for O-GlcNAc modification. For this purpose, an immunoprecipitation (IP) strategy with three different approaches was carried out and the O-GlcNAc signal of the identified proteins was properly controlled for specificity. Out of the 85 KSHV-encoded proteins, 18 proteins were found to be direct targets for O-GlcNAcylation. Selected proteins were further confirmed by mass spectrometry for O-GlcNAc modification. Correlation of the functional annotation and the O-GlcNAc status of KSHV proteins showed that the predominant targets were proteins involved in viral DNA synthesis and replication. These results indicate that O-GlcNAcylation plays a major role in the regulation of KSHV propagation."}

GlyCosmos6-Glycan-Motif-Image

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":0,"end":8},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":311,"end":319},"obj":"Glycan_Motif"},{"id":"T5","span":{"begin":366,"end":374},"obj":"Glycan_Motif"},{"id":"T7","span":{"begin":1018,"end":1026},"obj":"Glycan_Motif"},{"id":"T9","span":{"begin":1152,"end":1160},"obj":"Glycan_Motif"},{"id":"T11","span":{"begin":1404,"end":1412},"obj":"Glycan_Motif"},{"id":"T13","span":{"begin":1476,"end":1484},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G89565QL"},{"id":"A2","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G49108TO"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G89565QL"},{"id":"A4","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G49108TO"},{"id":"A5","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G89565QL"},{"id":"A6","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G49108TO"},{"id":"A7","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G89565QL"},{"id":"A8","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G49108TO"},{"id":"A9","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G89565QL"},{"id":"A10","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G49108TO"},{"id":"A11","pred":"image","subj":"T11","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G89565QL"},{"id":"A12","pred":"image","subj":"T11","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G49108TO"},{"id":"A13","pred":"image","subj":"T13","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G89565QL"},{"id":"A14","pred":"image","subj":"T13","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G49108TO"}],"text":"O-GlcNAc transferase inhibits KSHV propagation and modifies replication relevant viral proteins as detected by systematic O-GlcNAcylation analysis.\nO-GlcNAcylation is an inducible, highly dynamic and reversible post-translational modification, mediated by a unique enzyme named O-linked N-acetyl-d-glucosamine (O-GlcNAc) transferase (OGT). In response to nutrients, O-GlcNAc levels are differentially regulated on many cellular proteins involved in gene expression, translation, immune reactions, protein degradation, protein-protein interaction, apoptosis and signal transduction. In contrast to eukaryotic cells, little is known about the role of O-GlcNAcylation in the viral life cycle. Here, we show that the overexpression of the OGT reduces the replication efficiency of Kaposi's sarcoma-associated herpesvirus (KSHV) in a dose-dependent manner. In order to investigate the global impact of O-GlcNAcylation in the KSHV life cycle, we systematically analyzed the 85 annotated KSHV-encoded open reading frames for O-GlcNAc modification. For this purpose, an immunoprecipitation (IP) strategy with three different approaches was carried out and the O-GlcNAc signal of the identified proteins was properly controlled for specificity. Out of the 85 KSHV-encoded proteins, 18 proteins were found to be direct targets for O-GlcNAcylation. Selected proteins were further confirmed by mass spectrometry for O-GlcNAc modification. Correlation of the functional annotation and the O-GlcNAc status of KSHV proteins showed that the predominant targets were proteins involved in viral DNA synthesis and replication. These results indicate that O-GlcNAcylation plays a major role in the regulation of KSHV propagation."}

sentences

GlyCosmos6-Glycan-Motif-Structure

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":0,"end":8},"obj":"https://glytoucan.org/Structures/Glycans/G49108TO"},{"id":"T2","span":{"begin":0,"end":8},"obj":"https://glytoucan.org/Structures/Glycans/G89565QL"},{"id":"T3","span":{"begin":311,"end":319},"obj":"https://glytoucan.org/Structures/Glycans/G49108TO"},{"id":"T4","span":{"begin":311,"end":319},"obj":"https://glytoucan.org/Structures/Glycans/G89565QL"},{"id":"T5","span":{"begin":366,"end":374},"obj":"https://glytoucan.org/Structures/Glycans/G49108TO"},{"id":"T6","span":{"begin":366,"end":374},"obj":"https://glytoucan.org/Structures/Glycans/G89565QL"},{"id":"T7","span":{"begin":1018,"end":1026},"obj":"https://glytoucan.org/Structures/Glycans/G49108TO"},{"id":"T8","span":{"begin":1018,"end":1026},"obj":"https://glytoucan.org/Structures/Glycans/G89565QL"},{"id":"T9","span":{"begin":1152,"end":1160},"obj":"https://glytoucan.org/Structures/Glycans/G49108TO"},{"id":"T10","span":{"begin":1152,"end":1160},"obj":"https://glytoucan.org/Structures/Glycans/G89565QL"},{"id":"T11","span":{"begin":1404,"end":1412},"obj":"https://glytoucan.org/Structures/Glycans/G49108TO"},{"id":"T12","span":{"begin":1404,"end":1412},"obj":"https://glytoucan.org/Structures/Glycans/G89565QL"},{"id":"T13","span":{"begin":1476,"end":1484},"obj":"https://glytoucan.org/Structures/Glycans/G49108TO"},{"id":"T14","span":{"begin":1476,"end":1484},"obj":"https://glytoucan.org/Structures/Glycans/G89565QL"}],"text":"O-GlcNAc transferase inhibits KSHV propagation and modifies replication relevant viral proteins as detected by systematic O-GlcNAcylation analysis.\nO-GlcNAcylation is an inducible, highly dynamic and reversible post-translational modification, mediated by a unique enzyme named O-linked N-acetyl-d-glucosamine (O-GlcNAc) transferase (OGT). In response to nutrients, O-GlcNAc levels are differentially regulated on many cellular proteins involved in gene expression, translation, immune reactions, protein degradation, protein-protein interaction, apoptosis and signal transduction. In contrast to eukaryotic cells, little is known about the role of O-GlcNAcylation in the viral life cycle. Here, we show that the overexpression of the OGT reduces the replication efficiency of Kaposi's sarcoma-associated herpesvirus (KSHV) in a dose-dependent manner. In order to investigate the global impact of O-GlcNAcylation in the KSHV life cycle, we systematically analyzed the 85 annotated KSHV-encoded open reading frames for O-GlcNAc modification. For this purpose, an immunoprecipitation (IP) strategy with three different approaches was carried out and the O-GlcNAc signal of the identified proteins was properly controlled for specificity. Out of the 85 KSHV-encoded proteins, 18 proteins were found to be direct targets for O-GlcNAcylation. Selected proteins were further confirmed by mass spectrometry for O-GlcNAc modification. Correlation of the functional annotation and the O-GlcNAc status of KSHV proteins showed that the predominant targets were proteins involved in viral DNA synthesis and replication. These results indicate that O-GlcNAcylation plays a major role in the regulation of KSHV propagation."}

Glycosmos6-GlycoEpitope

{"project":"Glycosmos6-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":0,"end":8},"obj":"http://www.glycoepitope.jp/epitopes/EP0004"},{"id":"T2","span":{"begin":311,"end":319},"obj":"http://www.glycoepitope.jp/epitopes/EP0004"},{"id":"T3","span":{"begin":366,"end":374},"obj":"http://www.glycoepitope.jp/epitopes/EP0004"},{"id":"T4","span":{"begin":1018,"end":1026},"obj":"http://www.glycoepitope.jp/epitopes/EP0004"},{"id":"T5","span":{"begin":1152,"end":1160},"obj":"http://www.glycoepitope.jp/epitopes/EP0004"},{"id":"T6","span":{"begin":1404,"end":1412},"obj":"http://www.glycoepitope.jp/epitopes/EP0004"},{"id":"T7","span":{"begin":1476,"end":1484},"obj":"http://www.glycoepitope.jp/epitopes/EP0004"}],"text":"O-GlcNAc transferase inhibits KSHV propagation and modifies replication relevant viral proteins as detected by systematic O-GlcNAcylation analysis.\nO-GlcNAcylation is an inducible, highly dynamic and reversible post-translational modification, mediated by a unique enzyme named O-linked N-acetyl-d-glucosamine (O-GlcNAc) transferase (OGT). In response to nutrients, O-GlcNAc levels are differentially regulated on many cellular proteins involved in gene expression, translation, immune reactions, protein degradation, protein-protein interaction, apoptosis and signal transduction. In contrast to eukaryotic cells, little is known about the role of O-GlcNAcylation in the viral life cycle. Here, we show that the overexpression of the OGT reduces the replication efficiency of Kaposi's sarcoma-associated herpesvirus (KSHV) in a dose-dependent manner. In order to investigate the global impact of O-GlcNAcylation in the KSHV life cycle, we systematically analyzed the 85 annotated KSHV-encoded open reading frames for O-GlcNAc modification. For this purpose, an immunoprecipitation (IP) strategy with three different approaches was carried out and the O-GlcNAc signal of the identified proteins was properly controlled for specificity. Out of the 85 KSHV-encoded proteins, 18 proteins were found to be direct targets for O-GlcNAcylation. Selected proteins were further confirmed by mass spectrometry for O-GlcNAc modification. Correlation of the functional annotation and the O-GlcNAc status of KSHV proteins showed that the predominant targets were proteins involved in viral DNA synthesis and replication. These results indicate that O-GlcNAcylation plays a major role in the regulation of KSHV propagation."}

GlyCosmos15-Glycan

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":0,"end":8},"obj":"Glycan"},{"id":"T2","span":{"begin":311,"end":319},"obj":"Glycan"},{"id":"T3","span":{"begin":366,"end":374},"obj":"Glycan"},{"id":"T4","span":{"begin":1018,"end":1026},"obj":"Glycan"},{"id":"T5","span":{"begin":1152,"end":1160},"obj":"Glycan"},{"id":"T6","span":{"begin":1404,"end":1412},"obj":"Glycan"},{"id":"T7","span":{"begin":1476,"end":1484},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G49108TO"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G49108TO"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G49108TO"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G49108TO"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G49108TO"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G49108TO"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"https://glycosmos.org/glycans/show/G49108TO"}],"text":"O-GlcNAc transferase inhibits KSHV propagation and modifies replication relevant viral proteins as detected by systematic O-GlcNAcylation analysis.\nO-GlcNAcylation is an inducible, highly dynamic and reversible post-translational modification, mediated by a unique enzyme named O-linked N-acetyl-d-glucosamine (O-GlcNAc) transferase (OGT). In response to nutrients, O-GlcNAc levels are differentially regulated on many cellular proteins involved in gene expression, translation, immune reactions, protein degradation, protein-protein interaction, apoptosis and signal transduction. In contrast to eukaryotic cells, little is known about the role of O-GlcNAcylation in the viral life cycle. Here, we show that the overexpression of the OGT reduces the replication efficiency of Kaposi's sarcoma-associated herpesvirus (KSHV) in a dose-dependent manner. In order to investigate the global impact of O-GlcNAcylation in the KSHV life cycle, we systematically analyzed the 85 annotated KSHV-encoded open reading frames for O-GlcNAc modification. For this purpose, an immunoprecipitation (IP) strategy with three different approaches was carried out and the O-GlcNAc signal of the identified proteins was properly controlled for specificity. Out of the 85 KSHV-encoded proteins, 18 proteins were found to be direct targets for O-GlcNAcylation. Selected proteins were further confirmed by mass spectrometry for O-GlcNAc modification. Correlation of the functional annotation and the O-GlcNAc status of KSHV proteins showed that the predominant targets were proteins involved in viral DNA synthesis and replication. These results indicate that O-GlcNAcylation plays a major role in the regulation of KSHV propagation."}

ICD10

{"project":"ICD10","denotations":[{"id":"T1","span":{"begin":777,"end":793},"obj":"http://purl.bioontology.org/ontology/ICD10/C46"},{"id":"T2","span":{"begin":777,"end":793},"obj":"http://purl.bioontology.org/ontology/ICD10/C46.9"}],"text":"O-GlcNAc transferase inhibits KSHV propagation and modifies replication relevant viral proteins as detected by systematic O-GlcNAcylation analysis.\nO-GlcNAcylation is an inducible, highly dynamic and reversible post-translational modification, mediated by a unique enzyme named O-linked N-acetyl-d-glucosamine (O-GlcNAc) transferase (OGT). In response to nutrients, O-GlcNAc levels are differentially regulated on many cellular proteins involved in gene expression, translation, immune reactions, protein degradation, protein-protein interaction, apoptosis and signal transduction. In contrast to eukaryotic cells, little is known about the role of O-GlcNAcylation in the viral life cycle. Here, we show that the overexpression of the OGT reduces the replication efficiency of Kaposi's sarcoma-associated herpesvirus (KSHV) in a dose-dependent manner. In order to investigate the global impact of O-GlcNAcylation in the KSHV life cycle, we systematically analyzed the 85 annotated KSHV-encoded open reading frames for O-GlcNAc modification. For this purpose, an immunoprecipitation (IP) strategy with three different approaches was carried out and the O-GlcNAc signal of the identified proteins was properly controlled for specificity. Out of the 85 KSHV-encoded proteins, 18 proteins were found to be direct targets for O-GlcNAcylation. Selected proteins were further confirmed by mass spectrometry for O-GlcNAc modification. Correlation of the functional annotation and the O-GlcNAc status of KSHV proteins showed that the predominant targets were proteins involved in viral DNA synthesis and replication. These results indicate that O-GlcNAcylation plays a major role in the regulation of KSHV propagation."}

GlycoBiology-FMA

uniprot-human

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":9,"end":20},"obj":"http://www.uniprot.org/uniprot/Q99484"},{"id":"T2","span":{"begin":321,"end":332},"obj":"http://www.uniprot.org/uniprot/Q99484"},{"id":"T3","span":{"begin":334,"end":337},"obj":"http://www.uniprot.org/uniprot/O15294"},{"id":"T4","span":{"begin":735,"end":738},"obj":"http://www.uniprot.org/uniprot/O15294"}],"text":"O-GlcNAc transferase inhibits KSHV propagation and modifies replication relevant viral proteins as detected by systematic O-GlcNAcylation analysis.\nO-GlcNAcylation is an inducible, highly dynamic and reversible post-translational modification, mediated by a unique enzyme named O-linked N-acetyl-d-glucosamine (O-GlcNAc) transferase (OGT). In response to nutrients, O-GlcNAc levels are differentially regulated on many cellular proteins involved in gene expression, translation, immune reactions, protein degradation, protein-protein interaction, apoptosis and signal transduction. In contrast to eukaryotic cells, little is known about the role of O-GlcNAcylation in the viral life cycle. Here, we show that the overexpression of the OGT reduces the replication efficiency of Kaposi's sarcoma-associated herpesvirus (KSHV) in a dose-dependent manner. In order to investigate the global impact of O-GlcNAcylation in the KSHV life cycle, we systematically analyzed the 85 annotated KSHV-encoded open reading frames for O-GlcNAc modification. For this purpose, an immunoprecipitation (IP) strategy with three different approaches was carried out and the O-GlcNAc signal of the identified proteins was properly controlled for specificity. Out of the 85 KSHV-encoded proteins, 18 proteins were found to be direct targets for O-GlcNAcylation. Selected proteins were further confirmed by mass spectrometry for O-GlcNAc modification. Correlation of the functional annotation and the O-GlcNAc status of KSHV proteins showed that the predominant targets were proteins involved in viral DNA synthesis and replication. These results indicate that O-GlcNAcylation plays a major role in the regulation of KSHV propagation."}

uniprot-mouse

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":9,"end":20},"obj":"http://www.uniprot.org/uniprot/P38649"},{"id":"T2","span":{"begin":321,"end":332},"obj":"http://www.uniprot.org/uniprot/P38649"},{"id":"T3","span":{"begin":334,"end":337},"obj":"http://www.uniprot.org/uniprot/Q8CGY8"},{"id":"T4","span":{"begin":735,"end":738},"obj":"http://www.uniprot.org/uniprot/Q8CGY8"}],"text":"O-GlcNAc transferase inhibits KSHV propagation and modifies replication relevant viral proteins as detected by systematic O-GlcNAcylation analysis.\nO-GlcNAcylation is an inducible, highly dynamic and reversible post-translational modification, mediated by a unique enzyme named O-linked N-acetyl-d-glucosamine (O-GlcNAc) transferase (OGT). In response to nutrients, O-GlcNAc levels are differentially regulated on many cellular proteins involved in gene expression, translation, immune reactions, protein degradation, protein-protein interaction, apoptosis and signal transduction. In contrast to eukaryotic cells, little is known about the role of O-GlcNAcylation in the viral life cycle. Here, we show that the overexpression of the OGT reduces the replication efficiency of Kaposi's sarcoma-associated herpesvirus (KSHV) in a dose-dependent manner. In order to investigate the global impact of O-GlcNAcylation in the KSHV life cycle, we systematically analyzed the 85 annotated KSHV-encoded open reading frames for O-GlcNAc modification. For this purpose, an immunoprecipitation (IP) strategy with three different approaches was carried out and the O-GlcNAc signal of the identified proteins was properly controlled for specificity. Out of the 85 KSHV-encoded proteins, 18 proteins were found to be direct targets for O-GlcNAcylation. Selected proteins were further confirmed by mass spectrometry for O-GlcNAc modification. Correlation of the functional annotation and the O-GlcNAc status of KSHV proteins showed that the predominant targets were proteins involved in viral DNA synthesis and replication. These results indicate that O-GlcNAcylation plays a major role in the regulation of KSHV propagation."}

GlycoBiology-NCBITAXON

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":414,"end":418},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/9973"},{"id":"T2","span":{"begin":518,"end":533},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/66543"},{"id":"T3","span":{"begin":518,"end":533},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/415014"},{"id":"T4","span":{"begin":518,"end":533},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/66322"},{"id":"T5","span":{"begin":597,"end":607},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/2759"},{"id":"T6","span":{"begin":608,"end":613},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T7","span":{"begin":786,"end":793},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/47206"},{"id":"T8","span":{"begin":1083,"end":1085},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/55979"}],"text":"O-GlcNAc transferase inhibits KSHV propagation and modifies replication relevant viral proteins as detected by systematic O-GlcNAcylation analysis.\nO-GlcNAcylation is an inducible, highly dynamic and reversible post-translational modification, mediated by a unique enzyme named O-linked N-acetyl-d-glucosamine (O-GlcNAc) transferase (OGT). In response to nutrients, O-GlcNAc levels are differentially regulated on many cellular proteins involved in gene expression, translation, immune reactions, protein degradation, protein-protein interaction, apoptosis and signal transduction. In contrast to eukaryotic cells, little is known about the role of O-GlcNAcylation in the viral life cycle. Here, we show that the overexpression of the OGT reduces the replication efficiency of Kaposi's sarcoma-associated herpesvirus (KSHV) in a dose-dependent manner. In order to investigate the global impact of O-GlcNAcylation in the KSHV life cycle, we systematically analyzed the 85 annotated KSHV-encoded open reading frames for O-GlcNAc modification. For this purpose, an immunoprecipitation (IP) strategy with three different approaches was carried out and the O-GlcNAc signal of the identified proteins was properly controlled for specificity. Out of the 85 KSHV-encoded proteins, 18 proteins were found to be direct targets for O-GlcNAcylation. Selected proteins were further confirmed by mass spectrometry for O-GlcNAc modification. Correlation of the functional annotation and the O-GlcNAc status of KSHV proteins showed that the predominant targets were proteins involved in viral DNA synthesis and replication. These results indicate that O-GlcNAcylation plays a major role in the regulation of KSHV propagation."}

GO-BP

GO-CC

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":311,"end":332},"obj":"http://purl.obolibrary.org/obo/GO_0017122"},{"id":"T2","span":{"begin":608,"end":613},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"O-GlcNAc transferase inhibits KSHV propagation and modifies replication relevant viral proteins as detected by systematic O-GlcNAcylation analysis.\nO-GlcNAcylation is an inducible, highly dynamic and reversible post-translational modification, mediated by a unique enzyme named O-linked N-acetyl-d-glucosamine (O-GlcNAc) transferase (OGT). In response to nutrients, O-GlcNAc levels are differentially regulated on many cellular proteins involved in gene expression, translation, immune reactions, protein degradation, protein-protein interaction, apoptosis and signal transduction. In contrast to eukaryotic cells, little is known about the role of O-GlcNAcylation in the viral life cycle. Here, we show that the overexpression of the OGT reduces the replication efficiency of Kaposi's sarcoma-associated herpesvirus (KSHV) in a dose-dependent manner. In order to investigate the global impact of O-GlcNAcylation in the KSHV life cycle, we systematically analyzed the 85 annotated KSHV-encoded open reading frames for O-GlcNAc modification. For this purpose, an immunoprecipitation (IP) strategy with three different approaches was carried out and the O-GlcNAc signal of the identified proteins was properly controlled for specificity. Out of the 85 KSHV-encoded proteins, 18 proteins were found to be direct targets for O-GlcNAcylation. Selected proteins were further confirmed by mass spectrometry for O-GlcNAc modification. Correlation of the functional annotation and the O-GlcNAc status of KSHV proteins showed that the predominant targets were proteins involved in viral DNA synthesis and replication. These results indicate that O-GlcNAcylation plays a major role in the regulation of KSHV propagation."}

EDAM-topics

EDAM-DFO

Allie

{"project":"Allie","denotations":[{"id":"SS1_23580777_1_0","span":{"begin":278,"end":309},"obj":"expanded"},{"id":"SS2_23580777_1_0","span":{"begin":311,"end":319},"obj":"abbr"},{"id":"SS1_23580777_4_0","span":{"begin":777,"end":816},"obj":"expanded"},{"id":"SS2_23580777_4_0","span":{"begin":818,"end":822},"obj":"abbr"},{"id":"SS1_23580777_6_0","span":{"begin":1062,"end":1081},"obj":"expanded"},{"id":"SS2_23580777_6_0","span":{"begin":1083,"end":1085},"obj":"abbr"}],"relations":[{"id":"AE1_23580777_1_0","pred":"abbreviatedTo","subj":"SS1_23580777_1_0","obj":"SS2_23580777_1_0"},{"id":"AE1_23580777_4_0","pred":"abbreviatedTo","subj":"SS1_23580777_4_0","obj":"SS2_23580777_4_0"},{"id":"AE1_23580777_6_0","pred":"abbreviatedTo","subj":"SS1_23580777_6_0","obj":"SS2_23580777_6_0"}],"text":"O-GlcNAc transferase inhibits KSHV propagation and modifies replication relevant viral proteins as detected by systematic O-GlcNAcylation analysis.\nO-GlcNAcylation is an inducible, highly dynamic and reversible post-translational modification, mediated by a unique enzyme named O-linked N-acetyl-d-glucosamine (O-GlcNAc) transferase (OGT). In response to nutrients, O-GlcNAc levels are differentially regulated on many cellular proteins involved in gene expression, translation, immune reactions, protein degradation, protein-protein interaction, apoptosis and signal transduction. In contrast to eukaryotic cells, little is known about the role of O-GlcNAcylation in the viral life cycle. Here, we show that the overexpression of the OGT reduces the replication efficiency of Kaposi's sarcoma-associated herpesvirus (KSHV) in a dose-dependent manner. In order to investigate the global impact of O-GlcNAcylation in the KSHV life cycle, we systematically analyzed the 85 annotated KSHV-encoded open reading frames for O-GlcNAc modification. For this purpose, an immunoprecipitation (IP) strategy with three different approaches was carried out and the O-GlcNAc signal of the identified proteins was properly controlled for specificity. Out of the 85 KSHV-encoded proteins, 18 proteins were found to be direct targets for O-GlcNAcylation. Selected proteins were further confirmed by mass spectrometry for O-GlcNAc modification. Correlation of the functional annotation and the O-GlcNAc status of KSHV proteins showed that the predominant targets were proteins involved in viral DNA synthesis and replication. These results indicate that O-GlcNAcylation plays a major role in the regulation of KSHV propagation."}

PubmedHPO

{"project":"PubmedHPO","denotations":[{"id":"T1","span":{"begin":777,"end":793},"obj":"HP_0100726"},{"id":"T2","span":{"begin":786,"end":793},"obj":"HP_0100242"}],"text":"O-GlcNAc transferase inhibits KSHV propagation and modifies replication relevant viral proteins as detected by systematic O-GlcNAcylation analysis.\nO-GlcNAcylation is an inducible, highly dynamic and reversible post-translational modification, mediated by a unique enzyme named O-linked N-acetyl-d-glucosamine (O-GlcNAc) transferase (OGT). In response to nutrients, O-GlcNAc levels are differentially regulated on many cellular proteins involved in gene expression, translation, immune reactions, protein degradation, protein-protein interaction, apoptosis and signal transduction. In contrast to eukaryotic cells, little is known about the role of O-GlcNAcylation in the viral life cycle. Here, we show that the overexpression of the OGT reduces the replication efficiency of Kaposi's sarcoma-associated herpesvirus (KSHV) in a dose-dependent manner. In order to investigate the global impact of O-GlcNAcylation in the KSHV life cycle, we systematically analyzed the 85 annotated KSHV-encoded open reading frames for O-GlcNAc modification. For this purpose, an immunoprecipitation (IP) strategy with three different approaches was carried out and the O-GlcNAc signal of the identified proteins was properly controlled for specificity. Out of the 85 KSHV-encoded proteins, 18 proteins were found to be direct targets for O-GlcNAcylation. Selected proteins were further confirmed by mass spectrometry for O-GlcNAc modification. Correlation of the functional annotation and the O-GlcNAc status of KSHV proteins showed that the predominant targets were proteins involved in viral DNA synthesis and replication. These results indicate that O-GlcNAcylation plays a major role in the regulation of KSHV propagation."}

NGLY1-deficiency

{"project":"NGLY1-deficiency","denotations":[{"id":"PD-NGLY1-deficiency-B_T1","span":{"begin":2,"end":8},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T2","span":{"begin":313,"end":319},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T3","span":{"begin":368,"end":374},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T4","span":{"begin":1020,"end":1026},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T5","span":{"begin":1154,"end":1160},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T6","span":{"begin":1406,"end":1412},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T7","span":{"begin":1478,"end":1484},"obj":"chem:24139"}],"namespaces":[{"prefix":"hgnc","uri":"https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:"},{"prefix":"omim","uri":"https://www.omim.org/entry/"},{"prefix":"chem","uri":"https://pubchem.ncbi.nlm.nih.gov/compound/"}],"text":"O-GlcNAc transferase inhibits KSHV propagation and modifies replication relevant viral proteins as detected by systematic O-GlcNAcylation analysis.\nO-GlcNAcylation is an inducible, highly dynamic and reversible post-translational modification, mediated by a unique enzyme named O-linked N-acetyl-d-glucosamine (O-GlcNAc) transferase (OGT). In response to nutrients, O-GlcNAc levels are differentially regulated on many cellular proteins involved in gene expression, translation, immune reactions, protein degradation, protein-protein interaction, apoptosis and signal transduction. In contrast to eukaryotic cells, little is known about the role of O-GlcNAcylation in the viral life cycle. Here, we show that the overexpression of the OGT reduces the replication efficiency of Kaposi's sarcoma-associated herpesvirus (KSHV) in a dose-dependent manner. In order to investigate the global impact of O-GlcNAcylation in the KSHV life cycle, we systematically analyzed the 85 annotated KSHV-encoded open reading frames for O-GlcNAc modification. For this purpose, an immunoprecipitation (IP) strategy with three different approaches was carried out and the O-GlcNAc signal of the identified proteins was properly controlled for specificity. Out of the 85 KSHV-encoded proteins, 18 proteins were found to be direct targets for O-GlcNAcylation. Selected proteins were further confirmed by mass spectrometry for O-GlcNAc modification. Correlation of the functional annotation and the O-GlcNAc status of KSHV proteins showed that the predominant targets were proteins involved in viral DNA synthesis and replication. These results indicate that O-GlcNAcylation plays a major role in the regulation of KSHV propagation."}

GlycoBiology-Epitope

{"project":"GlycoBiology-Epitope","denotations":[{"id":"PD-GlycoEpitope-B_T1","span":{"begin":0,"end":8},"obj":"http://www.glycoepitope.jp/epitopes/EP0004"},{"id":"PD-GlycoEpitope-B_T2","span":{"begin":311,"end":319},"obj":"http://www.glycoepitope.jp/epitopes/EP0004"},{"id":"PD-GlycoEpitope-B_T3","span":{"begin":366,"end":374},"obj":"http://www.glycoepitope.jp/epitopes/EP0004"},{"id":"PD-GlycoEpitope-B_T4","span":{"begin":1018,"end":1026},"obj":"http://www.glycoepitope.jp/epitopes/EP0004"},{"id":"PD-GlycoEpitope-B_T5","span":{"begin":1152,"end":1160},"obj":"http://www.glycoepitope.jp/epitopes/EP0004"},{"id":"PD-GlycoEpitope-B_T6","span":{"begin":1404,"end":1412},"obj":"http://www.glycoepitope.jp/epitopes/EP0004"},{"id":"PD-GlycoEpitope-B_T7","span":{"begin":1476,"end":1484},"obj":"http://www.glycoepitope.jp/epitopes/EP0004"}],"text":"O-GlcNAc transferase inhibits KSHV propagation and modifies replication relevant viral proteins as detected by systematic O-GlcNAcylation analysis.\nO-GlcNAcylation is an inducible, highly dynamic and reversible post-translational modification, mediated by a unique enzyme named O-linked N-acetyl-d-glucosamine (O-GlcNAc) transferase (OGT). In response to nutrients, O-GlcNAc levels are differentially regulated on many cellular proteins involved in gene expression, translation, immune reactions, protein degradation, protein-protein interaction, apoptosis and signal transduction. In contrast to eukaryotic cells, little is known about the role of O-GlcNAcylation in the viral life cycle. Here, we show that the overexpression of the OGT reduces the replication efficiency of Kaposi's sarcoma-associated herpesvirus (KSHV) in a dose-dependent manner. In order to investigate the global impact of O-GlcNAcylation in the KSHV life cycle, we systematically analyzed the 85 annotated KSHV-encoded open reading frames for O-GlcNAc modification. For this purpose, an immunoprecipitation (IP) strategy with three different approaches was carried out and the O-GlcNAc signal of the identified proteins was properly controlled for specificity. Out of the 85 KSHV-encoded proteins, 18 proteins were found to be direct targets for O-GlcNAcylation. Selected proteins were further confirmed by mass spectrometry for O-GlcNAc modification. Correlation of the functional annotation and the O-GlcNAc status of KSHV proteins showed that the predominant targets were proteins involved in viral DNA synthesis and replication. These results indicate that O-GlcNAcylation plays a major role in the regulation of KSHV propagation."}

GlyTouCan-IUPAC

mondo_disease

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":30,"end":34},"obj":"Disease"},{"id":"T2","span":{"begin":777,"end":823},"obj":"Disease"},{"id":"T3","span":{"begin":920,"end":924},"obj":"Disease"},{"id":"T4","span":{"begin":981,"end":985},"obj":"Disease"},{"id":"T5","span":{"begin":1250,"end":1254},"obj":"Disease"},{"id":"T6","span":{"begin":1495,"end":1499},"obj":"Disease"},{"id":"T7","span":{"begin":1692,"end":1696},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0005055"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0005055"},{"id":"A3","pred":"mondo_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MONDO_0005055"},{"id":"A4","pred":"mondo_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MONDO_0005055"},{"id":"A5","pred":"mondo_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MONDO_0005055"},{"id":"A6","pred":"mondo_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/MONDO_0005055"},{"id":"A7","pred":"mondo_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/MONDO_0005055"}],"text":"O-GlcNAc transferase inhibits KSHV propagation and modifies replication relevant viral proteins as detected by systematic O-GlcNAcylation analysis.\nO-GlcNAcylation is an inducible, highly dynamic and reversible post-translational modification, mediated by a unique enzyme named O-linked N-acetyl-d-glucosamine (O-GlcNAc) transferase (OGT). In response to nutrients, O-GlcNAc levels are differentially regulated on many cellular proteins involved in gene expression, translation, immune reactions, protein degradation, protein-protein interaction, apoptosis and signal transduction. In contrast to eukaryotic cells, little is known about the role of O-GlcNAcylation in the viral life cycle. Here, we show that the overexpression of the OGT reduces the replication efficiency of Kaposi's sarcoma-associated herpesvirus (KSHV) in a dose-dependent manner. In order to investigate the global impact of O-GlcNAcylation in the KSHV life cycle, we systematically analyzed the 85 annotated KSHV-encoded open reading frames for O-GlcNAc modification. For this purpose, an immunoprecipitation (IP) strategy with three different approaches was carried out and the O-GlcNAc signal of the identified proteins was properly controlled for specificity. Out of the 85 KSHV-encoded proteins, 18 proteins were found to be direct targets for O-GlcNAcylation. Selected proteins were further confirmed by mass spectrometry for O-GlcNAc modification. Correlation of the functional annotation and the O-GlcNAc status of KSHV proteins showed that the predominant targets were proteins involved in viral DNA synthesis and replication. These results indicate that O-GlcNAcylation plays a major role in the regulation of KSHV propagation."}

NCBITAXON

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":30,"end":34},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":777,"end":816},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":818,"end":822},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":920,"end":924},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":981,"end":985},"obj":"OrganismTaxon"},{"id":"T6","span":{"begin":1250,"end":1254},"obj":"OrganismTaxon"},{"id":"T7","span":{"begin":1495,"end":1499},"obj":"OrganismTaxon"},{"id":"T8","span":{"begin":1692,"end":1696},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"37296"},{"id":"A2","pred":"db_id","subj":"T2","obj":"37296"},{"id":"A3","pred":"db_id","subj":"T3","obj":"37296"},{"id":"A4","pred":"db_id","subj":"T4","obj":"37296"},{"id":"A5","pred":"db_id","subj":"T5","obj":"37296"},{"id":"A6","pred":"db_id","subj":"T6","obj":"37296"},{"id":"A7","pred":"db_id","subj":"T7","obj":"37296"},{"id":"A8","pred":"db_id","subj":"T8","obj":"37296"}],"text":"O-GlcNAc transferase inhibits KSHV propagation and modifies replication relevant viral proteins as detected by systematic O-GlcNAcylation analysis.\nO-GlcNAcylation is an inducible, highly dynamic and reversible post-translational modification, mediated by a unique enzyme named O-linked N-acetyl-d-glucosamine (O-GlcNAc) transferase (OGT). In response to nutrients, O-GlcNAc levels are differentially regulated on many cellular proteins involved in gene expression, translation, immune reactions, protein degradation, protein-protein interaction, apoptosis and signal transduction. In contrast to eukaryotic cells, little is known about the role of O-GlcNAcylation in the viral life cycle. Here, we show that the overexpression of the OGT reduces the replication efficiency of Kaposi's sarcoma-associated herpesvirus (KSHV) in a dose-dependent manner. In order to investigate the global impact of O-GlcNAcylation in the KSHV life cycle, we systematically analyzed the 85 annotated KSHV-encoded open reading frames for O-GlcNAc modification. For this purpose, an immunoprecipitation (IP) strategy with three different approaches was carried out and the O-GlcNAc signal of the identified proteins was properly controlled for specificity. Out of the 85 KSHV-encoded proteins, 18 proteins were found to be direct targets for O-GlcNAcylation. Selected proteins were further confirmed by mass spectrometry for O-GlcNAc modification. Correlation of the functional annotation and the O-GlcNAc status of KSHV proteins showed that the predominant targets were proteins involved in viral DNA synthesis and replication. These results indicate that O-GlcNAcylation plays a major role in the regulation of KSHV propagation."}

Glycosmos15-GlycoEpitope

{"project":"Glycosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":0,"end":8},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":311,"end":319},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":366,"end":374},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":1018,"end":1026},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T5","span":{"begin":1152,"end":1160},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T6","span":{"begin":1404,"end":1412},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T7","span":{"begin":1476,"end":1484},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0004"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0004"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0004"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/EP0004"},{"id":"A5","pred":"glycoepitope_id","subj":"T5","obj":"http://www.glycoepitope.jp/epitopes/EP0004"},{"id":"A6","pred":"glycoepitope_id","subj":"T6","obj":"http://www.glycoepitope.jp/epitopes/EP0004"},{"id":"A7","pred":"glycoepitope_id","subj":"T7","obj":"http://www.glycoepitope.jp/epitopes/EP0004"}],"text":"O-GlcNAc transferase inhibits KSHV propagation and modifies replication relevant viral proteins as detected by systematic O-GlcNAcylation analysis.\nO-GlcNAcylation is an inducible, highly dynamic and reversible post-translational modification, mediated by a unique enzyme named O-linked N-acetyl-d-glucosamine (O-GlcNAc) transferase (OGT). In response to nutrients, O-GlcNAc levels are differentially regulated on many cellular proteins involved in gene expression, translation, immune reactions, protein degradation, protein-protein interaction, apoptosis and signal transduction. In contrast to eukaryotic cells, little is known about the role of O-GlcNAcylation in the viral life cycle. Here, we show that the overexpression of the OGT reduces the replication efficiency of Kaposi's sarcoma-associated herpesvirus (KSHV) in a dose-dependent manner. In order to investigate the global impact of O-GlcNAcylation in the KSHV life cycle, we systematically analyzed the 85 annotated KSHV-encoded open reading frames for O-GlcNAc modification. For this purpose, an immunoprecipitation (IP) strategy with three different approaches was carried out and the O-GlcNAc signal of the identified proteins was properly controlled for specificity. Out of the 85 KSHV-encoded proteins, 18 proteins were found to be direct targets for O-GlcNAcylation. Selected proteins were further confirmed by mass spectrometry for O-GlcNAc modification. Correlation of the functional annotation and the O-GlcNAc status of KSHV proteins showed that the predominant targets were proteins involved in viral DNA synthesis and replication. These results indicate that O-GlcNAcylation plays a major role in the regulation of KSHV propagation."}

Anatomy-UBERON

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":597,"end":613},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL_0000255"}],"text":"O-GlcNAc transferase inhibits KSHV propagation and modifies replication relevant viral proteins as detected by systematic O-GlcNAcylation analysis.\nO-GlcNAcylation is an inducible, highly dynamic and reversible post-translational modification, mediated by a unique enzyme named O-linked N-acetyl-d-glucosamine (O-GlcNAc) transferase (OGT). In response to nutrients, O-GlcNAc levels are differentially regulated on many cellular proteins involved in gene expression, translation, immune reactions, protein degradation, protein-protein interaction, apoptosis and signal transduction. In contrast to eukaryotic cells, little is known about the role of O-GlcNAcylation in the viral life cycle. Here, we show that the overexpression of the OGT reduces the replication efficiency of Kaposi's sarcoma-associated herpesvirus (KSHV) in a dose-dependent manner. In order to investigate the global impact of O-GlcNAcylation in the KSHV life cycle, we systematically analyzed the 85 annotated KSHV-encoded open reading frames for O-GlcNAc modification. For this purpose, an immunoprecipitation (IP) strategy with three different approaches was carried out and the O-GlcNAc signal of the identified proteins was properly controlled for specificity. Out of the 85 KSHV-encoded proteins, 18 proteins were found to be direct targets for O-GlcNAcylation. Selected proteins were further confirmed by mass spectrometry for O-GlcNAc modification. Correlation of the functional annotation and the O-GlcNAc status of KSHV proteins showed that the predominant targets were proteins involved in viral DNA synthesis and replication. These results indicate that O-GlcNAcylation plays a major role in the regulation of KSHV propagation."}

GlyCosmos15-HP

{"project":"GlyCosmos15-HP","denotations":[{"id":"T1","span":{"begin":777,"end":793},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0100726"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"O-GlcNAc transferase inhibits KSHV propagation and modifies replication relevant viral proteins as detected by systematic O-GlcNAcylation analysis.\nO-GlcNAcylation is an inducible, highly dynamic and reversible post-translational modification, mediated by a unique enzyme named O-linked N-acetyl-d-glucosamine (O-GlcNAc) transferase (OGT). In response to nutrients, O-GlcNAc levels are differentially regulated on many cellular proteins involved in gene expression, translation, immune reactions, protein degradation, protein-protein interaction, apoptosis and signal transduction. In contrast to eukaryotic cells, little is known about the role of O-GlcNAcylation in the viral life cycle. Here, we show that the overexpression of the OGT reduces the replication efficiency of Kaposi's sarcoma-associated herpesvirus (KSHV) in a dose-dependent manner. In order to investigate the global impact of O-GlcNAcylation in the KSHV life cycle, we systematically analyzed the 85 annotated KSHV-encoded open reading frames for O-GlcNAc modification. For this purpose, an immunoprecipitation (IP) strategy with three different approaches was carried out and the O-GlcNAc signal of the identified proteins was properly controlled for specificity. Out of the 85 KSHV-encoded proteins, 18 proteins were found to be direct targets for O-GlcNAcylation. Selected proteins were further confirmed by mass spectrometry for O-GlcNAc modification. Correlation of the functional annotation and the O-GlcNAc status of KSHV proteins showed that the predominant targets were proteins involved in viral DNA synthesis and replication. These results indicate that O-GlcNAcylation plays a major role in the regulation of KSHV propagation."}

Glycosmos15-CL

{"project":"Glycosmos15-CL","denotations":[{"id":"T1","span":{"begin":597,"end":613},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0000255"}],"text":"O-GlcNAc transferase inhibits KSHV propagation and modifies replication relevant viral proteins as detected by systematic O-GlcNAcylation analysis.\nO-GlcNAcylation is an inducible, highly dynamic and reversible post-translational modification, mediated by a unique enzyme named O-linked N-acetyl-d-glucosamine (O-GlcNAc) transferase (OGT). In response to nutrients, O-GlcNAc levels are differentially regulated on many cellular proteins involved in gene expression, translation, immune reactions, protein degradation, protein-protein interaction, apoptosis and signal transduction. In contrast to eukaryotic cells, little is known about the role of O-GlcNAcylation in the viral life cycle. Here, we show that the overexpression of the OGT reduces the replication efficiency of Kaposi's sarcoma-associated herpesvirus (KSHV) in a dose-dependent manner. In order to investigate the global impact of O-GlcNAcylation in the KSHV life cycle, we systematically analyzed the 85 annotated KSHV-encoded open reading frames for O-GlcNAc modification. For this purpose, an immunoprecipitation (IP) strategy with three different approaches was carried out and the O-GlcNAc signal of the identified proteins was properly controlled for specificity. Out of the 85 KSHV-encoded proteins, 18 proteins were found to be direct targets for O-GlcNAcylation. Selected proteins were further confirmed by mass spectrometry for O-GlcNAc modification. Correlation of the functional annotation and the O-GlcNAc status of KSHV proteins showed that the predominant targets were proteins involved in viral DNA synthesis and replication. These results indicate that O-GlcNAcylation plays a major role in the regulation of KSHV propagation."}