PubMed:20439465 JSONTXT

{"project":"GlyCosmos600-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":1115,"end":1122},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"}],"text":"Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition.\nHuman immunodeficiency virus type 1 (HIV-1) entry is mediated by the interaction between a variably glycosylated envelope glycoprotein (gp120) and host-cell receptors. Approximately half of the molecular mass of gp120 is contributed by N-glycans, which serve as potential epitopes and may shield gp120 from immune recognition. The role of gp120 glycans in the host immune response to HIV-1 has not been comprehensively studied at the molecular level. We developed a new approach to characterize cell-specific gp120 glycosylation, the regulation of glycosylation, and the effect of variable glycosylation on antibody reactivity. A model oligomeric gp120 was expressed in different cell types, including cell lines that represent host-infected cells or cells used to produce gp120 for vaccination purposes. N-Glycosylation of gp120 varied, depending on the cell type used for its expression and the metabolic manipulation during expression. The resultant glycosylation included changes in the ratio of high-mannose to complex N-glycans, terminal decoration, and branching. Differential glycosylation of gp120 affected envelope recognition by polyclonal antibodies from the sera of HIV-1-infected subjects. These results indicate that gp120 glycans contribute to antibody reactivity and should be considered in HIV-1 vaccine design."}

{"project":"GlyCosmos600-CLO","denotations":[{"id":"T1","span":{"begin":71,"end":76},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":262,"end":266},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T3","span":{"begin":605,"end":609},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T4","span":{"begin":790,"end":800},"obj":"http://purl.obolibrary.org/obo/CL_0000000"},{"id":"T5","span":{"begin":812,"end":816},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T6","span":{"begin":852,"end":857},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T7","span":{"begin":861,"end":866},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T8","span":{"begin":965,"end":974},"obj":"http://purl.obolibrary.org/obo/CL_0000000"}],"text":"Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition.\nHuman immunodeficiency virus type 1 (HIV-1) entry is mediated by the interaction between a variably glycosylated envelope glycoprotein (gp120) and host-cell receptors. Approximately half of the molecular mass of gp120 is contributed by N-glycans, which serve as potential epitopes and may shield gp120 from immune recognition. The role of gp120 glycans in the host immune response to HIV-1 has not been comprehensively studied at the molecular level. We developed a new approach to characterize cell-specific gp120 glycosylation, the regulation of glycosylation, and the effect of variable glycosylation on antibody reactivity. A model oligomeric gp120 was expressed in different cell types, including cell lines that represent host-infected cells or cells used to produce gp120 for vaccination purposes. N-Glycosylation of gp120 varied, depending on the cell type used for its expression and the metabolic manipulation during expression. The resultant glycosylation included changes in the ratio of high-mannose to complex N-glycans, terminal decoration, and branching. Differential glycosylation of gp120 affected envelope recognition by polyclonal antibodies from the sera of HIV-1-infected subjects. These results indicate that gp120 glycans contribute to antibody reactivity and should be considered in HIV-1 vaccine design."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":1115,"end":1122},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"}],"text":"Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition.\nHuman immunodeficiency virus type 1 (HIV-1) entry is mediated by the interaction between a variably glycosylated envelope glycoprotein (gp120) and host-cell receptors. Approximately half of the molecular mass of gp120 is contributed by N-glycans, which serve as potential epitopes and may shield gp120 from immune recognition. The role of gp120 glycans in the host immune response to HIV-1 has not been comprehensively studied at the molecular level. We developed a new approach to characterize cell-specific gp120 glycosylation, the regulation of glycosylation, and the effect of variable glycosylation on antibody reactivity. A model oligomeric gp120 was expressed in different cell types, including cell lines that represent host-infected cells or cells used to produce gp120 for vaccination purposes. N-Glycosylation of gp120 varied, depending on the cell type used for its expression and the metabolic manipulation during expression. The resultant glycosylation included changes in the ratio of high-mannose to complex N-glycans, terminal decoration, and branching. Differential glycosylation of gp120 affected envelope recognition by polyclonal antibodies from the sera of HIV-1-infected subjects. These results indicate that gp120 glycans contribute to antibody reactivity and should be considered in HIV-1 vaccine design."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":1115,"end":1122},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"}],"text":"Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition.\nHuman immunodeficiency virus type 1 (HIV-1) entry is mediated by the interaction between a variably glycosylated envelope glycoprotein (gp120) and host-cell receptors. Approximately half of the molecular mass of gp120 is contributed by N-glycans, which serve as potential epitopes and may shield gp120 from immune recognition. The role of gp120 glycans in the host immune response to HIV-1 has not been comprehensively studied at the molecular level. We developed a new approach to characterize cell-specific gp120 glycosylation, the regulation of glycosylation, and the effect of variable glycosylation on antibody reactivity. A model oligomeric gp120 was expressed in different cell types, including cell lines that represent host-infected cells or cells used to produce gp120 for vaccination purposes. N-Glycosylation of gp120 varied, depending on the cell type used for its expression and the metabolic manipulation during expression. The resultant glycosylation included changes in the ratio of high-mannose to complex N-glycans, terminal decoration, and branching. Differential glycosylation of gp120 affected envelope recognition by polyclonal antibodies from the sera of HIV-1-infected subjects. These results indicate that gp120 glycans contribute to antibody reactivity and should be considered in HIV-1 vaccine design."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":109},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":110,"end":277},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":278,"end":436},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":437,"end":560},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":561,"end":737},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":738,"end":914},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":915,"end":1048},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1049,"end":1180},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1181,"end":1313},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1314,"end":1439},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":109},"obj":"Sentence"},{"id":"T2","span":{"begin":110,"end":277},"obj":"Sentence"},{"id":"T3","span":{"begin":278,"end":436},"obj":"Sentence"},{"id":"T4","span":{"begin":437,"end":560},"obj":"Sentence"},{"id":"T5","span":{"begin":561,"end":737},"obj":"Sentence"},{"id":"T6","span":{"begin":738,"end":914},"obj":"Sentence"},{"id":"T7","span":{"begin":915,"end":1048},"obj":"Sentence"},{"id":"T8","span":{"begin":1049,"end":1180},"obj":"Sentence"},{"id":"T9","span":{"begin":1181,"end":1313},"obj":"Sentence"},{"id":"T10","span":{"begin":1314,"end":1439},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition.\nHuman immunodeficiency virus type 1 (HIV-1) entry is mediated by the interaction between a variably glycosylated envelope glycoprotein (gp120) and host-cell receptors. Approximately half of the molecular mass of gp120 is contributed by N-glycans, which serve as potential epitopes and may shield gp120 from immune recognition. The role of gp120 glycans in the host immune response to HIV-1 has not been comprehensively studied at the molecular level. We developed a new approach to characterize cell-specific gp120 glycosylation, the regulation of glycosylation, and the effect of variable glycosylation on antibody reactivity. A model oligomeric gp120 was expressed in different cell types, including cell lines that represent host-infected cells or cells used to produce gp120 for vaccination purposes. N-Glycosylation of gp120 varied, depending on the cell type used for its expression and the metabolic manipulation during expression. The resultant glycosylation included changes in the ratio of high-mannose to complex N-glycans, terminal decoration, and branching. Differential glycosylation of gp120 affected envelope recognition by polyclonal antibodies from the sera of HIV-1-infected subjects. These results indicate that gp120 glycans contribute to antibody reactivity and should be considered in HIV-1 vaccine design."}

{"project":"DisGeNET","denotations":[{"id":"T0","span":{"begin":1211,"end":1216},"obj":"gene:3700"},{"id":"T1","span":{"begin":1289,"end":1292},"obj":"disease:C0019693"},{"id":"T2","span":{"begin":1342,"end":1347},"obj":"gene:3700"},{"id":"T3","span":{"begin":1418,"end":1421},"obj":"disease:C0019693"}],"relations":[{"id":"R1","pred":"associated_with","subj":"T0","obj":"T1"},{"id":"R2","pred":"associated_with","subj":"T2","obj":"T3"}],"namespaces":[{"prefix":"gene","uri":"http://www.ncbi.nlm.nih.gov/gene/"},{"prefix":"disease","uri":"http://purl.bioontology.org/ontology/MEDLINEPLUS/"}],"text":"Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition.\nHuman immunodeficiency virus type 1 (HIV-1) entry is mediated by the interaction between a variably glycosylated envelope glycoprotein (gp120) and host-cell receptors. Approximately half of the molecular mass of gp120 is contributed by N-glycans, which serve as potential epitopes and may shield gp120 from immune recognition. The role of gp120 glycans in the host immune response to HIV-1 has not been comprehensively studied at the molecular level. We developed a new approach to characterize cell-specific gp120 glycosylation, the regulation of glycosylation, and the effect of variable glycosylation on antibody reactivity. A model oligomeric gp120 was expressed in different cell types, including cell lines that represent host-infected cells or cells used to produce gp120 for vaccination purposes. N-Glycosylation of gp120 varied, depending on the cell type used for its expression and the metabolic manipulation during expression. The resultant glycosylation included changes in the ratio of high-mannose to complex N-glycans, terminal decoration, and branching. Differential glycosylation of gp120 affected envelope recognition by polyclonal antibodies from the sera of HIV-1-infected subjects. These results indicate that gp120 glycans contribute to antibody reactivity and should be considered in HIV-1 vaccine design."}

{"project":"PubmedHPO","denotations":[{"id":"T1","span":{"begin":116,"end":132},"obj":"HP_0002721"}],"text":"Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition.\nHuman immunodeficiency virus type 1 (HIV-1) entry is mediated by the interaction between a variably glycosylated envelope glycoprotein (gp120) and host-cell receptors. Approximately half of the molecular mass of gp120 is contributed by N-glycans, which serve as potential epitopes and may shield gp120 from immune recognition. The role of gp120 glycans in the host immune response to HIV-1 has not been comprehensively studied at the molecular level. We developed a new approach to characterize cell-specific gp120 glycosylation, the regulation of glycosylation, and the effect of variable glycosylation on antibody reactivity. A model oligomeric gp120 was expressed in different cell types, including cell lines that represent host-infected cells or cells used to produce gp120 for vaccination purposes. N-Glycosylation of gp120 varied, depending on the cell type used for its expression and the metabolic manipulation during expression. The resultant glycosylation included changes in the ratio of high-mannose to complex N-glycans, terminal decoration, and branching. Differential glycosylation of gp120 affected envelope recognition by polyclonal antibodies from the sera of HIV-1-infected subjects. These results indicate that gp120 glycans contribute to antibody reactivity and should be considered in HIV-1 vaccine design."}

{"project":"Allie","denotations":[{"id":"SS1_20439465_1_0","span":{"begin":110,"end":145},"obj":"expanded"},{"id":"SS2_20439465_1_0","span":{"begin":147,"end":152},"obj":"abbr"}],"relations":[{"id":"AE1_20439465_1_0","pred":"abbreviatedTo","subj":"SS1_20439465_1_0","obj":"SS2_20439465_1_0"}],"text":"Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition.\nHuman immunodeficiency virus type 1 (HIV-1) entry is mediated by the interaction between a variably glycosylated envelope glycoprotein (gp120) and host-cell receptors. Approximately half of the molecular mass of gp120 is contributed by N-glycans, which serve as potential epitopes and may shield gp120 from immune recognition. The role of gp120 glycans in the host immune response to HIV-1 has not been comprehensively studied at the molecular level. We developed a new approach to characterize cell-specific gp120 glycosylation, the regulation of glycosylation, and the effect of variable glycosylation on antibody reactivity. A model oligomeric gp120 was expressed in different cell types, including cell lines that represent host-infected cells or cells used to produce gp120 for vaccination purposes. N-Glycosylation of gp120 varied, depending on the cell type used for its expression and the metabolic manipulation during expression. The resultant glycosylation included changes in the ratio of high-mannose to complex N-glycans, terminal decoration, and branching. Differential glycosylation of gp120 affected envelope recognition by polyclonal antibodies from the sera of HIV-1-infected subjects. These results indicate that gp120 glycans contribute to antibody reactivity and should be considered in HIV-1 vaccine design."}

{"project":"DisGeNET5_gene_disease","denotations":[{"id":"20439465-1#113#134#gene64006","span":{"begin":223,"end":244},"obj":"gene64006"},{"id":"20439465-1#113#134#gene100616444","span":{"begin":223,"end":244},"obj":"gene100616444"},{"id":"20439465-1#113#134#gene30816","span":{"begin":223,"end":244},"obj":"gene30816"},{"id":"20439465-1#136#141#gene3700","span":{"begin":246,"end":251},"obj":"gene3700"},{"id":"20439465-1#0#28#diseaseC3854222","span":{"begin":110,"end":138},"obj":"diseaseC3854222"}],"relations":[{"id":"113#134#gene640060#28#diseaseC3854222","pred":"associated_with","subj":"20439465-1#113#134#gene64006","obj":"20439465-1#0#28#diseaseC3854222"},{"id":"113#134#gene1006164440#28#diseaseC3854222","pred":"associated_with","subj":"20439465-1#113#134#gene100616444","obj":"20439465-1#0#28#diseaseC3854222"},{"id":"113#134#gene308160#28#diseaseC3854222","pred":"associated_with","subj":"20439465-1#113#134#gene30816","obj":"20439465-1#0#28#diseaseC3854222"},{"id":"136#141#gene37000#28#diseaseC3854222","pred":"associated_with","subj":"20439465-1#136#141#gene3700","obj":"20439465-1#0#28#diseaseC3854222"}],"text":"Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition.\nHuman immunodeficiency virus type 1 (HIV-1) entry is mediated by the interaction between a variably glycosylated envelope glycoprotein (gp120) and host-cell receptors. Approximately half of the molecular mass of gp120 is contributed by N-glycans, which serve as potential epitopes and may shield gp120 from immune recognition. The role of gp120 glycans in the host immune response to HIV-1 has not been comprehensively studied at the molecular level. We developed a new approach to characterize cell-specific gp120 glycosylation, the regulation of glycosylation, and the effect of variable glycosylation on antibody reactivity. A model oligomeric gp120 was expressed in different cell types, including cell lines that represent host-infected cells or cells used to produce gp120 for vaccination purposes. N-Glycosylation of gp120 varied, depending on the cell type used for its expression and the metabolic manipulation during expression. The resultant glycosylation included changes in the ratio of high-mannose to complex N-glycans, terminal decoration, and branching. Differential glycosylation of gp120 affected envelope recognition by polyclonal antibodies from the sera of HIV-1-infected subjects. These results indicate that gp120 glycans contribute to antibody reactivity and should be considered in HIV-1 vaccine design."}

{"project":"glycosmos-test-glycan-structure","denotations":[{"id":"PD-GlycanStructures-B_T1","span":{"begin":1115,"end":1122},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"}],"text":"Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition.\nHuman immunodeficiency virus type 1 (HIV-1) entry is mediated by the interaction between a variably glycosylated envelope glycoprotein (gp120) and host-cell receptors. Approximately half of the molecular mass of gp120 is contributed by N-glycans, which serve as potential epitopes and may shield gp120 from immune recognition. The role of gp120 glycans in the host immune response to HIV-1 has not been comprehensively studied at the molecular level. We developed a new approach to characterize cell-specific gp120 glycosylation, the regulation of glycosylation, and the effect of variable glycosylation on antibody reactivity. A model oligomeric gp120 was expressed in different cell types, including cell lines that represent host-infected cells or cells used to produce gp120 for vaccination purposes. N-Glycosylation of gp120 varied, depending on the cell type used for its expression and the metabolic manipulation during expression. The resultant glycosylation included changes in the ratio of high-mannose to complex N-glycans, terminal decoration, and branching. Differential glycosylation of gp120 affected envelope recognition by polyclonal antibodies from the sera of HIV-1-infected subjects. These results indicate that gp120 glycans contribute to antibody reactivity and should be considered in HIV-1 vaccine design."}

{"project":"glycosmos-test-structure-v1","denotations":[{"id":"PD-GlycanStructures-B_T1","span":{"begin":1115,"end":1122},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"}],"text":"Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition.\nHuman immunodeficiency virus type 1 (HIV-1) entry is mediated by the interaction between a variably glycosylated envelope glycoprotein (gp120) and host-cell receptors. Approximately half of the molecular mass of gp120 is contributed by N-glycans, which serve as potential epitopes and may shield gp120 from immune recognition. The role of gp120 glycans in the host immune response to HIV-1 has not been comprehensively studied at the molecular level. We developed a new approach to characterize cell-specific gp120 glycosylation, the regulation of glycosylation, and the effect of variable glycosylation on antibody reactivity. A model oligomeric gp120 was expressed in different cell types, including cell lines that represent host-infected cells or cells used to produce gp120 for vaccination purposes. N-Glycosylation of gp120 varied, depending on the cell type used for its expression and the metabolic manipulation during expression. The resultant glycosylation included changes in the ratio of high-mannose to complex N-glycans, terminal decoration, and branching. Differential glycosylation of gp120 affected envelope recognition by polyclonal antibodies from the sera of HIV-1-infected subjects. These results indicate that gp120 glycans contribute to antibody reactivity and should be considered in HIV-1 vaccine design."}

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patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition.\nHuman immunodeficiency virus type 1 (HIV-1) entry is mediated by the interaction between a variably glycosylated envelope glycoprotein (gp120) and host-cell receptors. Approximately half of the molecular mass of gp120 is contributed by N-glycans, which serve as potential epitopes and may shield gp120 from immune recognition. The role of gp120 glycans in the host immune response to HIV-1 has not been comprehensively studied at the molecular level. We developed a new approach to characterize cell-specific gp120 glycosylation, the regulation of glycosylation, and the effect of variable glycosylation on antibody reactivity. A model oligomeric gp120 was expressed in different cell types, including cell lines that represent host-infected cells or cells used to produce gp120 for vaccination purposes. N-Glycosylation of gp120 varied, depending on the cell type used for its expression and the metabolic manipulation during expression. The resultant glycosylation included changes in the ratio of high-mannose to complex N-glycans, terminal decoration, and branching. Differential glycosylation of gp120 affected envelope recognition by polyclonal antibodies from the sera of HIV-1-infected subjects. These results indicate that gp120 glycans contribute to antibody reactivity and should be considered in HIV-1 vaccine design."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":116,"end":132},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0021094"}],"text":"Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition.\nHuman immunodeficiency virus type 1 (HIV-1) entry is mediated by the interaction between a variably glycosylated envelope glycoprotein (gp120) and host-cell receptors. Approximately half of the molecular mass of gp120 is contributed by N-glycans, which serve as potential epitopes and may shield gp120 from immune recognition. The role of gp120 glycans in the host immune response to HIV-1 has not been comprehensively studied at the molecular level. We developed a new approach to characterize cell-specific gp120 glycosylation, the regulation of glycosylation, and the effect of variable glycosylation on antibody reactivity. A model oligomeric gp120 was expressed in different cell types, including cell lines that represent host-infected cells or cells used to produce gp120 for vaccination purposes. N-Glycosylation of gp120 varied, depending on the cell type used for its expression and the metabolic manipulation during expression. The resultant glycosylation included changes in the ratio of high-mannose to complex N-glycans, terminal decoration, and branching. Differential glycosylation of gp120 affected envelope recognition by polyclonal antibodies from the sera of HIV-1-infected subjects. These results indicate that gp120 glycans contribute to antibody reactivity and should be considered in HIV-1 vaccine design."}

{"project":"HP-phenotype","denotations":[{"id":"T1","span":{"begin":116,"end":132},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0002721"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition.\nHuman immunodeficiency virus type 1 (HIV-1) entry is mediated by the interaction between a variably glycosylated envelope glycoprotein (gp120) and host-cell receptors. Approximately half of the molecular mass of gp120 is contributed by N-glycans, which serve as potential epitopes and may shield gp120 from immune recognition. The role of gp120 glycans in the host immune response to HIV-1 has not been comprehensively studied at the molecular level. We developed a new approach to characterize cell-specific gp120 glycosylation, the regulation of glycosylation, and the effect of variable glycosylation on antibody reactivity. A model oligomeric gp120 was expressed in different cell types, including cell lines that represent host-infected cells or cells used to produce gp120 for vaccination purposes. N-Glycosylation of gp120 varied, depending on the cell type used for its expression and the metabolic manipulation during expression. The resultant glycosylation included changes in the ratio of high-mannose to complex N-glycans, terminal decoration, and branching. Differential glycosylation of gp120 affected envelope recognition by polyclonal antibodies from the sera of HIV-1-infected subjects. These results indicate that gp120 glycans contribute to antibody reactivity and should be considered in HIV-1 vaccine design."}

{"project":"GlyCosmos600-FMA","denotations":[{"id":"T1","span":{"begin":26,"end":29},"obj":"Body_part"},{"id":"T2","span":{"begin":71,"end":76},"obj":"Body_part"},{"id":"T3","span":{"begin":88,"end":96},"obj":"Body_part"},{"id":"T4","span":{"begin":147,"end":150},"obj":"Body_part"},{"id":"T5","span":{"begin":232,"end":244},"obj":"Body_part"},{"id":"T6","span":{"begin":262,"end":266},"obj":"Body_part"},{"id":"T7","span":{"begin":494,"end":497},"obj":"Body_part"},{"id":"T8","span":{"begin":605,"end":609},"obj":"Body_part"},{"id":"T9","span":{"begin":717,"end":725},"obj":"Body_part"},{"id":"T10","span":{"begin":790,"end":794},"obj":"Body_part"},{"id":"T11","span":{"begin":812,"end":816},"obj":"Body_part"},{"id":"T12","span":{"begin":852,"end":857},"obj":"Body_part"},{"id":"T13","span":{"begin":861,"end":866},"obj":"Body_part"},{"id":"T14","span":{"begin":965,"end":969},"obj":"Body_part"},{"id":"T15","span":{"begin":1115,"end":1122},"obj":"Body_part"},{"id":"T16","span":{"begin":1289,"end":1292},"obj":"Body_part"},{"id":"T17","span":{"begin":1370,"end":1378},"obj":"Body_part"},{"id":"T18","span":{"begin":1418,"end":1421},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"fma_id","subj":"T1","obj":"http://purl.org/sig/ont/fma/fma278683"},{"id":"A2","pred":"fma_id","subj":"T2","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A3","pred":"fma_id","subj":"T3","obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"A4","pred":"fma_id","subj":"T4","obj":"http://purl.org/sig/ont/fma/fma278683"},{"id":"A5","pred":"fma_id","subj":"T5","obj":"http://purl.org/sig/ont/fma/fma62925"},{"id":"A6","pred":"fma_id","subj":"T6","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A7","pred":"fma_id","subj":"T7","obj":"http://purl.org/sig/ont/fma/fma278683"},{"id":"A8","pred":"fma_id","subj":"T8","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A9","pred":"fma_id","subj":"T9","obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"A10","pred":"fma_id","subj":"T10","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A11","pred":"fma_id","subj":"T11","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A12","pred":"fma_id","subj":"T12","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A13","pred":"fma_id","subj":"T13","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A14","pred":"fma_id","subj":"T14","obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"A15","pred":"fma_id","subj":"T15","obj":"http://purl.org/sig/ont/fma/fma82801"},{"id":"A16","pred":"fma_id","subj":"T16","obj":"http://purl.org/sig/ont/fma/fma278683"},{"id":"A17","pred":"fma_id","subj":"T17","obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"A18","pred":"fma_id","subj":"T18","obj":"http://purl.org/sig/ont/fma/fma278683"}],"text":"Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition.\nHuman immunodeficiency virus type 1 (HIV-1) entry is mediated by the interaction between a variably glycosylated envelope glycoprotein (gp120) and host-cell receptors. Approximately half of the molecular mass of gp120 is contributed by N-glycans, which serve as potential epitopes and may shield gp120 from immune recognition. The role of gp120 glycans in the host immune response to HIV-1 has not been comprehensively studied at the molecular level. We developed a new approach to characterize cell-specific gp120 glycosylation, the regulation of glycosylation, and the effect of variable glycosylation on antibody reactivity. A model oligomeric gp120 was expressed in different cell types, including cell lines that represent host-infected cells or cells used to produce gp120 for vaccination purposes. N-Glycosylation of gp120 varied, depending on the cell type used for its expression and the metabolic manipulation during expression. The resultant glycosylation included changes in the ratio of high-mannose to complex N-glycans, terminal decoration, and branching. Differential glycosylation of gp120 affected envelope recognition by polyclonal antibodies from the sera of HIV-1-infected subjects. These results indicate that gp120 glycans contribute to antibody reactivity and should be considered in HIV-1 vaccine design."}

{"project":"Lectin-Jamboree-Sentence","blocks":[{"id":"T1","span":{"begin":0,"end":109},"obj":"Sentence"},{"id":"T2","span":{"begin":110,"end":277},"obj":"Sentence"},{"id":"T3","span":{"begin":278,"end":436},"obj":"Sentence"},{"id":"T4","span":{"begin":437,"end":560},"obj":"Sentence"},{"id":"T5","span":{"begin":561,"end":737},"obj":"Sentence"},{"id":"T6","span":{"begin":738,"end":914},"obj":"Sentence"},{"id":"T7","span":{"begin":915,"end":1048},"obj":"Sentence"},{"id":"T8","span":{"begin":1049,"end":1180},"obj":"Sentence"},{"id":"T9","span":{"begin":1181,"end":1313},"obj":"Sentence"},{"id":"T10","span":{"begin":1314,"end":1439},"obj":"Sentence"}],"text":"Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition.\nHuman immunodeficiency virus type 1 (HIV-1) entry is mediated by the interaction between a variably glycosylated envelope glycoprotein (gp120) and host-cell receptors. Approximately half of the molecular mass of gp120 is contributed by N-glycans, which serve as potential epitopes and may shield gp120 from immune recognition. The role of gp120 glycans in the host immune response to HIV-1 has not been comprehensively studied at the molecular level. We developed a new approach to characterize cell-specific gp120 glycosylation, the regulation of glycosylation, and the effect of variable glycosylation on antibody reactivity. A model oligomeric gp120 was expressed in different cell types, including cell lines that represent host-infected cells or cells used to produce gp120 for vaccination purposes. N-Glycosylation of gp120 varied, depending on the cell type used for its expression and the metabolic manipulation during expression. The resultant glycosylation included changes in the ratio of high-mannose to complex N-glycans, terminal decoration, and branching. Differential glycosylation of gp120 affected envelope recognition by polyclonal antibodies from the sera of HIV-1-infected subjects. These results indicate that gp120 glycans contribute to antibody reactivity and should be considered in HIV-1 vaccine design."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":110,"end":145},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"11676"}],"text":"Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition.\nHuman immunodeficiency virus type 1 (HIV-1) entry is mediated by the interaction between a variably glycosylated envelope glycoprotein (gp120) and host-cell receptors. Approximately half of the molecular mass of gp120 is contributed by N-glycans, which serve as potential epitopes and may shield gp120 from immune recognition. The role of gp120 glycans in the host immune response to HIV-1 has not been comprehensively studied at the molecular level. We developed a new approach to characterize cell-specific gp120 glycosylation, the regulation of glycosylation, and the effect of variable glycosylation on antibody reactivity. A model oligomeric gp120 was expressed in different cell types, including cell lines that represent host-infected cells or cells used to produce gp120 for vaccination purposes. N-Glycosylation of gp120 varied, depending on the cell type used for its expression and the metabolic manipulation during expression. The resultant glycosylation included changes in the ratio of high-mannose to complex N-glycans, terminal decoration, and branching. Differential glycosylation of gp120 affected envelope recognition by polyclonal antibodies from the sera of HIV-1-infected subjects. These results indicate that gp120 glycans contribute to antibody reactivity and should be considered in HIV-1 vaccine design."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":223,"end":231},"obj":"Body_part"},{"id":"T2","span":{"begin":399,"end":405},"obj":"Body_part"},{"id":"T3","span":{"begin":1226,"end":1234},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/GO_0031975"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0003062"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/GO_0031975"}],"text":"Glycosylation patterns of HIV-1 gp120 depend on the type of expressing cells and affect antibody recognition.\nHuman immunodeficiency virus type 1 (HIV-1) entry is mediated by the interaction between a variably glycosylated envelope glycoprotein (gp120) and host-cell receptors. Approximately half of the molecular mass of gp120 is contributed by N-glycans, which serve as potential epitopes and may shield gp120 from immune recognition. The role of gp120 glycans in the host immune response to HIV-1 has not been comprehensively studied at the molecular level. We developed a new approach to characterize cell-specific gp120 glycosylation, the regulation of glycosylation, and the effect of variable glycosylation on antibody reactivity. A model oligomeric gp120 was expressed in different cell types, including cell lines that represent host-infected cells or cells used to produce gp120 for vaccination purposes. N-Glycosylation of gp120 varied, depending on the cell type used for its expression and the metabolic manipulation during expression. The resultant glycosylation included changes in the ratio of high-mannose to complex N-glycans, terminal decoration, and branching. Differential glycosylation of gp120 affected envelope recognition by polyclonal antibodies from the sera of HIV-1-infected subjects. These results indicate that gp120 glycans contribute to antibody reactivity and should be considered in HIV-1 vaccine design."}