PubMed:10089214 JSONTXT

{"project":"GlyCosmos6-UBERON","denotations":[{"id":"T1","span":{"begin":159,"end":166},"obj":"Body_part"},{"id":"T2","span":{"begin":822,"end":831},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0002416"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0001130"}],"text":"Differential expression of alpha2-6 sialylated polylactosamine structures by human B and T cells.\nWe found that human peripheral B and T cells differed in the surface expression of alpha2-6 sialylated type 2 chain glycans. In contrast to B cells, T cells expressed only sialoglycans with repeated N-acetyllactosamine (Galss1-4GlcNAc) disaccharides. This finding was based on the specificity of the monoclonal antibodies HB6, HB9 (CD24), HD66 (CDw76), FB21, and CRIS4 (CDw76) with the alpha2-6 sialylated model gangliosides IV6NeuAcnLc4Cer (2-6 SPG), VI6NeuAcnLc6Cer (2-6 SnHC), VIII6NeuAcnLc8Cer (2-6 SnOC), and X6NeuAcnLc10Cer (2-6 SnDC). We found that, in addition to their common requirement of an alpha2-6 bound terminal sialic acid for binding, the antibodies displayed preferences for the length of the carbohydrate backbones. Some of them bound mainly to 2-6 SPG with one N-acetyllactosamine (LacNAc) unit (HB9, HD66); others preferentially to 2-6 SnHC and 2-6 SnOC, with two and three LacNAc units, respectively (HB6 and FB21); and one of them exclusively to very polar alpha2-6 sialylated type 2 chain antigens (CRIS4) such as to 2-6 SnOC and even more polar gangliosides with three and more LacNAc units. These specificities could be correlated with the cellular binding of the antibodies as follows: whereas all antibodies bound to human CD 19 positive peripheral B cells, their reactivity with CD3 positive T cells was either nearly lacking (HD66, HB9), intermediate (about 65%: HB6, FB21) or strongly positive (CRIS4, 95%). Thus, the binding of the antibodies to 2-6 sialylated glycans with multiple lactosamine units appeared to determine their binding to T-cells."}

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":47,"end":62},"obj":"https://glytoucan.org/Structures/Glycans/G00058MO"},{"id":"T2","span":{"begin":297,"end":316},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T3","span":{"begin":725,"end":736},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T4","span":{"begin":879,"end":898},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"}],"text":"Differential expression of alpha2-6 sialylated polylactosamine structures by human B and T cells.\nWe found that human peripheral B and T cells differed in the surface expression of alpha2-6 sialylated type 2 chain glycans. In contrast to B cells, T cells expressed only sialoglycans with repeated N-acetyllactosamine (Galss1-4GlcNAc) disaccharides. This finding was based on the specificity of the monoclonal antibodies HB6, HB9 (CD24), HD66 (CDw76), FB21, and CRIS4 (CDw76) with the alpha2-6 sialylated model gangliosides IV6NeuAcnLc4Cer (2-6 SPG), VI6NeuAcnLc6Cer (2-6 SnHC), VIII6NeuAcnLc8Cer (2-6 SnOC), and X6NeuAcnLc10Cer (2-6 SnDC). We found that, in addition to their common requirement of an alpha2-6 bound terminal sialic acid for binding, the antibodies displayed preferences for the length of the carbohydrate backbones. Some of them bound mainly to 2-6 SPG with one N-acetyllactosamine (LacNAc) unit (HB9, HD66); others preferentially to 2-6 SnHC and 2-6 SnOC, with two and three LacNAc units, respectively (HB6 and FB21); and one of them exclusively to very polar alpha2-6 sialylated type 2 chain antigens (CRIS4) such as to 2-6 SnOC and even more polar gangliosides with three and more LacNAc units. These specificities could be correlated with the cellular binding of the antibodies as follows: whereas all antibodies bound to human CD 19 positive peripheral B cells, their reactivity with CD3 positive T cells was either nearly lacking (HD66, HB9), intermediate (about 65%: HB6, FB21) or strongly positive (CRIS4, 95%). Thus, the binding of the antibodies to 2-6 sialylated glycans with multiple lactosamine units appeared to determine their binding to T-cells."}

{"project":"GlyCosmos600-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":47,"end":62},"obj":"https://glytoucan.org/Structures/Glycans/G00058MO"},{"id":"T2","span":{"begin":297,"end":316},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T3","span":{"begin":725,"end":736},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T4","span":{"begin":879,"end":898},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"}],"text":"Differential expression of alpha2-6 sialylated polylactosamine structures by human B and T cells.\nWe found that human peripheral B and T cells differed in the surface expression of alpha2-6 sialylated type 2 chain glycans. In contrast to B cells, T cells expressed only sialoglycans with repeated N-acetyllactosamine (Galss1-4GlcNAc) disaccharides. This finding was based on the specificity of the monoclonal antibodies HB6, HB9 (CD24), HD66 (CDw76), FB21, and CRIS4 (CDw76) with the alpha2-6 sialylated model gangliosides IV6NeuAcnLc4Cer (2-6 SPG), VI6NeuAcnLc6Cer (2-6 SnHC), VIII6NeuAcnLc8Cer (2-6 SnOC), and X6NeuAcnLc10Cer (2-6 SnDC). We found that, in addition to their common requirement of an alpha2-6 bound terminal sialic acid for binding, the antibodies displayed preferences for the length of the carbohydrate backbones. Some of them bound mainly to 2-6 SPG with one N-acetyllactosamine (LacNAc) unit (HB9, HD66); others preferentially to 2-6 SnHC and 2-6 SnOC, with two and three LacNAc units, respectively (HB6 and FB21); and one of them exclusively to very polar alpha2-6 sialylated type 2 chain antigens (CRIS4) such as to 2-6 SnOC and even more polar gangliosides with three and more LacNAc units. These specificities could be correlated with the cellular binding of the antibodies as follows: whereas all antibodies bound to human CD 19 positive peripheral B cells, their reactivity with CD3 positive T cells was either nearly lacking (HD66, HB9), intermediate (about 65%: HB6, FB21) or strongly positive (CRIS4, 95%). Thus, the binding of the antibodies to 2-6 sialylated glycans with multiple lactosamine units appeared to determine their binding to T-cells."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":77,"end":82},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":112,"end":117},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":1343,"end":1348},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"NCBItxid:9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"NCBItxid:9606"},{"id":"A3","pred":"db_id","subj":"T3","obj":"NCBItxid:9606"}],"text":"Differential expression of alpha2-6 sialylated polylactosamine structures by human B and T cells.\nWe found that human peripheral B and T cells differed in the surface expression of alpha2-6 sialylated type 2 chain glycans. In contrast to B cells, T cells expressed only sialoglycans with repeated N-acetyllactosamine (Galss1-4GlcNAc) disaccharides. This finding was based on the specificity of the monoclonal antibodies HB6, HB9 (CD24), HD66 (CDw76), FB21, and CRIS4 (CDw76) with the alpha2-6 sialylated model gangliosides IV6NeuAcnLc4Cer (2-6 SPG), VI6NeuAcnLc6Cer (2-6 SnHC), VIII6NeuAcnLc8Cer (2-6 SnOC), and X6NeuAcnLc10Cer (2-6 SnDC). We found that, in addition to their common requirement of an alpha2-6 bound terminal sialic acid for binding, the antibodies displayed preferences for the length of the carbohydrate backbones. Some of them bound mainly to 2-6 SPG with one N-acetyllactosamine (LacNAc) unit (HB9, HD66); others preferentially to 2-6 SnHC and 2-6 SnOC, with two and three LacNAc units, respectively (HB6 and FB21); and one of them exclusively to very polar alpha2-6 sialylated type 2 chain antigens (CRIS4) such as to 2-6 SnOC and even more polar gangliosides with three and more LacNAc units. These specificities could be correlated with the cellular binding of the antibodies as follows: whereas all antibodies bound to human CD 19 positive peripheral B cells, their reactivity with CD3 positive T cells was either nearly lacking (HD66, HB9), intermediate (about 65%: HB6, FB21) or strongly positive (CRIS4, 95%). Thus, the binding of the antibodies to 2-6 sialylated glycans with multiple lactosamine units appeared to determine their binding to T-cells."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":47,"end":62},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":297,"end":316},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":725,"end":736},"obj":"Glycan_Motif"},{"id":"T4","span":{"begin":879,"end":898},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00058MO"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00055MO"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81533KY"},{"id":"A4","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00055MO"}],"text":"Differential expression of alpha2-6 sialylated polylactosamine structures by human B and T cells.\nWe found that human peripheral B and T cells differed in the surface expression of alpha2-6 sialylated type 2 chain glycans. In contrast to B cells, T cells expressed only sialoglycans with repeated N-acetyllactosamine (Galss1-4GlcNAc) disaccharides. This finding was based on the specificity of the monoclonal antibodies HB6, HB9 (CD24), HD66 (CDw76), FB21, and CRIS4 (CDw76) with the alpha2-6 sialylated model gangliosides IV6NeuAcnLc4Cer (2-6 SPG), VI6NeuAcnLc6Cer (2-6 SnHC), VIII6NeuAcnLc8Cer (2-6 SnOC), and X6NeuAcnLc10Cer (2-6 SnDC). We found that, in addition to their common requirement of an alpha2-6 bound terminal sialic acid for binding, the antibodies displayed preferences for the length of the carbohydrate backbones. Some of them bound mainly to 2-6 SPG with one N-acetyllactosamine (LacNAc) unit (HB9, HD66); others preferentially to 2-6 SnHC and 2-6 SnOC, with two and three LacNAc units, respectively (HB6 and FB21); and one of them exclusively to very polar alpha2-6 sialylated type 2 chain antigens (CRIS4) such as to 2-6 SnOC and even more polar gangliosides with three and more LacNAc units. These specificities could be correlated with the cellular binding of the antibodies as follows: whereas all antibodies bound to human CD 19 positive peripheral B cells, their reactivity with CD3 positive T cells was either nearly lacking (HD66, HB9), intermediate (about 65%: HB6, FB21) or strongly positive (CRIS4, 95%). Thus, the binding of the antibodies to 2-6 sialylated glycans with multiple lactosamine units appeared to determine their binding to T-cells."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":47,"end":62},"obj":"https://glytoucan.org/Structures/Glycans/G00058MO"},{"id":"T2","span":{"begin":297,"end":316},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"},{"id":"T3","span":{"begin":725,"end":736},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T4","span":{"begin":879,"end":898},"obj":"https://glytoucan.org/Structures/Glycans/G00055MO"}],"text":"Differential expression of alpha2-6 sialylated polylactosamine structures by human B and T cells.\nWe found that human peripheral B and T cells differed in the surface expression of alpha2-6 sialylated type 2 chain glycans. In contrast to B cells, T cells expressed only sialoglycans with repeated N-acetyllactosamine (Galss1-4GlcNAc) disaccharides. This finding was based on the specificity of the monoclonal antibodies HB6, HB9 (CD24), HD66 (CDw76), FB21, and CRIS4 (CDw76) with the alpha2-6 sialylated model gangliosides IV6NeuAcnLc4Cer (2-6 SPG), VI6NeuAcnLc6Cer (2-6 SnHC), VIII6NeuAcnLc8Cer (2-6 SnOC), and X6NeuAcnLc10Cer (2-6 SnDC). We found that, in addition to their common requirement of an alpha2-6 bound terminal sialic acid for binding, the antibodies displayed preferences for the length of the carbohydrate backbones. Some of them bound mainly to 2-6 SPG with one N-acetyllactosamine (LacNAc) unit (HB9, HD66); others preferentially to 2-6 SnHC and 2-6 SnOC, with two and three LacNAc units, respectively (HB6 and FB21); and one of them exclusively to very polar alpha2-6 sialylated type 2 chain antigens (CRIS4) such as to 2-6 SnOC and even more polar gangliosides with three and more LacNAc units. These specificities could be correlated with the cellular binding of the antibodies as follows: whereas all antibodies bound to human CD 19 positive peripheral B cells, their reactivity with CD3 positive T cells was either nearly lacking (HD66, HB9), intermediate (about 65%: HB6, FB21) or strongly positive (CRIS4, 95%). Thus, the binding of the antibodies to 2-6 sialylated glycans with multiple lactosamine units appeared to determine their binding to T-cells."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":97},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":98,"end":222},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":223,"end":348},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":349,"end":639},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":640,"end":832},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":833,"end":1214},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":1215,"end":1536},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":1537,"end":1678},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":97},"obj":"Sentence"},{"id":"T2","span":{"begin":98,"end":222},"obj":"Sentence"},{"id":"T3","span":{"begin":223,"end":348},"obj":"Sentence"},{"id":"T4","span":{"begin":349,"end":639},"obj":"Sentence"},{"id":"T5","span":{"begin":640,"end":832},"obj":"Sentence"},{"id":"T6","span":{"begin":833,"end":1214},"obj":"Sentence"},{"id":"T7","span":{"begin":1215,"end":1536},"obj":"Sentence"},{"id":"T8","span":{"begin":1537,"end":1678},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Differential expression of alpha2-6 sialylated polylactosamine structures by human B and T cells.\nWe found that human peripheral B and T cells differed in the surface expression of alpha2-6 sialylated type 2 chain glycans. In contrast to B cells, T cells expressed only sialoglycans with repeated N-acetyllactosamine (Galss1-4GlcNAc) disaccharides. This finding was based on the specificity of the monoclonal antibodies HB6, HB9 (CD24), HD66 (CDw76), FB21, and CRIS4 (CDw76) with the alpha2-6 sialylated model gangliosides IV6NeuAcnLc4Cer (2-6 SPG), VI6NeuAcnLc6Cer (2-6 SnHC), VIII6NeuAcnLc8Cer (2-6 SnOC), and X6NeuAcnLc10Cer (2-6 SnDC). We found that, in addition to their common requirement of an alpha2-6 bound terminal sialic acid for binding, the antibodies displayed preferences for the length of the carbohydrate backbones. Some of them bound mainly to 2-6 SPG with one N-acetyllactosamine (LacNAc) unit (HB9, HD66); others preferentially to 2-6 SnHC and 2-6 SnOC, with two and three LacNAc units, respectively (HB6 and FB21); and one of them exclusively to very polar alpha2-6 sialylated type 2 chain antigens (CRIS4) such as to 2-6 SnOC and even more polar gangliosides with three and more LacNAc units. These specificities could be correlated with the cellular binding of the antibodies as follows: whereas all antibodies bound to human CD 19 positive peripheral B cells, their reactivity with CD3 positive T cells was either nearly lacking (HD66, HB9), intermediate (about 65%: HB6, FB21) or strongly positive (CRIS4, 95%). Thus, the binding of the antibodies to 2-6 sialylated glycans with multiple lactosamine units appeared to determine their binding to T-cells."}

{"project":"GlyCosmos6-CLO","denotations":[{"id":"T1","span":{"begin":89,"end":96},"obj":"http://purl.obolibrary.org/obo/CL_0000084"},{"id":"T2","span":{"begin":91,"end":96},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T3","span":{"begin":135,"end":142},"obj":"http://purl.obolibrary.org/obo/CL_0000084"},{"id":"T4","span":{"begin":137,"end":142},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T5","span":{"begin":238,"end":245},"obj":"http://purl.obolibrary.org/obo/CL_0000236"},{"id":"T6","span":{"begin":240,"end":245},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T7","span":{"begin":247,"end":254},"obj":"http://purl.obolibrary.org/obo/CL_0000084"},{"id":"T8","span":{"begin":249,"end":254},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T9","span":{"begin":1349,"end":1354},"obj":"http://purl.obolibrary.org/obo/CLO_0053432"},{"id":"T10","span":{"begin":1375,"end":1382},"obj":"http://purl.obolibrary.org/obo/CL_0000236"},{"id":"T11","span":{"begin":1377,"end":1382},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T12","span":{"begin":1406,"end":1409},"obj":"http://purl.obolibrary.org/obo/CLO_0052882"},{"id":"T13","span":{"begin":1406,"end":1409},"obj":"http://purl.obolibrary.org/obo/CLO_0053434"},{"id":"T14","span":{"begin":1419,"end":1426},"obj":"http://purl.obolibrary.org/obo/CL_0000084"},{"id":"T15","span":{"begin":1421,"end":1426},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T16","span":{"begin":1670,"end":1677},"obj":"http://purl.obolibrary.org/obo/CL_0000084"},{"id":"T17","span":{"begin":1672,"end":1677},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"Differential expression of alpha2-6 sialylated polylactosamine structures by human B and T cells.\nWe found that human peripheral B and T cells differed in the surface expression of alpha2-6 sialylated type 2 chain glycans. In contrast to B cells, T cells expressed only sialoglycans with repeated N-acetyllactosamine (Galss1-4GlcNAc) disaccharides. This finding was based on the specificity of the monoclonal antibodies HB6, HB9 (CD24), HD66 (CDw76), FB21, and CRIS4 (CDw76) with the alpha2-6 sialylated model gangliosides IV6NeuAcnLc4Cer (2-6 SPG), VI6NeuAcnLc6Cer (2-6 SnHC), VIII6NeuAcnLc8Cer (2-6 SnOC), and X6NeuAcnLc10Cer (2-6 SnDC). We found that, in addition to their common requirement of an alpha2-6 bound terminal sialic acid for binding, the antibodies displayed preferences for the length of the carbohydrate backbones. Some of them bound mainly to 2-6 SPG with one N-acetyllactosamine (LacNAc) unit (HB9, HD66); others preferentially to 2-6 SnHC and 2-6 SnOC, with two and three LacNAc units, respectively (HB6 and FB21); and one of them exclusively to very polar alpha2-6 sialylated type 2 chain antigens (CRIS4) such as to 2-6 SnOC and even more polar gangliosides with three and more LacNAc units. These specificities could be correlated with the cellular binding of the antibodies as follows: whereas all antibodies bound to human CD 19 positive peripheral B cells, their reactivity with CD3 positive T cells was either nearly lacking (HD66, HB9), intermediate (about 65%: HB6, FB21) or strongly positive (CRIS4, 95%). Thus, the binding of the antibodies to 2-6 sialylated glycans with multiple lactosamine units appeared to determine their binding to T-cells."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":633,"end":637},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0014889"}],"text":"Differential expression of alpha2-6 sialylated polylactosamine structures by human B and T cells.\nWe found that human peripheral B and T cells differed in the surface expression of alpha2-6 sialylated type 2 chain glycans. In contrast to B cells, T cells expressed only sialoglycans with repeated N-acetyllactosamine (Galss1-4GlcNAc) disaccharides. This finding was based on the specificity of the monoclonal antibodies HB6, HB9 (CD24), HD66 (CDw76), FB21, and CRIS4 (CDw76) with the alpha2-6 sialylated model gangliosides IV6NeuAcnLc4Cer (2-6 SPG), VI6NeuAcnLc6Cer (2-6 SnHC), VIII6NeuAcnLc8Cer (2-6 SnOC), and X6NeuAcnLc10Cer (2-6 SnDC). We found that, in addition to their common requirement of an alpha2-6 bound terminal sialic acid for binding, the antibodies displayed preferences for the length of the carbohydrate backbones. Some of them bound mainly to 2-6 SPG with one N-acetyllactosamine (LacNAc) unit (HB9, HD66); others preferentially to 2-6 SnHC and 2-6 SnOC, with two and three LacNAc units, respectively (HB6 and FB21); and one of them exclusively to very polar alpha2-6 sialylated type 2 chain antigens (CRIS4) such as to 2-6 SnOC and even more polar gangliosides with three and more LacNAc units. These specificities could be correlated with the cellular binding of the antibodies as follows: whereas all antibodies bound to human CD 19 positive peripheral B cells, their reactivity with CD3 positive T cells was either nearly lacking (HD66, HB9), intermediate (about 65%: HB6, FB21) or strongly positive (CRIS4, 95%). Thus, the binding of the antibodies to 2-6 sialylated glycans with multiple lactosamine units appeared to determine their binding to T-cells."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":91,"end":96},"obj":"FMAID:68646"},{"id":"_T2","span":{"begin":91,"end":96},"obj":"FMAID:169002"},{"id":"_T3","span":{"begin":118,"end":128},"obj":"FMAID:222825"},{"id":"_T4","span":{"begin":118,"end":128},"obj":"FMAID:74552"},{"id":"_T5","span":{"begin":118,"end":128},"obj":"FMAID:179289"},{"id":"_T6","span":{"begin":137,"end":142},"obj":"FMAID:169002"},{"id":"_T7","span":{"begin":137,"end":142},"obj":"FMAID:68646"},{"id":"_T8","span":{"begin":159,"end":166},"obj":"FMAID:50594"},{"id":"_T9","span":{"begin":159,"end":166},"obj":"FMAID:146300"},{"id":"_T10","span":{"begin":240,"end":245},"obj":"FMAID:68646"},{"id":"_T11","span":{"begin":240,"end":245},"obj":"FMAID:169002"},{"id":"_T12","span":{"begin":249,"end":254},"obj":"FMAID:68646"},{"id":"_T13","span":{"begin":249,"end":254},"obj":"FMAID:169002"},{"id":"_T14","span":{"begin":297,"end":316},"obj":"FMAID:196780"},{"id":"_T15","span":{"begin":297,"end":316},"obj":"FMAID:82786"},{"id":"_T16","span":{"begin":334,"end":347},"obj":"FMAID:196733"},{"id":"_T17","span":{"begin":334,"end":347},"obj":"FMAID:82744"},{"id":"_T18","span":{"begin":409,"end":419},"obj":"FMAID:167180"},{"id":"_T19","span":{"begin":510,"end":522},"obj":"FMAID:82816"},{"id":"_T20","span":{"begin":510,"end":522},"obj":"FMAID:196811"},{"id":"_T21","span":{"begin":754,"end":764},"obj":"FMAID:167180"},{"id":"_T22","span":{"begin":809,"end":821},"obj":"FMAID:197276"},{"id":"_T23","span":{"begin":809,"end":821},"obj":"FMAID:82737"},{"id":"_T24","span":{"begin":822,"end":831},"obj":"FMAID:102867"},{"id":"_T25","span":{"begin":879,"end":898},"obj":"FMAID:82786"},{"id":"_T26","span":{"begin":879,"end":898},"obj":"FMAID:196780"},{"id":"_T27","span":{"begin":1168,"end":1180},"obj":"FMAID:82816"},{"id":"_T28","span":{"begin":1168,"end":1180},"obj":"FMAID:196811"},{"id":"_T29","span":{"begin":1288,"end":1298},"obj":"FMAID:167180"},{"id":"_T30","span":{"begin":1323,"end":1333},"obj":"FMAID:167180"},{"id":"_T31","span":{"begin":1364,"end":1374},"obj":"FMAID:179289"},{"id":"_T32","span":{"begin":1364,"end":1374},"obj":"FMAID:74552"},{"id":"_T33","span":{"begin":1364,"end":1374},"obj":"FMAID:222825"},{"id":"_T34","span":{"begin":1364,"end":1382},"obj":"FMAID:201651"},{"id":"_T35","span":{"begin":1364,"end":1382},"obj":"FMAID:86697"},{"id":"_T36","span":{"begin":1377,"end":1382},"obj":"FMAID:169002"},{"id":"_T37","span":{"begin":1377,"end":1382},"obj":"FMAID:68646"},{"id":"_T38","span":{"begin":1421,"end":1426},"obj":"FMAID:68646"},{"id":"_T39","span":{"begin":1421,"end":1426},"obj":"FMAID:169002"},{"id":"_T40","span":{"begin":1466,"end":1478},"obj":"FMAID:74531"},{"id":"_T41","span":{"begin":1466,"end":1478},"obj":"FMAID:179268"},{"id":"_T42","span":{"begin":1562,"end":1572},"obj":"FMAID:167180"},{"id":"_T43","span":{"begin":1613,"end":1624},"obj":"FMAID:196787"},{"id":"_T44","span":{"begin":1613,"end":1624},"obj":"FMAID:82792"},{"id":"_T45","span":{"begin":1672,"end":1677},"obj":"FMAID:68646"},{"id":"_T46","span":{"begin":1672,"end":1677},"obj":"FMAID:169002"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Differential expression of alpha2-6 sialylated polylactosamine structures by human B and T cells.\nWe found that human peripheral B and T cells differed in the surface expression of alpha2-6 sialylated type 2 chain glycans. In contrast to B cells, T cells expressed only sialoglycans with repeated N-acetyllactosamine (Galss1-4GlcNAc) disaccharides. This finding was based on the specificity of the monoclonal antibodies HB6, HB9 (CD24), HD66 (CDw76), FB21, and CRIS4 (CDw76) with the alpha2-6 sialylated model gangliosides IV6NeuAcnLc4Cer (2-6 SPG), VI6NeuAcnLc6Cer (2-6 SnHC), VIII6NeuAcnLc8Cer (2-6 SnOC), and X6NeuAcnLc10Cer (2-6 SnDC). We found that, in addition to their common requirement of an alpha2-6 bound terminal sialic acid for binding, the antibodies displayed preferences for the length of the carbohydrate backbones. Some of them bound mainly to 2-6 SPG with one N-acetyllactosamine (LacNAc) unit (HB9, HD66); others preferentially to 2-6 SnHC and 2-6 SnOC, with two and three LacNAc units, respectively (HB6 and FB21); and one of them exclusively to very polar alpha2-6 sialylated type 2 chain antigens (CRIS4) such as to 2-6 SnOC and even more polar gangliosides with three and more LacNAc units. These specificities could be correlated with the cellular binding of the antibodies as follows: whereas all antibodies bound to human CD 19 positive peripheral B cells, their reactivity with CD3 positive T cells was either nearly lacking (HD66, HB9), intermediate (about 65%: HB6, FB21) or strongly positive (CRIS4, 95%). Thus, the binding of the antibodies to 2-6 sialylated glycans with multiple lactosamine units appeared to determine their binding to T-cells."}

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":420,"end":423},"obj":"http://www.uniprot.org/uniprot/O75355"},{"id":"T2","span":{"begin":1021,"end":1024},"obj":"http://www.uniprot.org/uniprot/O75355"},{"id":"T3","span":{"begin":1491,"end":1494},"obj":"http://www.uniprot.org/uniprot/O75355"},{"id":"T4","span":{"begin":430,"end":434},"obj":"http://www.uniprot.org/uniprot/P25063"},{"id":"T5","span":{"begin":544,"end":547},"obj":"http://www.uniprot.org/uniprot/Q9UF80"},{"id":"T6","span":{"begin":866,"end":869},"obj":"http://www.uniprot.org/uniprot/Q9UF80"}],"text":"Differential expression of alpha2-6 sialylated polylactosamine structures by human B and T cells.\nWe found that human peripheral B and T cells differed in the surface expression of alpha2-6 sialylated type 2 chain glycans. In contrast to B cells, T cells expressed only sialoglycans with repeated N-acetyllactosamine (Galss1-4GlcNAc) disaccharides. This finding was based on the specificity of the monoclonal antibodies HB6, HB9 (CD24), HD66 (CDw76), FB21, and CRIS4 (CDw76) with the alpha2-6 sialylated model gangliosides IV6NeuAcnLc4Cer (2-6 SPG), VI6NeuAcnLc6Cer (2-6 SnHC), VIII6NeuAcnLc8Cer (2-6 SnOC), and X6NeuAcnLc10Cer (2-6 SnDC). We found that, in addition to their common requirement of an alpha2-6 bound terminal sialic acid for binding, the antibodies displayed preferences for the length of the carbohydrate backbones. Some of them bound mainly to 2-6 SPG with one N-acetyllactosamine (LacNAc) unit (HB9, HD66); others preferentially to 2-6 SnHC and 2-6 SnOC, with two and three LacNAc units, respectively (HB6 and FB21); and one of them exclusively to very polar alpha2-6 sialylated type 2 chain antigens (CRIS4) such as to 2-6 SnOC and even more polar gangliosides with three and more LacNAc units. These specificities could be correlated with the cellular binding of the antibodies as follows: whereas all antibodies bound to human CD 19 positive peripheral B cells, their reactivity with CD3 positive T cells was either nearly lacking (HD66, HB9), intermediate (about 65%: HB6, FB21) or strongly positive (CRIS4, 95%). Thus, the binding of the antibodies to 2-6 sialylated glycans with multiple lactosamine units appeared to determine their binding to T-cells."}

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":430,"end":434},"obj":"http://www.uniprot.org/uniprot/P24807"}],"text":"Differential expression of alpha2-6 sialylated polylactosamine structures by human B and T cells.\nWe found that human peripheral B and T cells differed in the surface expression of alpha2-6 sialylated type 2 chain glycans. In contrast to B cells, T cells expressed only sialoglycans with repeated N-acetyllactosamine (Galss1-4GlcNAc) disaccharides. This finding was based on the specificity of the monoclonal antibodies HB6, HB9 (CD24), HD66 (CDw76), FB21, and CRIS4 (CDw76) with the alpha2-6 sialylated model gangliosides IV6NeuAcnLc4Cer (2-6 SPG), VI6NeuAcnLc6Cer (2-6 SnHC), VIII6NeuAcnLc8Cer (2-6 SnOC), and X6NeuAcnLc10Cer (2-6 SnDC). We found that, in addition to their common requirement of an alpha2-6 bound terminal sialic acid for binding, the antibodies displayed preferences for the length of the carbohydrate backbones. Some of them bound mainly to 2-6 SPG with one N-acetyllactosamine (LacNAc) unit (HB9, HD66); others preferentially to 2-6 SnHC and 2-6 SnOC, with two and three LacNAc units, respectively (HB6 and FB21); and one of them exclusively to very polar alpha2-6 sialylated type 2 chain antigens (CRIS4) such as to 2-6 SnOC and even more polar gangliosides with three and more LacNAc units. These specificities could be correlated with the cellular binding of the antibodies as follows: whereas all antibodies bound to human CD 19 positive peripheral B cells, their reactivity with CD3 positive T cells was either nearly lacking (HD66, HB9), intermediate (about 65%: HB6, FB21) or strongly positive (CRIS4, 95%). Thus, the binding of the antibodies to 2-6 sialylated glycans with multiple lactosamine units appeared to determine their binding to T-cells."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":91,"end":96},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T2","span":{"begin":137,"end":142},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T3","span":{"begin":240,"end":245},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T4","span":{"begin":249,"end":254},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T5","span":{"begin":354,"end":361},"obj":"http://purl.bioontology.org/ontology/STY/T033"},{"id":"T6","span":{"begin":398,"end":408},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/608684"},{"id":"T7","span":{"begin":1377,"end":1382},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T8","span":{"begin":1421,"end":1426},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T9","span":{"begin":1672,"end":1677},"obj":"http://purl.bioontology.org/ontology/STY/T025"}],"text":"Differential expression of alpha2-6 sialylated polylactosamine structures by human B and T cells.\nWe found that human peripheral B and T cells differed in the surface expression of alpha2-6 sialylated type 2 chain glycans. In contrast to B cells, T cells expressed only sialoglycans with repeated N-acetyllactosamine (Galss1-4GlcNAc) disaccharides. This finding was based on the specificity of the monoclonal antibodies HB6, HB9 (CD24), HD66 (CDw76), FB21, and CRIS4 (CDw76) with the alpha2-6 sialylated model gangliosides IV6NeuAcnLc4Cer (2-6 SPG), VI6NeuAcnLc6Cer (2-6 SnHC), VIII6NeuAcnLc8Cer (2-6 SnOC), and X6NeuAcnLc10Cer (2-6 SnDC). We found that, in addition to their common requirement of an alpha2-6 bound terminal sialic acid for binding, the antibodies displayed preferences for the length of the carbohydrate backbones. Some of them bound mainly to 2-6 SPG with one N-acetyllactosamine (LacNAc) unit (HB9, HD66); others preferentially to 2-6 SnHC and 2-6 SnOC, with two and three LacNAc units, respectively (HB6 and FB21); and one of them exclusively to very polar alpha2-6 sialylated type 2 chain antigens (CRIS4) such as to 2-6 SnOC and even more polar gangliosides with three and more LacNAc units. These specificities could be correlated with the cellular binding of the antibodies as follows: whereas all antibodies bound to human CD 19 positive peripheral B cells, their reactivity with CD3 positive T cells was either nearly lacking (HD66, HB9), intermediate (about 65%: HB6, FB21) or strongly positive (CRIS4, 95%). Thus, the binding of the antibodies to 2-6 sialylated glycans with multiple lactosamine units appeared to determine their binding to T-cells."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":36,"end":46},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T2","span":{"begin":190,"end":200},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T3","span":{"begin":493,"end":503},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T4","span":{"begin":1087,"end":1097},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T5","span":{"begin":1580,"end":1590},"obj":"http://purl.obolibrary.org/obo/GO_0097503"},{"id":"T6","span":{"begin":1264,"end":1272},"obj":"http://purl.obolibrary.org/obo/GO_0007349"},{"id":"T7","span":{"begin":1364,"end":1382},"obj":"http://purl.obolibrary.org/obo/GO_0002454"},{"id":"T8","span":{"begin":1364,"end":1382},"obj":"http://purl.obolibrary.org/obo/GO_0002453"},{"id":"T9","span":{"begin":1364,"end":1382},"obj":"http://purl.obolibrary.org/obo/GO_0002343"}],"text":"Differential expression of alpha2-6 sialylated polylactosamine structures by human B and T cells.\nWe found that human peripheral B and T cells differed in the surface expression of alpha2-6 sialylated type 2 chain glycans. In contrast to B cells, T cells expressed only sialoglycans with repeated N-acetyllactosamine (Galss1-4GlcNAc) disaccharides. This finding was based on the specificity of the monoclonal antibodies HB6, HB9 (CD24), HD66 (CDw76), FB21, and CRIS4 (CDw76) with the alpha2-6 sialylated model gangliosides IV6NeuAcnLc4Cer (2-6 SPG), VI6NeuAcnLc6Cer (2-6 SnHC), VIII6NeuAcnLc8Cer (2-6 SnOC), and X6NeuAcnLc10Cer (2-6 SnDC). We found that, in addition to their common requirement of an alpha2-6 bound terminal sialic acid for binding, the antibodies displayed preferences for the length of the carbohydrate backbones. Some of them bound mainly to 2-6 SPG with one N-acetyllactosamine (LacNAc) unit (HB9, HD66); others preferentially to 2-6 SnHC and 2-6 SnOC, with two and three LacNAc units, respectively (HB6 and FB21); and one of them exclusively to very polar alpha2-6 sialylated type 2 chain antigens (CRIS4) such as to 2-6 SnOC and even more polar gangliosides with three and more LacNAc units. These specificities could be correlated with the cellular binding of the antibodies as follows: whereas all antibodies bound to human CD 19 positive peripheral B cells, their reactivity with CD3 positive T cells was either nearly lacking (HD66, HB9), intermediate (about 65%: HB6, FB21) or strongly positive (CRIS4, 95%). Thus, the binding of the antibodies to 2-6 sialylated glycans with multiple lactosamine units appeared to determine their binding to T-cells."}

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":409,"end":419},"obj":"http://purl.obolibrary.org/obo/GO_0003823"},{"id":"T2","span":{"begin":754,"end":764},"obj":"http://purl.obolibrary.org/obo/GO_0003823"},{"id":"T3","span":{"begin":1288,"end":1298},"obj":"http://purl.obolibrary.org/obo/GO_0003823"},{"id":"T4","span":{"begin":1323,"end":1333},"obj":"http://purl.obolibrary.org/obo/GO_0003823"},{"id":"T5","span":{"begin":1562,"end":1572},"obj":"http://purl.obolibrary.org/obo/GO_0003823"},{"id":"T6","span":{"begin":741,"end":748},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T7","span":{"begin":1273,"end":1280},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T8","span":{"begin":1547,"end":1554},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T9","span":{"begin":1659,"end":1666},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T10","span":{"begin":741,"end":748},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T11","span":{"begin":1273,"end":1280},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T12","span":{"begin":1547,"end":1554},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T13","span":{"begin":1659,"end":1666},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T14","span":{"begin":741,"end":748},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T15","span":{"begin":1273,"end":1280},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T16","span":{"begin":1547,"end":1554},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T17","span":{"begin":1659,"end":1666},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T18","span":{"begin":741,"end":748},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T19","span":{"begin":1273,"end":1280},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T20","span":{"begin":1547,"end":1554},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T21","span":{"begin":1659,"end":1666},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T22","span":{"begin":1659,"end":1677},"obj":"http://purl.obolibrary.org/obo/GO_0042608"}],"text":"Differential expression of alpha2-6 sialylated polylactosamine structures by human B and T cells.\nWe found that human peripheral B and T cells differed in the surface expression of alpha2-6 sialylated type 2 chain glycans. In contrast to B cells, T cells expressed only sialoglycans with repeated N-acetyllactosamine (Galss1-4GlcNAc) disaccharides. This finding was based on the specificity of the monoclonal antibodies HB6, HB9 (CD24), HD66 (CDw76), FB21, and CRIS4 (CDw76) with the alpha2-6 sialylated model gangliosides IV6NeuAcnLc4Cer (2-6 SPG), VI6NeuAcnLc6Cer (2-6 SnHC), VIII6NeuAcnLc8Cer (2-6 SnOC), and X6NeuAcnLc10Cer (2-6 SnDC). We found that, in addition to their common requirement of an alpha2-6 bound terminal sialic acid for binding, the antibodies displayed preferences for the length of the carbohydrate backbones. Some of them bound mainly to 2-6 SPG with one N-acetyllactosamine (LacNAc) unit (HB9, HD66); others preferentially to 2-6 SnHC and 2-6 SnOC, with two and three LacNAc units, respectively (HB6 and FB21); and one of them exclusively to very polar alpha2-6 sialylated type 2 chain antigens (CRIS4) such as to 2-6 SnOC and even more polar gangliosides with three and more LacNAc units. These specificities could be correlated with the cellular binding of the antibodies as follows: whereas all antibodies bound to human CD 19 positive peripheral B cells, their reactivity with CD3 positive T cells was either nearly lacking (HD66, HB9), intermediate (about 65%: HB6, FB21) or strongly positive (CRIS4, 95%). Thus, the binding of the antibodies to 2-6 sialylated glycans with multiple lactosamine units appeared to determine their binding to T-cells."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":91,"end":96},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T2","span":{"begin":137,"end":142},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T3","span":{"begin":240,"end":245},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T4","span":{"begin":249,"end":254},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T5","span":{"begin":1377,"end":1382},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T6","span":{"begin":1421,"end":1426},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T7","span":{"begin":1672,"end":1677},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"Differential expression of alpha2-6 sialylated polylactosamine structures by human B and T cells.\nWe found that human peripheral B and T cells differed in the surface expression of alpha2-6 sialylated type 2 chain glycans. In contrast to B cells, T cells expressed only sialoglycans with repeated N-acetyllactosamine (Galss1-4GlcNAc) disaccharides. This finding was based on the specificity of the monoclonal antibodies HB6, HB9 (CD24), HD66 (CDw76), FB21, and CRIS4 (CDw76) with the alpha2-6 sialylated model gangliosides IV6NeuAcnLc4Cer (2-6 SPG), VI6NeuAcnLc6Cer (2-6 SnHC), VIII6NeuAcnLc8Cer (2-6 SnOC), and X6NeuAcnLc10Cer (2-6 SnDC). We found that, in addition to their common requirement of an alpha2-6 bound terminal sialic acid for binding, the antibodies displayed preferences for the length of the carbohydrate backbones. Some of them bound mainly to 2-6 SPG with one N-acetyllactosamine (LacNAc) unit (HB9, HD66); others preferentially to 2-6 SnHC and 2-6 SnOC, with two and three LacNAc units, respectively (HB6 and FB21); and one of them exclusively to very polar alpha2-6 sialylated type 2 chain antigens (CRIS4) such as to 2-6 SnOC and even more polar gangliosides with three and more LacNAc units. These specificities could be correlated with the cellular binding of the antibodies as follows: whereas all antibodies bound to human CD 19 positive peripheral B cells, their reactivity with CD3 positive T cells was either nearly lacking (HD66, HB9), intermediate (about 65%: HB6, FB21) or strongly positive (CRIS4, 95%). Thus, the binding of the antibodies to 2-6 sialylated glycans with multiple lactosamine units appeared to determine their binding to T-cells."}

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":77,"end":82},"obj":"http://edamontology.org/topic_2815"},{"id":"T2","span":{"begin":112,"end":117},"obj":"http://edamontology.org/topic_2815"},{"id":"T3","span":{"begin":716,"end":724},"obj":"http://edamontology.org/topic_0749"},{"id":"T4","span":{"begin":809,"end":821},"obj":"http://edamontology.org/topic_0152"},{"id":"T5","span":{"begin":1111,"end":1119},"obj":"http://edamontology.org/topic_2830"},{"id":"T6","span":{"begin":1343,"end":1348},"obj":"http://edamontology.org/topic_2815"}],"text":"Differential expression of alpha2-6 sialylated polylactosamine structures by human B and T cells.\nWe found that human peripheral B and T cells differed in the surface expression of alpha2-6 sialylated type 2 chain glycans. In contrast to B cells, T cells expressed only sialoglycans with repeated N-acetyllactosamine (Galss1-4GlcNAc) disaccharides. This finding was based on the specificity of the monoclonal antibodies HB6, HB9 (CD24), HD66 (CDw76), FB21, and CRIS4 (CDw76) with the alpha2-6 sialylated model gangliosides IV6NeuAcnLc4Cer (2-6 SPG), VI6NeuAcnLc6Cer (2-6 SnHC), VIII6NeuAcnLc8Cer (2-6 SnOC), and X6NeuAcnLc10Cer (2-6 SnDC). We found that, in addition to their common requirement of an alpha2-6 bound terminal sialic acid for binding, the antibodies displayed preferences for the length of the carbohydrate backbones. Some of them bound mainly to 2-6 SPG with one N-acetyllactosamine (LacNAc) unit (HB9, HD66); others preferentially to 2-6 SnHC and 2-6 SnOC, with two and three LacNAc units, respectively (HB6 and FB21); and one of them exclusively to very polar alpha2-6 sialylated type 2 chain antigens (CRIS4) such as to 2-6 SnOC and even more polar gangliosides with three and more LacNAc units. These specificities could be correlated with the cellular binding of the antibodies as follows: whereas all antibodies bound to human CD 19 positive peripheral B cells, their reactivity with CD3 positive T cells was either nearly lacking (HD66, HB9), intermediate (about 65%: HB6, FB21) or strongly positive (CRIS4, 95%). Thus, the binding of the antibodies to 2-6 sialylated glycans with multiple lactosamine units appeared to determine their binding to T-cells."}

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":0,"end":23},"obj":"http://edamontology.org/operation_3742"},{"id":"T2","span":{"begin":63,"end":73},"obj":"http://edamontology.org/data_0883"},{"id":"T3","span":{"begin":1244,"end":1254},"obj":"http://edamontology.org/operation_3465"}],"text":"Differential expression of alpha2-6 sialylated polylactosamine structures by human B and T cells.\nWe found that human peripheral B and T cells differed in the surface expression of alpha2-6 sialylated type 2 chain glycans. In contrast to B cells, T cells expressed only sialoglycans with repeated N-acetyllactosamine (Galss1-4GlcNAc) disaccharides. This finding was based on the specificity of the monoclonal antibodies HB6, HB9 (CD24), HD66 (CDw76), FB21, and CRIS4 (CDw76) with the alpha2-6 sialylated model gangliosides IV6NeuAcnLc4Cer (2-6 SPG), VI6NeuAcnLc6Cer (2-6 SnHC), VIII6NeuAcnLc8Cer (2-6 SnOC), and X6NeuAcnLc10Cer (2-6 SnDC). We found that, in addition to their common requirement of an alpha2-6 bound terminal sialic acid for binding, the antibodies displayed preferences for the length of the carbohydrate backbones. Some of them bound mainly to 2-6 SPG with one N-acetyllactosamine (LacNAc) unit (HB9, HD66); others preferentially to 2-6 SnHC and 2-6 SnOC, with two and three LacNAc units, respectively (HB6 and FB21); and one of them exclusively to very polar alpha2-6 sialylated type 2 chain antigens (CRIS4) such as to 2-6 SnOC and even more polar gangliosides with three and more LacNAc units. These specificities could be correlated with the cellular binding of the antibodies as follows: whereas all antibodies bound to human CD 19 positive peripheral B cells, their reactivity with CD3 positive T cells was either nearly lacking (HD66, HB9), intermediate (about 65%: HB6, FB21) or strongly positive (CRIS4, 95%). Thus, the binding of the antibodies to 2-6 sialylated glycans with multiple lactosamine units appeared to determine their binding to T-cells."}

{"project":"GlyCosmos600-FMA","denotations":[{"id":"PD-FMA-PAE-B_T1","span":{"begin":91,"end":96},"obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"PD-FMA-PAE-B_T2","span":{"begin":137,"end":142},"obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"PD-FMA-PAE-B_T3","span":{"begin":240,"end":245},"obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"PD-FMA-PAE-B_T4","span":{"begin":249,"end":254},"obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"PD-FMA-PAE-B_T5","span":{"begin":334,"end":347},"obj":"http://purl.org/sig/ont/fma/fma82744"},{"id":"PD-FMA-PAE-B_T6","span":{"begin":409,"end":419},"obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"PD-FMA-PAE-B_T7","span":{"begin":510,"end":522},"obj":"http://purl.org/sig/ont/fma/fma82816"},{"id":"PD-FMA-PAE-B_T8","span":{"begin":754,"end":764},"obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"PD-FMA-PAE-B_T9","span":{"begin":809,"end":821},"obj":"http://purl.org/sig/ont/fma/fma82737"},{"id":"PD-FMA-PAE-B_T10","span":{"begin":822,"end":831},"obj":"http://purl.org/sig/ont/fma/fma13478"},{"id":"PD-FMA-PAE-B_T11","span":{"begin":1168,"end":1180},"obj":"http://purl.org/sig/ont/fma/fma82816"},{"id":"PD-FMA-PAE-B_T12","span":{"begin":1288,"end":1298},"obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"PD-FMA-PAE-B_T13","span":{"begin":1323,"end":1333},"obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"PD-FMA-PAE-B_T14","span":{"begin":1377,"end":1382},"obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"PD-FMA-PAE-B_T15","span":{"begin":1421,"end":1426},"obj":"http://purl.org/sig/ont/fma/fma68646"},{"id":"PD-FMA-PAE-B_T16","span":{"begin":1562,"end":1572},"obj":"http://purl.org/sig/ont/fma/fma62871"},{"id":"PD-FMA-PAE-B_T17","span":{"begin":1672,"end":1677},"obj":"http://purl.org/sig/ont/fma/fma68646"}],"text":"Differential expression of alpha2-6 sialylated polylactosamine structures by human B and T cells.\nWe found that human peripheral B and T cells differed in the surface expression of alpha2-6 sialylated type 2 chain glycans. In contrast to B cells, T cells expressed only sialoglycans with repeated N-acetyllactosamine (Galss1-4GlcNAc) disaccharides. This finding was based on the specificity of the monoclonal antibodies HB6, HB9 (CD24), HD66 (CDw76), FB21, and CRIS4 (CDw76) with the alpha2-6 sialylated model gangliosides IV6NeuAcnLc4Cer (2-6 SPG), VI6NeuAcnLc6Cer (2-6 SnHC), VIII6NeuAcnLc8Cer (2-6 SnOC), and X6NeuAcnLc10Cer (2-6 SnDC). We found that, in addition to their common requirement of an alpha2-6 bound terminal sialic acid for binding, the antibodies displayed preferences for the length of the carbohydrate backbones. Some of them bound mainly to 2-6 SPG with one N-acetyllactosamine (LacNAc) unit (HB9, HD66); others preferentially to 2-6 SnHC and 2-6 SnOC, with two and three LacNAc units, respectively (HB6 and FB21); and one of them exclusively to very polar alpha2-6 sialylated type 2 chain antigens (CRIS4) such as to 2-6 SnOC and even more polar gangliosides with three and more LacNAc units. These specificities could be correlated with the cellular binding of the antibodies as follows: whereas all antibodies bound to human CD 19 positive peripheral B cells, their reactivity with CD3 positive T cells was either nearly lacking (HD66, HB9), intermediate (about 65%: HB6, FB21) or strongly positive (CRIS4, 95%). Thus, the binding of the antibodies to 2-6 sialylated glycans with multiple lactosamine units appeared to determine their binding to T-cells."}

{"project":"GlyCosmos600-CLO","denotations":[{"id":"T1","span":{"begin":89,"end":96},"obj":"http://purl.obolibrary.org/obo/CL_0000084"},{"id":"T2","span":{"begin":135,"end":142},"obj":"http://purl.obolibrary.org/obo/CL_0000084"},{"id":"T3","span":{"begin":238,"end":245},"obj":"http://purl.obolibrary.org/obo/CL_0000236"},{"id":"T4","span":{"begin":247,"end":254},"obj":"http://purl.obolibrary.org/obo/CL_0000084"},{"id":"T5","span":{"begin":1349,"end":1354},"obj":"http://purl.obolibrary.org/obo/CLO_0053432"},{"id":"T6","span":{"begin":1375,"end":1382},"obj":"http://purl.obolibrary.org/obo/CL_0000236"},{"id":"T7","span":{"begin":1406,"end":1409},"obj":"http://purl.obolibrary.org/obo/CLO_0053434"},{"id":"T8","span":{"begin":1406,"end":1409},"obj":"http://purl.obolibrary.org/obo/CLO_0052882"},{"id":"T9","span":{"begin":1419,"end":1426},"obj":"http://purl.obolibrary.org/obo/CL_0000084"},{"id":"T10","span":{"begin":1672,"end":1677},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"Differential expression of alpha2-6 sialylated polylactosamine structures by human B and T cells.\nWe found that human peripheral B and T cells differed in the surface expression of alpha2-6 sialylated type 2 chain glycans. In contrast to B cells, T cells expressed only sialoglycans with repeated N-acetyllactosamine (Galss1-4GlcNAc) disaccharides. This finding was based on the specificity of the monoclonal antibodies HB6, HB9 (CD24), HD66 (CDw76), FB21, and CRIS4 (CDw76) with the alpha2-6 sialylated model gangliosides IV6NeuAcnLc4Cer (2-6 SPG), VI6NeuAcnLc6Cer (2-6 SnHC), VIII6NeuAcnLc8Cer (2-6 SnOC), and X6NeuAcnLc10Cer (2-6 SnDC). We found that, in addition to their common requirement of an alpha2-6 bound terminal sialic acid for binding, the antibodies displayed preferences for the length of the carbohydrate backbones. Some of them bound mainly to 2-6 SPG with one N-acetyllactosamine (LacNAc) unit (HB9, HD66); others preferentially to 2-6 SnHC and 2-6 SnOC, with two and three LacNAc units, respectively (HB6 and FB21); and one of them exclusively to very polar alpha2-6 sialylated type 2 chain antigens (CRIS4) such as to 2-6 SnOC and even more polar gangliosides with three and more LacNAc units. These specificities could be correlated with the cellular binding of the antibodies as follows: whereas all antibodies bound to human CD 19 positive peripheral B cells, their reactivity with CD3 positive T cells was either nearly lacking (HD66, HB9), intermediate (about 65%: HB6, FB21) or strongly positive (CRIS4, 95%). Thus, the binding of the antibodies to 2-6 sialylated glycans with multiple lactosamine units appeared to determine their binding to T-cells."}

{"project":"glycosmos-test-glycan-structure","denotations":[{"id":"PD-GlycanStructures-B_T1","span":{"begin":900,"end":906},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa27/trivialname"},{"id":"PD-GlycanStructures-B_T2","span":{"begin":993,"end":999},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa27/trivialname"},{"id":"PD-GlycanStructures-B_T3","span":{"begin":1201,"end":1207},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa27/trivialname"},{"id":"PD-GlycanStructures-B_T4","span":{"begin":1613,"end":1624},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa158/trivialname"}],"text":"Differential expression of alpha2-6 sialylated polylactosamine structures by human B and T cells.\nWe found that human peripheral B and T cells differed in the surface expression of alpha2-6 sialylated type 2 chain glycans. In contrast to B cells, T cells expressed only sialoglycans with repeated N-acetyllactosamine (Galss1-4GlcNAc) disaccharides. This finding was based on the specificity of the monoclonal antibodies HB6, HB9 (CD24), HD66 (CDw76), FB21, and CRIS4 (CDw76) with the alpha2-6 sialylated model gangliosides IV6NeuAcnLc4Cer (2-6 SPG), VI6NeuAcnLc6Cer (2-6 SnHC), VIII6NeuAcnLc8Cer (2-6 SnOC), and X6NeuAcnLc10Cer (2-6 SnDC). We found that, in addition to their common requirement of an alpha2-6 bound terminal sialic acid for binding, the antibodies displayed preferences for the length of the carbohydrate backbones. Some of them bound mainly to 2-6 SPG with one N-acetyllactosamine (LacNAc) unit (HB9, HD66); others preferentially to 2-6 SnHC and 2-6 SnOC, with two and three LacNAc units, respectively (HB6 and FB21); and one of them exclusively to very polar alpha2-6 sialylated type 2 chain antigens (CRIS4) such as to 2-6 SnOC and even more polar gangliosides with three and more LacNAc units. These specificities could be correlated with the cellular binding of the antibodies as follows: whereas all antibodies bound to human CD 19 positive peripheral B cells, their reactivity with CD3 positive T cells was either nearly lacking (HD66, HB9), intermediate (about 65%: HB6, FB21) or strongly positive (CRIS4, 95%). Thus, the binding of the antibodies to 2-6 sialylated glycans with multiple lactosamine units appeared to determine their binding to T-cells."}

{"project":"glycosmos-test-structure-v1","denotations":[{"id":"PD-GlycanStructures-B_T1","span":{"begin":900,"end":906},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa27/trivialname"},{"id":"PD-GlycanStructures-B_T2","span":{"begin":993,"end":999},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa27/trivialname"},{"id":"PD-GlycanStructures-B_T3","span":{"begin":1201,"end":1207},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa27/trivialname"},{"id":"PD-GlycanStructures-B_T4","span":{"begin":1613,"end":1624},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa158/trivialname"}],"text":"Differential expression of alpha2-6 sialylated polylactosamine structures by human B and T cells.\nWe found that human peripheral B and T cells differed in the surface expression of alpha2-6 sialylated type 2 chain glycans. In contrast to B cells, T cells expressed only sialoglycans with repeated N-acetyllactosamine (Galss1-4GlcNAc) disaccharides. This finding was based on the specificity of the monoclonal antibodies HB6, HB9 (CD24), HD66 (CDw76), FB21, and CRIS4 (CDw76) with the alpha2-6 sialylated model gangliosides IV6NeuAcnLc4Cer (2-6 SPG), VI6NeuAcnLc6Cer (2-6 SnHC), VIII6NeuAcnLc8Cer (2-6 SnOC), and X6NeuAcnLc10Cer (2-6 SnDC). We found that, in addition to their common requirement of an alpha2-6 bound terminal sialic acid for binding, the antibodies displayed preferences for the length of the carbohydrate backbones. Some of them bound mainly to 2-6 SPG with one N-acetyllactosamine (LacNAc) unit (HB9, HD66); others preferentially to 2-6 SnHC and 2-6 SnOC, with two and three LacNAc units, respectively (HB6 and FB21); and one of them exclusively to very polar alpha2-6 sialylated type 2 chain antigens (CRIS4) such as to 2-6 SnOC and even more polar gangliosides with three and more LacNAc units. These specificities could be correlated with the cellular binding of the antibodies as follows: whereas all antibodies bound to human CD 19 positive peripheral B cells, their reactivity with CD3 positive T cells was either nearly lacking (HD66, HB9), intermediate (about 65%: HB6, FB21) or strongly positive (CRIS4, 95%). Thus, the binding of the antibodies to 2-6 sialylated glycans with multiple lactosamine units appeared to determine their binding to T-cells."}

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expression of alpha2-6 sialylated polylactosamine structures by human B and T cells.\nWe found that human peripheral B and T cells differed in the surface expression of alpha2-6 sialylated type 2 chain glycans. In contrast to B cells, T cells expressed only sialoglycans with repeated N-acetyllactosamine (Galss1-4GlcNAc) disaccharides. This finding was based on the specificity of the monoclonal antibodies HB6, HB9 (CD24), HD66 (CDw76), FB21, and CRIS4 (CDw76) with the alpha2-6 sialylated model gangliosides IV6NeuAcnLc4Cer (2-6 SPG), VI6NeuAcnLc6Cer (2-6 SnHC), VIII6NeuAcnLc8Cer (2-6 SnOC), and X6NeuAcnLc10Cer (2-6 SnDC). We found that, in addition to their common requirement of an alpha2-6 bound terminal sialic acid for binding, the antibodies displayed preferences for the length of the carbohydrate backbones. Some of them bound mainly to 2-6 SPG with one N-acetyllactosamine (LacNAc) unit (HB9, HD66); others preferentially to 2-6 SnHC and 2-6 SnOC, with two and three LacNAc units, respectively (HB6 and FB21); and one of them exclusively to very polar alpha2-6 sialylated type 2 chain antigens (CRIS4) such as to 2-6 SnOC and even more polar gangliosides with three and more LacNAc units. These specificities could be correlated with the cellular binding of the antibodies as follows: whereas all antibodies bound to human CD 19 positive peripheral B cells, their reactivity with CD3 positive T cells was either nearly lacking (HD66, HB9), intermediate (about 65%: HB6, FB21) or strongly positive (CRIS4, 95%). Thus, the binding of the antibodies to 2-6 sialylated glycans with multiple lactosamine units appeared to determine their binding to T-cells."}

{"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":47,"end":62},"obj":"http://rdf.glycoinfo.org/glycan/G00058MO"},{"id":"T2","span":{"begin":1613,"end":1624},"obj":"http://rdf.glycoinfo.org/glycan/G00055MO"}],"text":"Differential expression of alpha2-6 sialylated polylactosamine structures by human B and T cells.\nWe found that human peripheral B and T cells differed in the surface expression of alpha2-6 sialylated type 2 chain glycans. In contrast to B cells, T cells expressed only sialoglycans with repeated N-acetyllactosamine (Galss1-4GlcNAc) disaccharides. This finding was based on the specificity of the monoclonal antibodies HB6, HB9 (CD24), HD66 (CDw76), FB21, and CRIS4 (CDw76) with the alpha2-6 sialylated model gangliosides IV6NeuAcnLc4Cer (2-6 SPG), VI6NeuAcnLc6Cer (2-6 SnHC), VIII6NeuAcnLc8Cer (2-6 SnOC), and X6NeuAcnLc10Cer (2-6 SnDC). We found that, in addition to their common requirement of an alpha2-6 bound terminal sialic acid for binding, the antibodies displayed preferences for the length of the carbohydrate backbones. Some of them bound mainly to 2-6 SPG with one N-acetyllactosamine (LacNAc) unit (HB9, HD66); others preferentially to 2-6 SnHC and 2-6 SnOC, with two and three LacNAc units, respectively (HB6 and FB21); and one of them exclusively to very polar alpha2-6 sialylated type 2 chain antigens (CRIS4) such as to 2-6 SnOC and even more polar gangliosides with three and more LacNAc units. These specificities could be correlated with the cellular binding of the antibodies as follows: whereas all antibodies bound to human CD 19 positive peripheral B cells, their reactivity with CD3 positive T cells was either nearly lacking (HD66, HB9), intermediate (about 65%: HB6, FB21) or strongly positive (CRIS4, 95%). Thus, the binding of the antibodies to 2-6 sialylated glycans with multiple lactosamine units appeared to determine their binding to T-cells."}

{"project":"GlyTouCan-IUPAC","denotations":[{"id":"GlycanIUPAC_T1","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G41652MJ\""},{"id":"GlycanIUPAC_T2","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G20761YC\""},{"id":"GlycanIUPAC_T3","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G19807HM\""},{"id":"GlycanIUPAC_T4","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G20351TE\""},{"id":"GlycanIUPAC_T5","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G71957MR\""},{"id":"GlycanIUPAC_T6","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G59040AE\""},{"id":"GlycanIUPAC_T7","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G14987PW\""},{"id":"GlycanIUPAC_T8","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G95064PC\""},{"id":"GlycanIUPAC_T9","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G39143AQ\""},{"id":"GlycanIUPAC_T10","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G65149OO\""},{"id":"GlycanIUPAC_T11","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G02766SY\""},{"id":"GlycanIUPAC_T12","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G26019KJ\""},{"id":"GlycanIUPAC_T13","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G36429CZ\""},{"id":"GlycanIUPAC_T14","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G89633TP\""},{"id":"GlycanIUPAC_T15","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G28494FO\""},{"id":"GlycanIUPAC_T16","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G06219CP\""},{"id":"GlycanIUPAC_T17","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G44237SM\""},{"id":"GlycanIUPAC_T18","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G57948RL\""},{"id":"GlycanIUPAC_T19","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G64016DN\""},{"id":"GlycanIUPAC_T20","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G14536PC\""},{"id":"GlycanIUPAC_T21","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G14356FW\""},{"id":"GlycanIUPAC_T22","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G34565UO\""},{"id":"GlycanIUPAC_T23","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G67124MW\""},{"id":"GlycanIUPAC_T24","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G71457ZU\""},{"id":"GlycanIUPAC_T25","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G55228VZ\""},{"id":"GlycanIUPAC_T26","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G31034MJ\""},{"id":"GlycanIUPAC_T27","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G25776IP\""},{"id":"GlycanIUPAC_T28","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G64442BV\""},{"id":"GlycanIUPAC_T29","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G57018LE\""},{"id":"GlycanIUPAC_T30","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G61761GX\""},{"id":"GlycanIUPAC_T31","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G76318UX\""},{"id":"GlycanIUPAC_T32","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G61906ER\""},{"id":"GlycanIUPAC_T33","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G68723GR\""},{"id":"GlycanIUPAC_T34","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G19540LE\""},{"id":"GlycanIUPAC_T35","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G74944PO\""},{"id":"GlycanIUPAC_T36","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G89489ZJ\""},{"id":"GlycanIUPAC_T37","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G04434YU\""},{"id":"GlycanIUPAC_T38","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G21450PB\""},{"id":"GlycanIUPAC_T39","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G93629QY\""},{"id":"GlycanIUPAC_T40","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G02603TR\""},{"id":"GlycanIUPAC_T41","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G40280JP\""},{"id":"GlycanIUPAC_T42","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G95259IC\""},{"id":"GlycanIUPAC_T43","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G26900FE\""},{"id":"GlycanIUPAC_T44","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G21346KK\""},{"id":"GlycanIUPAC_T45","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G62509FF\""},{"id":"GlycanIUPAC_T46","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G83932AK\""},{"id":"GlycanIUPAC_T47","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G96978IB\""},{"id":"GlycanIUPAC_T48","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G34275DN\""},{"id":"GlycanIUPAC_T49","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G07071JF\""},{"id":"GlycanIUPAC_T50","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G80639QD\""},{"id":"GlycanIUPAC_T51","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G99460PJ\""},{"id":"GlycanIUPAC_T52","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G22024BZ\""},{"id":"GlycanIUPAC_T53","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G74097ZY\""},{"id":"GlycanIUPAC_T54","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G84439YP\""},{"id":"GlycanIUPAC_T55","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G52207WQ\""},{"id":"GlycanIUPAC_T56","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G90695MS\""},{"id":"GlycanIUPAC_T57","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G50398QX\""},{"id":"GlycanIUPAC_T58","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G12166ZT\""},{"id":"GlycanIUPAC_T59","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G48368BR\""},{"id":"GlycanIUPAC_T60","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G57407RW\""},{"id":"GlycanIUPAC_T61","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G00386TY\""},{"id":"GlycanIUPAC_T62","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G18723JK\""},{"id":"GlycanIUPAC_T63","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G93757OR\""},{"id":"GlycanIUPAC_T64","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G29006SI\""},{"id":"GlycanIUPAC_T65","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G03099OQ\""},{"id":"GlycanIUPAC_T66","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G53739OW\""},{"id":"GlycanIUPAC_T67","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G70440ZO\""},{"id":"GlycanIUPAC_T68","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G29951RR\""},{"id":"GlycanIUPAC_T69","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G58402TI\""},{"id":"GlycanIUPAC_T70","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G39875TP\""},{"id":"GlycanIUPAC_T71","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G83439QV\""},{"id":"GlycanIUPAC_T72","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G41762RC\""},{"id":"GlycanIUPAC_T73","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G91604UI\""},{"id":"GlycanIUPAC_T74","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G88447WE\""},{"id":"GlycanIUPAC_T75","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G93634BS\""},{"id":"GlycanIUPAC_T76","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G02587BH\""},{"id":"GlycanIUPAC_T77","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G43511MX\""},{"id":"GlycanIUPAC_T78","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G64958DH\""},{"id":"GlycanIUPAC_T79","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G30384TR\""},{"id":"GlycanIUPAC_T80","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G15624EX\""},{"id":"GlycanIUPAC_T81","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G22706ST\""},{"id":"GlycanIUPAC_T82","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G57408PI\""},{"id":"GlycanIUPAC_T83","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G86403XX\""},{"id":"GlycanIUPAC_T84","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G78043YB\""},{"id":"GlycanIUPAC_T85","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G18952JK\""},{"id":"GlycanIUPAC_T86","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G49020ND\""},{"id":"GlycanIUPAC_T87","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G63590YW\""},{"id":"GlycanIUPAC_T88","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G22793KS\""},{"id":"GlycanIUPAC_T89","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G64134SS\""},{"id":"GlycanIUPAC_T90","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G17338HY\""},{"id":"GlycanIUPAC_T91","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G99745XF\""},{"id":"GlycanIUPAC_T92","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G27782HN\""},{"id":"GlycanIUPAC_T93","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G57496DC\""},{"id":"GlycanIUPAC_T94","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G93169WB\""},{"id":"GlycanIUPAC_T95","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G05518TD\""},{"id":"GlycanIUPAC_T96","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G62603DN\""},{"id":"GlycanIUPAC_T97","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G59574FS\""},{"id":"GlycanIUPAC_T98","span":{"begin":1319,"end":1322},"obj":"\"http://rdf.glycoinfo.org/glycan/G47567WC\""}],"text":"Differential expression of alpha2-6 sialylated polylactosamine structures by human B and T cells.\nWe found that human peripheral B and T cells differed in the surface expression of alpha2-6 sialylated type 2 chain glycans. In contrast to B cells, T cells expressed only sialoglycans with repeated N-acetyllactosamine (Galss1-4GlcNAc) disaccharides. This finding was based on the specificity of the monoclonal antibodies HB6, HB9 (CD24), HD66 (CDw76), FB21, and CRIS4 (CDw76) with the alpha2-6 sialylated model gangliosides IV6NeuAcnLc4Cer (2-6 SPG), VI6NeuAcnLc6Cer (2-6 SnHC), VIII6NeuAcnLc8Cer (2-6 SnOC), and X6NeuAcnLc10Cer (2-6 SnDC). We found that, in addition to their common requirement of an alpha2-6 bound terminal sialic acid for binding, the antibodies displayed preferences for the length of the carbohydrate backbones. Some of them bound mainly to 2-6 SPG with one N-acetyllactosamine (LacNAc) unit (HB9, HD66); others preferentially to 2-6 SnHC and 2-6 SnOC, with two and three LacNAc units, respectively (HB6 and FB21); and one of them exclusively to very polar alpha2-6 sialylated type 2 chain antigens (CRIS4) such as to 2-6 SnOC and even more polar gangliosides with three and more LacNAc units. These specificities could be correlated with the cellular binding of the antibodies as follows: whereas all antibodies bound to human CD 19 positive peripheral B cells, their reactivity with CD3 positive T cells was either nearly lacking (HD66, HB9), intermediate (about 65%: HB6, FB21) or strongly positive (CRIS4, 95%). Thus, the binding of the antibodies to 2-6 sialylated glycans with multiple lactosamine units appeared to determine their binding to T-cells."}