PubMed:26066491 JSONTXT

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":994,"end":1010},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":1043,"end":1055},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":1057,"end":1063},"obj":"Glycan_Motif"},{"id":"T4","span":{"begin":1161,"end":1168},"obj":"Glycan_Motif"},{"id":"T5","span":{"begin":1180,"end":1186},"obj":"Glycan_Motif"},{"id":"T6","span":{"begin":1200,"end":1211},"obj":"Glycan_Motif"},{"id":"T7","span":{"begin":1236,"end":1242},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00031MO"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81533KY"},{"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/G00031MO"},{"id":"A5","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81533KY"},{"id":"A6","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81533KY"},{"id":"A7","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00039MO"}],"text":"Atlantic Salmon Carries a Range of Novel O-Glycan Structures Differentially Localized on Skin and Intestinal Mucins.\nAquaculture is a growing industry, increasing the need for understanding host-pathogen interactions in fish. The skin and mucosal surfaces, covered by a mucus layer composed of mucins, is the first point of contact between fish and pathogens. Highly O-glycosylated mucins have been shown to be an important part of the defense against pathogens, and pathogens bind to host surfaces using lectin-like adhesins. However, knowledge of piscine O-glycosylation is very limited. We characterized mucin O-glycosylation of five freshwater acclimated Atlantic salmon, using mass spectrometry. Of the 109 O-glycans found, most were sialylated and differed in distribution among skin, pyloric ceca, and proximal and distal intestine. Skin O-glycans were shorter (2-6 residues) and less diverse (33 structures) than intestinal O-glycans (2-13 residues, 93 structures). Skin mucins carried O-glycan cores 1, 2, 3, and 5 and three types of sialic acids (Neu5Ac, Neu5Gc, and Kdn) and had sialyl-Tn as the predominant structure. Intestinal mucins carried only cores 1, 2, and 5, Neu5Ac was the only sialic acid present, and sialylated core 5 was the most dominant structure. This structural characterization can be used for identifying structures of putative importance in host-pathogen interactions for further testing in biological assays and disease intervention therapies."}

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":116},"obj":"Sentence"},{"id":"T2","span":{"begin":117,"end":225},"obj":"Sentence"},{"id":"T3","span":{"begin":226,"end":359},"obj":"Sentence"},{"id":"T4","span":{"begin":360,"end":526},"obj":"Sentence"},{"id":"T5","span":{"begin":527,"end":589},"obj":"Sentence"},{"id":"T6","span":{"begin":590,"end":700},"obj":"Sentence"},{"id":"T7","span":{"begin":701,"end":839},"obj":"Sentence"},{"id":"T8","span":{"begin":840,"end":973},"obj":"Sentence"},{"id":"T9","span":{"begin":974,"end":1129},"obj":"Sentence"},{"id":"T10","span":{"begin":1130,"end":1275},"obj":"Sentence"},{"id":"T11","span":{"begin":1276,"end":1477},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":116},"obj":"Sentence"},{"id":"T2","span":{"begin":117,"end":225},"obj":"Sentence"},{"id":"T3","span":{"begin":226,"end":359},"obj":"Sentence"},{"id":"T4","span":{"begin":360,"end":526},"obj":"Sentence"},{"id":"T5","span":{"begin":527,"end":589},"obj":"Sentence"},{"id":"T6","span":{"begin":590,"end":700},"obj":"Sentence"},{"id":"T7","span":{"begin":701,"end":839},"obj":"Sentence"},{"id":"T8","span":{"begin":840,"end":973},"obj":"Sentence"},{"id":"T9","span":{"begin":974,"end":1129},"obj":"Sentence"},{"id":"T10","span":{"begin":1130,"end":1275},"obj":"Sentence"},{"id":"T11","span":{"begin":1276,"end":1477},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Atlantic Salmon Carries a Range of Novel O-Glycan Structures Differentially Localized on Skin and Intestinal Mucins.\nAquaculture is a growing industry, increasing the need for understanding host-pathogen interactions in fish. The skin and mucosal surfaces, covered by a mucus layer composed of mucins, is the first point of contact between fish and pathogens. Highly O-glycosylated mucins have been shown to be an important part of the defense against pathogens, and pathogens bind to host surfaces using lectin-like adhesins. However, knowledge of piscine O-glycosylation is very limited. We characterized mucin O-glycosylation of five freshwater acclimated Atlantic salmon, using mass spectrometry. Of the 109 O-glycans found, most were sialylated and differed in distribution among skin, pyloric ceca, and proximal and distal intestine. Skin O-glycans were shorter (2-6 residues) and less diverse (33 structures) than intestinal O-glycans (2-13 residues, 93 structures). Skin mucins carried O-glycan cores 1, 2, 3, and 5 and three types of sialic acids (Neu5Ac, Neu5Gc, and Kdn) and had sialyl-Tn as the predominant structure. Intestinal mucins carried only cores 1, 2, and 5, Neu5Ac was the only sialic acid present, and sialylated core 5 was the most dominant structure. This structural characterization can be used for identifying structures of putative importance in host-pathogen interactions for further testing in biological assays and disease intervention therapies."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":994,"end":1010},"obj":"https://glytoucan.org/Structures/Glycans/G00031MO"},{"id":"T2","span":{"begin":1043,"end":1055},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T3","span":{"begin":1057,"end":1063},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T4","span":{"begin":1161,"end":1168},"obj":"https://glytoucan.org/Structures/Glycans/G00031MO"},{"id":"T5","span":{"begin":1180,"end":1186},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T6","span":{"begin":1200,"end":1211},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"}],"text":"Atlantic Salmon Carries a Range of Novel O-Glycan Structures Differentially Localized on Skin and Intestinal Mucins.\nAquaculture is a growing industry, increasing the need for understanding host-pathogen interactions in fish. The skin and mucosal surfaces, covered by a mucus layer composed of mucins, is the first point of contact between fish and pathogens. Highly O-glycosylated mucins have been shown to be an important part of the defense against pathogens, and pathogens bind to host surfaces using lectin-like adhesins. However, knowledge of piscine O-glycosylation is very limited. We characterized mucin O-glycosylation of five freshwater acclimated Atlantic salmon, using mass spectrometry. Of the 109 O-glycans found, most were sialylated and differed in distribution among skin, pyloric ceca, and proximal and distal intestine. Skin O-glycans were shorter (2-6 residues) and less diverse (33 structures) than intestinal O-glycans (2-13 residues, 93 structures). Skin mucins carried O-glycan cores 1, 2, 3, and 5 and three types of sialic acids (Neu5Ac, Neu5Gc, and Kdn) and had sialyl-Tn as the predominant structure. Intestinal mucins carried only cores 1, 2, and 5, Neu5Ac was the only sialic acid present, and sialylated core 5 was the most dominant structure. This structural characterization can be used for identifying structures of putative importance in host-pathogen interactions for further testing in biological assays and disease intervention therapies."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":89,"end":93},"obj":"http://purl.obolibrary.org/obo/MAT_0000284"},{"id":"T2","span":{"begin":98,"end":108},"obj":"http://purl.obolibrary.org/obo/MAT_0000043"},{"id":"T3","span":{"begin":230,"end":234},"obj":"http://purl.obolibrary.org/obo/MAT_0000284"},{"id":"T4","span":{"begin":785,"end":789},"obj":"http://purl.obolibrary.org/obo/MAT_0000284"},{"id":"T5","span":{"begin":809,"end":817},"obj":"http://purl.obolibrary.org/obo/MAT_0000491"},{"id":"T6","span":{"begin":829,"end":838},"obj":"http://purl.obolibrary.org/obo/MAT_0000043"},{"id":"T7","span":{"begin":840,"end":844},"obj":"http://purl.obolibrary.org/obo/MAT_0000284"},{"id":"T8","span":{"begin":921,"end":931},"obj":"http://purl.obolibrary.org/obo/MAT_0000043"},{"id":"T9","span":{"begin":974,"end":978},"obj":"http://purl.obolibrary.org/obo/MAT_0000284"},{"id":"T10","span":{"begin":1130,"end":1140},"obj":"http://purl.obolibrary.org/obo/MAT_0000043"}],"text":"Atlantic Salmon Carries a Range of Novel O-Glycan Structures Differentially Localized on Skin and Intestinal Mucins.\nAquaculture is a growing industry, increasing the need for understanding host-pathogen interactions in fish. The skin and mucosal surfaces, covered by a mucus layer composed of mucins, is the first point of contact between fish and pathogens. Highly O-glycosylated mucins have been shown to be an important part of the defense against pathogens, and pathogens bind to host surfaces using lectin-like adhesins. However, knowledge of piscine O-glycosylation is very limited. We characterized mucin O-glycosylation of five freshwater acclimated Atlantic salmon, using mass spectrometry. Of the 109 O-glycans found, most were sialylated and differed in distribution among skin, pyloric ceca, and proximal and distal intestine. Skin O-glycans were shorter (2-6 residues) and less diverse (33 structures) than intestinal O-glycans (2-13 residues, 93 structures). Skin mucins carried O-glycan cores 1, 2, 3, and 5 and three types of sialic acids (Neu5Ac, Neu5Gc, and Kdn) and had sialyl-Tn as the predominant structure. Intestinal mucins carried only cores 1, 2, and 5, Neu5Ac was the only sialic acid present, and sialylated core 5 was the most dominant structure. This structural characterization can be used for identifying structures of putative importance in host-pathogen interactions for further testing in biological assays and disease intervention therapies."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":1057,"end":1063},"obj":"Glycan"},{"id":"T2","span":{"begin":1180,"end":1186},"obj":"Glycan"},{"id":"T3","span":{"begin":1236,"end":1242},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A4","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A5","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G00039MO"},{"id":"A6","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00039MO"}],"text":"Atlantic Salmon Carries a Range of Novel O-Glycan Structures Differentially Localized on Skin and Intestinal Mucins.\nAquaculture is a growing industry, increasing the need for understanding host-pathogen interactions in fish. The skin and mucosal surfaces, covered by a mucus layer composed of mucins, is the first point of contact between fish and pathogens. Highly O-glycosylated mucins have been shown to be an important part of the defense against pathogens, and pathogens bind to host surfaces using lectin-like adhesins. However, knowledge of piscine O-glycosylation is very limited. We characterized mucin O-glycosylation of five freshwater acclimated Atlantic salmon, using mass spectrometry. Of the 109 O-glycans found, most were sialylated and differed in distribution among skin, pyloric ceca, and proximal and distal intestine. Skin O-glycans were shorter (2-6 residues) and less diverse (33 structures) than intestinal O-glycans (2-13 residues, 93 structures). Skin mucins carried O-glycan cores 1, 2, 3, and 5 and three types of sialic acids (Neu5Ac, Neu5Gc, and Kdn) and had sialyl-Tn as the predominant structure. Intestinal mucins carried only cores 1, 2, and 5, Neu5Ac was the only sialic acid present, and sialylated core 5 was the most dominant structure. This structural characterization can be used for identifying structures of putative importance in host-pathogen interactions for further testing in biological assays and disease intervention therapies."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":89,"end":93},"obj":"Body_part"},{"id":"T2","span":{"begin":98,"end":108},"obj":"Body_part"},{"id":"T3","span":{"begin":230,"end":234},"obj":"Body_part"},{"id":"T4","span":{"begin":785,"end":789},"obj":"Body_part"},{"id":"T5","span":{"begin":809,"end":817},"obj":"Body_part"},{"id":"T6","span":{"begin":829,"end":838},"obj":"Body_part"},{"id":"T7","span":{"begin":840,"end":844},"obj":"Body_part"},{"id":"T8","span":{"begin":921,"end":931},"obj":"Body_part"},{"id":"T9","span":{"begin":974,"end":978},"obj":"Body_part"},{"id":"T10","span":{"begin":1130,"end":1140},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000284"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000043"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000284"},{"id":"A4","pred":"mat_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MAT_0000284"},{"id":"A5","pred":"mat_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MAT_0000491"},{"id":"A6","pred":"mat_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/MAT_0000043"},{"id":"A7","pred":"mat_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/MAT_0000284"},{"id":"A8","pred":"mat_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/MAT_0000043"},{"id":"A9","pred":"mat_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/MAT_0000284"},{"id":"A10","pred":"mat_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/MAT_0000043"}],"text":"Atlantic Salmon Carries a Range of Novel O-Glycan Structures Differentially Localized on Skin and Intestinal Mucins.\nAquaculture is a growing industry, increasing the need for understanding host-pathogen interactions in fish. The skin and mucosal surfaces, covered by a mucus layer composed of mucins, is the first point of contact between fish and pathogens. Highly O-glycosylated mucins have been shown to be an important part of the defense against pathogens, and pathogens bind to host surfaces using lectin-like adhesins. However, knowledge of piscine O-glycosylation is very limited. We characterized mucin O-glycosylation of five freshwater acclimated Atlantic salmon, using mass spectrometry. Of the 109 O-glycans found, most were sialylated and differed in distribution among skin, pyloric ceca, and proximal and distal intestine. Skin O-glycans were shorter (2-6 residues) and less diverse (33 structures) than intestinal O-glycans (2-13 residues, 93 structures). Skin mucins carried O-glycan cores 1, 2, 3, and 5 and three types of sialic acids (Neu5Ac, Neu5Gc, and Kdn) and had sialyl-Tn as the predominant structure. Intestinal mucins carried only cores 1, 2, and 5, Neu5Ac was the only sialic acid present, and sialylated core 5 was the most dominant structure. This structural characterization can be used for identifying structures of putative importance in host-pathogen interactions for further testing in biological assays and disease intervention therapies."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":1057,"end":1063},"obj":"Glycan"},{"id":"T2","span":{"begin":1180,"end":1186},"obj":"Glycan"},{"id":"T3","span":{"begin":1236,"end":1242},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A4","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G76685HR"},{"id":"A5","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G76685HR"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G00039MO"},{"id":"A6","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00039MO"}],"text":"Atlantic Salmon Carries a Range of Novel O-Glycan Structures Differentially Localized on Skin and Intestinal Mucins.\nAquaculture is a growing industry, increasing the need for understanding host-pathogen interactions in fish. The skin and mucosal surfaces, covered by a mucus layer composed of mucins, is the first point of contact between fish and pathogens. Highly O-glycosylated mucins have been shown to be an important part of the defense against pathogens, and pathogens bind to host surfaces using lectin-like adhesins. However, knowledge of piscine O-glycosylation is very limited. We characterized mucin O-glycosylation of five freshwater acclimated Atlantic salmon, using mass spectrometry. Of the 109 O-glycans found, most were sialylated and differed in distribution among skin, pyloric ceca, and proximal and distal intestine. Skin O-glycans were shorter (2-6 residues) and less diverse (33 structures) than intestinal O-glycans (2-13 residues, 93 structures). Skin mucins carried O-glycan cores 1, 2, 3, and 5 and three types of sialic acids (Neu5Ac, Neu5Gc, and Kdn) and had sialyl-Tn as the predominant structure. Intestinal mucins carried only cores 1, 2, and 5, Neu5Ac was the only sialic acid present, and sialylated core 5 was the most dominant structure. This structural characterization can be used for identifying structures of putative importance in host-pathogen interactions for further testing in biological assays and disease intervention therapies."}

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":89,"end":93},"obj":"Body_part"},{"id":"T5","span":{"begin":230,"end":234},"obj":"Body_part"},{"id":"T9","span":{"begin":270,"end":275},"obj":"Body_part"},{"id":"T10","span":{"begin":276,"end":281},"obj":"Body_part"},{"id":"T12","span":{"begin":785,"end":789},"obj":"Body_part"},{"id":"T16","span":{"begin":799,"end":803},"obj":"Body_part"},{"id":"T17","span":{"begin":822,"end":838},"obj":"Body_part"},{"id":"T18","span":{"begin":840,"end":844},"obj":"Body_part"},{"id":"T22","span":{"begin":974,"end":978},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000014"},{"id":"A2","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0001003"},{"id":"A3","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0002097"},{"id":"A4","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0002199"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0000014"},{"id":"A6","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0001003"},{"id":"A7","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0002097"},{"id":"A8","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0002199"},{"id":"A9","pred":"uberon_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/UBERON_0000912"},{"id":"A10","pred":"uberon_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/UBERON_0000119"},{"id":"A11","pred":"uberon_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/UBERON_0022303"},{"id":"A12","pred":"uberon_id","subj":"T12","obj":"http://purl.obolibrary.org/obo/UBERON_0000014"},{"id":"A13","pred":"uberon_id","subj":"T12","obj":"http://purl.obolibrary.org/obo/UBERON_0001003"},{"id":"A14","pred":"uberon_id","subj":"T12","obj":"http://purl.obolibrary.org/obo/UBERON_0002097"},{"id":"A15","pred":"uberon_id","subj":"T12","obj":"http://purl.obolibrary.org/obo/UBERON_0002199"},{"id":"A16","pred":"uberon_id","subj":"T16","obj":"http://purl.obolibrary.org/obo/UBERON_0001153"},{"id":"A17","pred":"uberon_id","subj":"T17","obj":"http://purl.obolibrary.org/obo/UBERON_0002116"},{"id":"A18","pred":"uberon_id","subj":"T18","obj":"http://purl.obolibrary.org/obo/UBERON_0000014"},{"id":"A19","pred":"uberon_id","subj":"T18","obj":"http://purl.obolibrary.org/obo/UBERON_0001003"},{"id":"A20","pred":"uberon_id","subj":"T18","obj":"http://purl.obolibrary.org/obo/UBERON_0002097"},{"id":"A21","pred":"uberon_id","subj":"T18","obj":"http://purl.obolibrary.org/obo/UBERON_0002199"},{"id":"A22","pred":"uberon_id","subj":"T22","obj":"http://purl.obolibrary.org/obo/UBERON_0000014"},{"id":"A23","pred":"uberon_id","subj":"T22","obj":"http://purl.obolibrary.org/obo/UBERON_0001003"},{"id":"A24","pred":"uberon_id","subj":"T22","obj":"http://purl.obolibrary.org/obo/UBERON_0002097"},{"id":"A25","pred":"uberon_id","subj":"T22","obj":"http://purl.obolibrary.org/obo/UBERON_0002199"}],"text":"Atlantic Salmon Carries a Range of Novel O-Glycan Structures Differentially Localized on Skin and Intestinal Mucins.\nAquaculture is a growing industry, increasing the need for understanding host-pathogen interactions in fish. The skin and mucosal surfaces, covered by a mucus layer composed of mucins, is the first point of contact between fish and pathogens. Highly O-glycosylated mucins have been shown to be an important part of the defense against pathogens, and pathogens bind to host surfaces using lectin-like adhesins. However, knowledge of piscine O-glycosylation is very limited. We characterized mucin O-glycosylation of five freshwater acclimated Atlantic salmon, using mass spectrometry. Of the 109 O-glycans found, most were sialylated and differed in distribution among skin, pyloric ceca, and proximal and distal intestine. Skin O-glycans were shorter (2-6 residues) and less diverse (33 structures) than intestinal O-glycans (2-13 residues, 93 structures). Skin mucins carried O-glycan cores 1, 2, 3, and 5 and three types of sialic acids (Neu5Ac, Neu5Gc, and Kdn) and had sialyl-Tn as the predominant structure. Intestinal mucins carried only cores 1, 2, and 5, Neu5Ac was the only sialic acid present, and sialylated core 5 was the most dominant structure. This structural characterization can be used for identifying structures of putative importance in host-pathogen interactions for further testing in biological assays and disease intervention therapies."}

{"project":"GlyCosmos15-Taxon","denotations":[{"id":"T1","span":{"begin":220,"end":224},"obj":"Organism"},{"id":"T7","span":{"begin":340,"end":344},"obj":"Organism"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"117565"},{"id":"A2","pred":"db_id","subj":"T1","obj":"117569"},{"id":"A3","pred":"db_id","subj":"T1","obj":"118072"},{"id":"A4","pred":"db_id","subj":"T1","obj":"7777"},{"id":"A5","pred":"db_id","subj":"T1","obj":"7878"},{"id":"A6","pred":"db_id","subj":"T1","obj":"7898"},{"id":"A7","pred":"db_id","subj":"T7","obj":"117565"},{"id":"A8","pred":"db_id","subj":"T7","obj":"117569"},{"id":"A9","pred":"db_id","subj":"T7","obj":"118072"},{"id":"A10","pred":"db_id","subj":"T7","obj":"7777"},{"id":"A11","pred":"db_id","subj":"T7","obj":"7878"},{"id":"A12","pred":"db_id","subj":"T7","obj":"7898"}],"text":"Atlantic Salmon Carries a Range of Novel O-Glycan Structures Differentially Localized on Skin and Intestinal Mucins.\nAquaculture is a growing industry, increasing the need for understanding host-pathogen interactions in fish. The skin and mucosal surfaces, covered by a mucus layer composed of mucins, is the first point of contact between fish and pathogens. Highly O-glycosylated mucins have been shown to be an important part of the defense against pathogens, and pathogens bind to host surfaces using lectin-like adhesins. However, knowledge of piscine O-glycosylation is very limited. We characterized mucin O-glycosylation of five freshwater acclimated Atlantic salmon, using mass spectrometry. Of the 109 O-glycans found, most were sialylated and differed in distribution among skin, pyloric ceca, and proximal and distal intestine. Skin O-glycans were shorter (2-6 residues) and less diverse (33 structures) than intestinal O-glycans (2-13 residues, 93 structures). Skin mucins carried O-glycan cores 1, 2, 3, and 5 and three types of sialic acids (Neu5Ac, Neu5Gc, and Kdn) and had sialyl-Tn as the predominant structure. Intestinal mucins carried only cores 1, 2, and 5, Neu5Ac was the only sialic acid present, and sialylated core 5 was the most dominant structure. This structural characterization can be used for identifying structures of putative importance in host-pathogen interactions for further testing in biological assays and disease intervention therapies."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":116},"obj":"Sentence"},{"id":"T2","span":{"begin":117,"end":225},"obj":"Sentence"},{"id":"T3","span":{"begin":226,"end":359},"obj":"Sentence"},{"id":"T4","span":{"begin":360,"end":526},"obj":"Sentence"},{"id":"T5","span":{"begin":527,"end":589},"obj":"Sentence"},{"id":"T6","span":{"begin":590,"end":700},"obj":"Sentence"},{"id":"T7","span":{"begin":701,"end":839},"obj":"Sentence"},{"id":"T8","span":{"begin":840,"end":973},"obj":"Sentence"},{"id":"T9","span":{"begin":974,"end":1129},"obj":"Sentence"},{"id":"T10","span":{"begin":1130,"end":1275},"obj":"Sentence"},{"id":"T11","span":{"begin":1276,"end":1477},"obj":"Sentence"}],"text":"Atlantic Salmon Carries a Range of Novel O-Glycan Structures Differentially Localized on Skin and Intestinal Mucins.\nAquaculture is a growing industry, increasing the need for understanding host-pathogen interactions in fish. The skin and mucosal surfaces, covered by a mucus layer composed of mucins, is the first point of contact between fish and pathogens. Highly O-glycosylated mucins have been shown to be an important part of the defense against pathogens, and pathogens bind to host surfaces using lectin-like adhesins. However, knowledge of piscine O-glycosylation is very limited. We characterized mucin O-glycosylation of five freshwater acclimated Atlantic salmon, using mass spectrometry. Of the 109 O-glycans found, most were sialylated and differed in distribution among skin, pyloric ceca, and proximal and distal intestine. Skin O-glycans were shorter (2-6 residues) and less diverse (33 structures) than intestinal O-glycans (2-13 residues, 93 structures). Skin mucins carried O-glycan cores 1, 2, 3, and 5 and three types of sialic acids (Neu5Ac, Neu5Gc, and Kdn) and had sialyl-Tn as the predominant structure. Intestinal mucins carried only cores 1, 2, and 5, Neu5Ac was the only sialic acid present, and sialylated core 5 was the most dominant structure. This structural characterization can be used for identifying structures of putative importance in host-pathogen interactions for further testing in biological assays and disease intervention therapies."}

{"project":"GlyCosmos15-FMA","denotations":[{"id":"T1","span":{"begin":89,"end":93},"obj":"Body_part"},{"id":"T2","span":{"begin":98,"end":108},"obj":"Body_part"},{"id":"T3","span":{"begin":230,"end":234},"obj":"Body_part"},{"id":"T4","span":{"begin":270,"end":275},"obj":"Body_part"},{"id":"T5","span":{"begin":785,"end":789},"obj":"Body_part"},{"id":"T6","span":{"begin":829,"end":838},"obj":"Body_part"},{"id":"T7","span":{"begin":840,"end":844},"obj":"Body_part"},{"id":"T8","span":{"begin":921,"end":931},"obj":"Body_part"},{"id":"T9","span":{"begin":974,"end":978},"obj":"Body_part"},{"id":"T10","span":{"begin":1130,"end":1140},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"FMA:7163"},{"id":"A2","pred":"db_id","subj":"T2","obj":"FMA:7199"},{"id":"A3","pred":"db_id","subj":"T3","obj":"FMA:7163"},{"id":"A4","pred":"db_id","subj":"T4","obj":"FMA:66938"},{"id":"A5","pred":"db_id","subj":"T5","obj":"FMA:7163"},{"id":"A6","pred":"db_id","subj":"T6","obj":"FMA:7199"},{"id":"A7","pred":"db_id","subj":"T7","obj":"FMA:7163"},{"id":"A8","pred":"db_id","subj":"T8","obj":"FMA:7199"},{"id":"A9","pred":"db_id","subj":"T9","obj":"FMA:7163"},{"id":"A10","pred":"db_id","subj":"T10","obj":"FMA:7199"}],"namespaces":[{"prefix":"FMA","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"Atlantic Salmon Carries a Range of Novel O-Glycan Structures Differentially Localized on Skin and Intestinal Mucins.\nAquaculture is a growing industry, increasing the need for understanding host-pathogen interactions in fish. The skin and mucosal surfaces, covered by a mucus layer composed of mucins, is the first point of contact between fish and pathogens. Highly O-glycosylated mucins have been shown to be an important part of the defense against pathogens, and pathogens bind to host surfaces using lectin-like adhesins. However, knowledge of piscine O-glycosylation is very limited. We characterized mucin O-glycosylation of five freshwater acclimated Atlantic salmon, using mass spectrometry. Of the 109 O-glycans found, most were sialylated and differed in distribution among skin, pyloric ceca, and proximal and distal intestine. Skin O-glycans were shorter (2-6 residues) and less diverse (33 structures) than intestinal O-glycans (2-13 residues, 93 structures). Skin mucins carried O-glycan cores 1, 2, 3, and 5 and three types of sialic acids (Neu5Ac, Neu5Gc, and Kdn) and had sialyl-Tn as the predominant structure. Intestinal mucins carried only cores 1, 2, and 5, Neu5Ac was the only sialic acid present, and sialylated core 5 was the most dominant structure. This structural characterization can be used for identifying structures of putative importance in host-pathogen interactions for further testing in biological assays and disease intervention therapies."}

{"project":"GlyCosmos15-MAT","denotations":[{"id":"T1","span":{"begin":89,"end":93},"obj":"Body_part"},{"id":"T2","span":{"begin":98,"end":108},"obj":"Body_part"},{"id":"T3","span":{"begin":230,"end":234},"obj":"Body_part"},{"id":"T4","span":{"begin":785,"end":789},"obj":"Body_part"},{"id":"T5","span":{"begin":809,"end":817},"obj":"Body_part"},{"id":"T6","span":{"begin":829,"end":838},"obj":"Body_part"},{"id":"T7","span":{"begin":840,"end":844},"obj":"Body_part"},{"id":"T8","span":{"begin":921,"end":931},"obj":"Body_part"},{"id":"T9","span":{"begin":974,"end":978},"obj":"Body_part"},{"id":"T10","span":{"begin":1130,"end":1140},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000284"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000043"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000284"},{"id":"A4","pred":"mat_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MAT_0000284"},{"id":"A5","pred":"mat_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/MAT_0000491"},{"id":"A6","pred":"mat_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/MAT_0000043"},{"id":"A7","pred":"mat_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/MAT_0000284"},{"id":"A8","pred":"mat_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/MAT_0000043"},{"id":"A9","pred":"mat_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/MAT_0000284"},{"id":"A10","pred":"mat_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/MAT_0000043"}],"text":"Atlantic Salmon Carries a Range of Novel O-Glycan Structures Differentially Localized on Skin and Intestinal Mucins.\nAquaculture is a growing industry, increasing the need for understanding host-pathogen interactions in fish. The skin and mucosal surfaces, covered by a mucus layer composed of mucins, is the first point of contact between fish and pathogens. Highly O-glycosylated mucins have been shown to be an important part of the defense against pathogens, and pathogens bind to host surfaces using lectin-like adhesins. However, knowledge of piscine O-glycosylation is very limited. We characterized mucin O-glycosylation of five freshwater acclimated Atlantic salmon, using mass spectrometry. Of the 109 O-glycans found, most were sialylated and differed in distribution among skin, pyloric ceca, and proximal and distal intestine. Skin O-glycans were shorter (2-6 residues) and less diverse (33 structures) than intestinal O-glycans (2-13 residues, 93 structures). Skin mucins carried O-glycan cores 1, 2, 3, and 5 and three types of sialic acids (Neu5Ac, Neu5Gc, and Kdn) and had sialyl-Tn as the predominant structure. Intestinal mucins carried only cores 1, 2, and 5, Neu5Ac was the only sialic acid present, and sialylated core 5 was the most dominant structure. This structural characterization can be used for identifying structures of putative importance in host-pathogen interactions for further testing in biological assays and disease intervention therapies."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":220,"end":224},"obj":"OrganismTaxon"},{"id":"T7","span":{"begin":340,"end":344},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"117565"},{"id":"A2","pred":"db_id","subj":"T1","obj":"117569"},{"id":"A3","pred":"db_id","subj":"T1","obj":"118072"},{"id":"A4","pred":"db_id","subj":"T1","obj":"7777"},{"id":"A5","pred":"db_id","subj":"T1","obj":"7878"},{"id":"A6","pred":"db_id","subj":"T1","obj":"7898"},{"id":"A7","pred":"db_id","subj":"T7","obj":"117565"},{"id":"A8","pred":"db_id","subj":"T7","obj":"117569"},{"id":"A9","pred":"db_id","subj":"T7","obj":"118072"},{"id":"A10","pred":"db_id","subj":"T7","obj":"7777"},{"id":"A11","pred":"db_id","subj":"T7","obj":"7878"},{"id":"A12","pred":"db_id","subj":"T7","obj":"7898"}],"text":"Atlantic Salmon Carries a Range of Novel O-Glycan Structures Differentially Localized on Skin and Intestinal Mucins.\nAquaculture is a growing industry, increasing the need for understanding host-pathogen interactions in fish. The skin and mucosal surfaces, covered by a mucus layer composed of mucins, is the first point of contact between fish and pathogens. Highly O-glycosylated mucins have been shown to be an important part of the defense against pathogens, and pathogens bind to host surfaces using lectin-like adhesins. However, knowledge of piscine O-glycosylation is very limited. We characterized mucin O-glycosylation of five freshwater acclimated Atlantic salmon, using mass spectrometry. Of the 109 O-glycans found, most were sialylated and differed in distribution among skin, pyloric ceca, and proximal and distal intestine. Skin O-glycans were shorter (2-6 residues) and less diverse (33 structures) than intestinal O-glycans (2-13 residues, 93 structures). Skin mucins carried O-glycan cores 1, 2, 3, and 5 and three types of sialic acids (Neu5Ac, Neu5Gc, and Kdn) and had sialyl-Tn as the predominant structure. Intestinal mucins carried only cores 1, 2, and 5, Neu5Ac was the only sialic acid present, and sialylated core 5 was the most dominant structure. This structural characterization can be used for identifying structures of putative importance in host-pathogen interactions for further testing in biological assays and disease intervention therapies."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":89,"end":93},"obj":"Body_part"},{"id":"T5","span":{"begin":230,"end":234},"obj":"Body_part"},{"id":"T9","span":{"begin":270,"end":275},"obj":"Body_part"},{"id":"T10","span":{"begin":276,"end":281},"obj":"Body_part"},{"id":"T12","span":{"begin":785,"end":789},"obj":"Body_part"},{"id":"T16","span":{"begin":799,"end":803},"obj":"Body_part"},{"id":"T17","span":{"begin":822,"end":838},"obj":"Body_part"},{"id":"T18","span":{"begin":840,"end":844},"obj":"Body_part"},{"id":"T22","span":{"begin":974,"end":978},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000014"},{"id":"A2","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0001003"},{"id":"A3","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0002097"},{"id":"A4","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0002199"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0000014"},{"id":"A6","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0001003"},{"id":"A7","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0002097"},{"id":"A8","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/UBERON_0002199"},{"id":"A9","pred":"uberon_id","subj":"T9","obj":"http://purl.obolibrary.org/obo/UBERON_0000912"},{"id":"A10","pred":"uberon_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/UBERON_0000119"},{"id":"A11","pred":"uberon_id","subj":"T10","obj":"http://purl.obolibrary.org/obo/UBERON_0022303"},{"id":"A12","pred":"uberon_id","subj":"T12","obj":"http://purl.obolibrary.org/obo/UBERON_0000014"},{"id":"A13","pred":"uberon_id","subj":"T12","obj":"http://purl.obolibrary.org/obo/UBERON_0001003"},{"id":"A14","pred":"uberon_id","subj":"T12","obj":"http://purl.obolibrary.org/obo/UBERON_0002097"},{"id":"A15","pred":"uberon_id","subj":"T12","obj":"http://purl.obolibrary.org/obo/UBERON_0002199"},{"id":"A16","pred":"uberon_id","subj":"T16","obj":"http://purl.obolibrary.org/obo/UBERON_0001153"},{"id":"A17","pred":"uberon_id","subj":"T17","obj":"http://purl.obolibrary.org/obo/UBERON_0002116"},{"id":"A18","pred":"uberon_id","subj":"T18","obj":"http://purl.obolibrary.org/obo/UBERON_0000014"},{"id":"A19","pred":"uberon_id","subj":"T18","obj":"http://purl.obolibrary.org/obo/UBERON_0001003"},{"id":"A20","pred":"uberon_id","subj":"T18","obj":"http://purl.obolibrary.org/obo/UBERON_0002097"},{"id":"A21","pred":"uberon_id","subj":"T18","obj":"http://purl.obolibrary.org/obo/UBERON_0002199"},{"id":"A22","pred":"uberon_id","subj":"T22","obj":"http://purl.obolibrary.org/obo/UBERON_0000014"},{"id":"A23","pred":"uberon_id","subj":"T22","obj":"http://purl.obolibrary.org/obo/UBERON_0001003"},{"id":"A24","pred":"uberon_id","subj":"T22","obj":"http://purl.obolibrary.org/obo/UBERON_0002097"},{"id":"A25","pred":"uberon_id","subj":"T22","obj":"http://purl.obolibrary.org/obo/UBERON_0002199"}],"text":"Atlantic Salmon Carries a Range of Novel O-Glycan Structures Differentially Localized on Skin and Intestinal Mucins.\nAquaculture is a growing industry, increasing the need for understanding host-pathogen interactions in fish. The skin and mucosal surfaces, covered by a mucus layer composed of mucins, is the first point of contact between fish and pathogens. Highly O-glycosylated mucins have been shown to be an important part of the defense against pathogens, and pathogens bind to host surfaces using lectin-like adhesins. However, knowledge of piscine O-glycosylation is very limited. We characterized mucin O-glycosylation of five freshwater acclimated Atlantic salmon, using mass spectrometry. Of the 109 O-glycans found, most were sialylated and differed in distribution among skin, pyloric ceca, and proximal and distal intestine. Skin O-glycans were shorter (2-6 residues) and less diverse (33 structures) than intestinal O-glycans (2-13 residues, 93 structures). Skin mucins carried O-glycan cores 1, 2, 3, and 5 and three types of sialic acids (Neu5Ac, Neu5Gc, and Kdn) and had sialyl-Tn as the predominant structure. Intestinal mucins carried only cores 1, 2, and 5, Neu5Ac was the only sialic acid present, and sialylated core 5 was the most dominant structure. This structural characterization can be used for identifying structures of putative importance in host-pathogen interactions for further testing in biological assays and disease intervention therapies."}