PubMed:19282391 JSONTXT

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":108,"end":119},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T2","span":{"begin":1304,"end":1315},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T3","span":{"begin":1430,"end":1441},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"}],"text":"The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving novel GDP-linked precursors.\nThe sialic acid-like sugar 5,7-diacetamido-3,5,7,9-tetradeoxy-D-glycero-D-galacto-nonulosonic acid, or legion-aminic acid, is found as a virulence-associated cell-surface glycoconjugate in the Gram-negative bacteria Legionella pneumophila and Campylobacter coli. L. pneumophila serogroup 1 strains, causative agents of Legionnaire's disease, contain an alpha2,4-linked homopolymer of legionaminic acid within their lipopolysaccharide O-chains, whereas the gastrointestinal pathogen C. coli modifies its flagellin with this monosaccharide via O-linkage. In this work, we have purified and biochemically characterized 11 candidate biosynthetic enzymes from Campylobacter jejuni, thereby fully reconstituting the biosynthesis of legionaminic acid and its CMP-activated form, starting from fructose-6-P. This pathway involves unique GDP-linked intermediates, likely providing a cellular mechanism for differentiating between this and similar UDP-linked pathways, such as UDP-2,4-diacetamido-bacillosamine biosynthesis involved in N-linked protein glycosylation. Importantly, these findings provide a facile method for efficient large-scale synthesis of legionaminic acid, and since legionaminic acid and sialic acid share the same D-glycero-D-galacto absolute configuration, this sugar may now be evaluated for its potential as a sialic acid mimic."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":108,"end":119},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":1304,"end":1315},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":1430,"end":1441},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G81533KY"},{"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"}],"text":"The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving novel GDP-linked precursors.\nThe sialic acid-like sugar 5,7-diacetamido-3,5,7,9-tetradeoxy-D-glycero-D-galacto-nonulosonic acid, or legion-aminic acid, is found as a virulence-associated cell-surface glycoconjugate in the Gram-negative bacteria Legionella pneumophila and Campylobacter coli. L. pneumophila serogroup 1 strains, causative agents of Legionnaire's disease, contain an alpha2,4-linked homopolymer of legionaminic acid within their lipopolysaccharide O-chains, whereas the gastrointestinal pathogen C. coli modifies its flagellin with this monosaccharide via O-linkage. In this work, we have purified and biochemically characterized 11 candidate biosynthetic enzymes from Campylobacter jejuni, thereby fully reconstituting the biosynthesis of legionaminic acid and its CMP-activated form, starting from fructose-6-P. This pathway involves unique GDP-linked intermediates, likely providing a cellular mechanism for differentiating between this and similar UDP-linked pathways, such as UDP-2,4-diacetamido-bacillosamine biosynthesis involved in N-linked protein glycosylation. Importantly, these findings provide a facile method for efficient large-scale synthesis of legionaminic acid, and since legionaminic acid and sialic acid share the same D-glycero-D-galacto absolute configuration, this sugar may now be evaluated for its potential as a sialic acid mimic."}

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":103},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":104,"end":366},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":367,"end":656},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":657,"end":903},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":904,"end":1161},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":1162,"end":1448},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":103},"obj":"Sentence"},{"id":"T2","span":{"begin":104,"end":366},"obj":"Sentence"},{"id":"T3","span":{"begin":367,"end":656},"obj":"Sentence"},{"id":"T4","span":{"begin":657,"end":1161},"obj":"Sentence"},{"id":"T5","span":{"begin":1162,"end":1448},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":103},"obj":"Sentence"},{"id":"T2","span":{"begin":104,"end":366},"obj":"Sentence"},{"id":"T3","span":{"begin":367,"end":656},"obj":"Sentence"},{"id":"T4","span":{"begin":657,"end":903},"obj":"Sentence"},{"id":"T5","span":{"begin":904,"end":1161},"obj":"Sentence"},{"id":"T6","span":{"begin":1162,"end":1448},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving novel GDP-linked precursors.\nThe sialic acid-like sugar 5,7-diacetamido-3,5,7,9-tetradeoxy-D-glycero-D-galacto-nonulosonic acid, or legion-aminic acid, is found as a virulence-associated cell-surface glycoconjugate in the Gram-negative bacteria Legionella pneumophila and Campylobacter coli. L. pneumophila serogroup 1 strains, causative agents of Legionnaire's disease, contain an alpha2,4-linked homopolymer of legionaminic acid within their lipopolysaccharide O-chains, whereas the gastrointestinal pathogen C. coli modifies its flagellin with this monosaccharide via O-linkage. In this work, we have purified and biochemically characterized 11 candidate biosynthetic enzymes from Campylobacter jejuni, thereby fully reconstituting the biosynthesis of legionaminic acid and its CMP-activated form, starting from fructose-6-P. This pathway involves unique GDP-linked intermediates, likely providing a cellular mechanism for differentiating between this and similar UDP-linked pathways, such as UDP-2,4-diacetamido-bacillosamine biosynthesis involved in N-linked protein glycosylation. Importantly, these findings provide a facile method for efficient large-scale synthesis of legionaminic acid, and since legionaminic acid and sialic acid share the same D-glycero-D-galacto absolute configuration, this sugar may now be evaluated for its potential as a sialic acid mimic."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":108,"end":119},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T2","span":{"begin":1304,"end":1315},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"},{"id":"T3","span":{"begin":1430,"end":1441},"obj":"https://glytoucan.org/Structures/Glycans/G81533KY"}],"text":"The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving novel GDP-linked precursors.\nThe sialic acid-like sugar 5,7-diacetamido-3,5,7,9-tetradeoxy-D-glycero-D-galacto-nonulosonic acid, or legion-aminic acid, is found as a virulence-associated cell-surface glycoconjugate in the Gram-negative bacteria Legionella pneumophila and Campylobacter coli. L. pneumophila serogroup 1 strains, causative agents of Legionnaire's disease, contain an alpha2,4-linked homopolymer of legionaminic acid within their lipopolysaccharide O-chains, whereas the gastrointestinal pathogen C. coli modifies its flagellin with this monosaccharide via O-linkage. In this work, we have purified and biochemically characterized 11 candidate biosynthetic enzymes from Campylobacter jejuni, thereby fully reconstituting the biosynthesis of legionaminic acid and its CMP-activated form, starting from fructose-6-P. This pathway involves unique GDP-linked intermediates, likely providing a cellular mechanism for differentiating between this and similar UDP-linked pathways, such as UDP-2,4-diacetamido-bacillosamine biosynthesis involved in N-linked protein glycosylation. Importantly, these findings provide a facile method for efficient large-scale synthesis of legionaminic acid, and since legionaminic acid and sialic acid share the same D-glycero-D-galacto absolute configuration, this sugar may now be evaluated for its potential as a sialic acid mimic."}

{"project":"GlycoBiology-PACDB","denotations":[{"id":"_T1","span":{"begin":759,"end":779},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC257,LEC564"}],"text":"The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving novel GDP-linked precursors.\nThe sialic acid-like sugar 5,7-diacetamido-3,5,7,9-tetradeoxy-D-glycero-D-galacto-nonulosonic acid, or legion-aminic acid, is found as a virulence-associated cell-surface glycoconjugate in the Gram-negative bacteria Legionella pneumophila and Campylobacter coli. L. pneumophila serogroup 1 strains, causative agents of Legionnaire's disease, contain an alpha2,4-linked homopolymer of legionaminic acid within their lipopolysaccharide O-chains, whereas the gastrointestinal pathogen C. coli modifies its flagellin with this monosaccharide via O-linkage. In this work, we have purified and biochemically characterized 11 candidate biosynthetic enzymes from Campylobacter jejuni, thereby fully reconstituting the biosynthesis of legionaminic acid and its CMP-activated form, starting from fructose-6-P. This pathway involves unique GDP-linked intermediates, likely providing a cellular mechanism for differentiating between this and similar UDP-linked pathways, such as UDP-2,4-diacetamido-bacillosamine biosynthesis involved in N-linked protein glycosylation. Importantly, these findings provide a facile method for efficient large-scale synthesis of legionaminic acid, and since legionaminic acid and sialic acid share the same D-glycero-D-galacto absolute configuration, this sugar may now be evaluated for its potential as a sialic acid mimic."}

{"project":"ICD10","denotations":[{"id":"T1","span":{"begin":423,"end":444},"obj":"http://purl.bioontology.org/ontology/ICD10/A48.1"}],"text":"The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving novel GDP-linked precursors.\nThe sialic acid-like sugar 5,7-diacetamido-3,5,7,9-tetradeoxy-D-glycero-D-galacto-nonulosonic acid, or legion-aminic acid, is found as a virulence-associated cell-surface glycoconjugate in the Gram-negative bacteria Legionella pneumophila and Campylobacter coli. L. pneumophila serogroup 1 strains, causative agents of Legionnaire's disease, contain an alpha2,4-linked homopolymer of legionaminic acid within their lipopolysaccharide O-chains, whereas the gastrointestinal pathogen C. coli modifies its flagellin with this monosaccharide via O-linkage. In this work, we have purified and biochemically characterized 11 candidate biosynthetic enzymes from Campylobacter jejuni, thereby fully reconstituting the biosynthesis of legionaminic acid and its CMP-activated form, starting from fructose-6-P. This pathway involves unique GDP-linked intermediates, likely providing a cellular mechanism for differentiating between this and similar UDP-linked pathways, such as UDP-2,4-diacetamido-bacillosamine biosynthesis involved in N-linked protein glycosylation. Importantly, these findings provide a facile method for efficient large-scale synthesis of legionaminic acid, and since legionaminic acid and sialic acid share the same D-glycero-D-galacto absolute configuration, this sugar may now be evaluated for its potential as a sialic acid mimic."}

{"project":"GlycoBiology-FMA","denotations":[{"id":"_T1","span":{"begin":125,"end":130},"obj":"FMAID:196724"},{"id":"_T2","span":{"begin":207,"end":213},"obj":"FMAID:179799"},{"id":"_T3","span":{"begin":214,"end":225},"obj":"FMAID:196728"},{"id":"_T4","span":{"begin":214,"end":225},"obj":"FMAID:82739"},{"id":"_T5","span":{"begin":262,"end":274},"obj":"FMAID:200942"},{"id":"_T6","span":{"begin":262,"end":274},"obj":"FMAID:212684"},{"id":"_T7","span":{"begin":267,"end":274},"obj":"FMAID:50594"},{"id":"_T8","span":{"begin":267,"end":274},"obj":"FMAID:146300"},{"id":"_T9","span":{"begin":275,"end":289},"obj":"FMAID:196776"},{"id":"_T10","span":{"begin":275,"end":289},"obj":"FMAID:82782"},{"id":"_T11","span":{"begin":519,"end":537},"obj":"FMAID:82785"},{"id":"_T12","span":{"begin":519,"end":537},"obj":"FMAID:196779"},{"id":"_T13","span":{"begin":519,"end":537},"obj":"FMAID:196735"},{"id":"_T14","span":{"begin":519,"end":537},"obj":"FMAID:82746"},{"id":"_T15","span":{"begin":627,"end":641},"obj":"FMAID:196730"},{"id":"_T16","span":{"begin":627,"end":641},"obj":"FMAID:82741"},{"id":"_T17","span":{"begin":944,"end":957},"obj":"FMAID:74531"},{"id":"_T18","span":{"begin":944,"end":957},"obj":"FMAID:179268"},{"id":"_T19","span":{"begin":1139,"end":1146},"obj":"FMAID:67257"},{"id":"_T20","span":{"begin":1139,"end":1146},"obj":"FMAID:165447"},{"id":"_T21","span":{"begin":1380,"end":1385},"obj":"FMAID:196724"}],"namespaces":[{"prefix":"FMAID","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving novel GDP-linked precursors.\nThe sialic acid-like sugar 5,7-diacetamido-3,5,7,9-tetradeoxy-D-glycero-D-galacto-nonulosonic acid, or legion-aminic acid, is found as a virulence-associated cell-surface glycoconjugate in the Gram-negative bacteria Legionella pneumophila and Campylobacter coli. L. pneumophila serogroup 1 strains, causative agents of Legionnaire's disease, contain an alpha2,4-linked homopolymer of legionaminic acid within their lipopolysaccharide O-chains, whereas the gastrointestinal pathogen C. coli modifies its flagellin with this monosaccharide via O-linkage. In this work, we have purified and biochemically characterized 11 candidate biosynthetic enzymes from Campylobacter jejuni, thereby fully reconstituting the biosynthesis of legionaminic acid and its CMP-activated form, starting from fructose-6-P. This pathway involves unique GDP-linked intermediates, likely providing a cellular mechanism for differentiating between this and similar UDP-linked pathways, such as UDP-2,4-diacetamido-bacillosamine biosynthesis involved in N-linked protein glycosylation. Importantly, these findings provide a facile method for efficient large-scale synthesis of legionaminic acid, and since legionaminic acid and sialic acid share the same D-glycero-D-galacto absolute configuration, this sugar may now be evaluated for its potential as a sialic acid mimic."}

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":4,"end":7},"obj":"http://www.uniprot.org/uniprot/P21941"},{"id":"T2","span":{"begin":856,"end":859},"obj":"http://www.uniprot.org/uniprot/P21941"}],"text":"The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving novel GDP-linked precursors.\nThe sialic acid-like sugar 5,7-diacetamido-3,5,7,9-tetradeoxy-D-glycero-D-galacto-nonulosonic acid, or legion-aminic acid, is found as a virulence-associated cell-surface glycoconjugate in the Gram-negative bacteria Legionella pneumophila and Campylobacter coli. L. pneumophila serogroup 1 strains, causative agents of Legionnaire's disease, contain an alpha2,4-linked homopolymer of legionaminic acid within their lipopolysaccharide O-chains, whereas the gastrointestinal pathogen C. coli modifies its flagellin with this monosaccharide via O-linkage. In this work, we have purified and biochemically characterized 11 candidate biosynthetic enzymes from Campylobacter jejuni, thereby fully reconstituting the biosynthesis of legionaminic acid and its CMP-activated form, starting from fructose-6-P. This pathway involves unique GDP-linked intermediates, likely providing a cellular mechanism for differentiating between this and similar UDP-linked pathways, such as UDP-2,4-diacetamido-bacillosamine biosynthesis involved in N-linked protein glycosylation. Importantly, these findings provide a facile method for efficient large-scale synthesis of legionaminic acid, and since legionaminic acid and sialic acid share the same D-glycero-D-galacto absolute configuration, this sugar may now be evaluated for its potential as a sialic acid mimic."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":297,"end":319},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/130805"},{"id":"T2","span":{"begin":297,"end":319},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/130804"},{"id":"T3","span":{"begin":311,"end":319},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/2"},{"id":"T4","span":{"begin":311,"end":319},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/629395"},{"id":"T5","span":{"begin":320,"end":330},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/445"},{"id":"T6","span":{"begin":320,"end":330},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/118969"},{"id":"T7","span":{"begin":320,"end":342},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/446"},{"id":"T8","span":{"begin":759,"end":779},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/197"},{"id":"T9","span":{"begin":987,"end":996},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/127244"},{"id":"T10","span":{"begin":1181,"end":1189},"obj":"http://purl.bioontology.org/ontology/STY/T033"}],"text":"The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving novel GDP-linked precursors.\nThe sialic acid-like sugar 5,7-diacetamido-3,5,7,9-tetradeoxy-D-glycero-D-galacto-nonulosonic acid, or legion-aminic acid, is found as a virulence-associated cell-surface glycoconjugate in the Gram-negative bacteria Legionella pneumophila and Campylobacter coli. L. pneumophila serogroup 1 strains, causative agents of Legionnaire's disease, contain an alpha2,4-linked homopolymer of legionaminic acid within their lipopolysaccharide O-chains, whereas the gastrointestinal pathogen C. coli modifies its flagellin with this monosaccharide via O-linkage. In this work, we have purified and biochemically characterized 11 candidate biosynthetic enzymes from Campylobacter jejuni, thereby fully reconstituting the biosynthesis of legionaminic acid and its CMP-activated form, starting from fructose-6-P. This pathway involves unique GDP-linked intermediates, likely providing a cellular mechanism for differentiating between this and similar UDP-linked pathways, such as UDP-2,4-diacetamido-bacillosamine biosynthesis involved in N-linked protein glycosylation. Importantly, these findings provide a facile method for efficient large-scale synthesis of legionaminic acid, and since legionaminic acid and sialic acid share the same D-glycero-D-galacto absolute configuration, this sugar may now be evaluated for its potential as a sialic acid mimic."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":52,"end":64},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T2","span":{"begin":814,"end":826},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T3","span":{"begin":1105,"end":1117},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T4","span":{"begin":241,"end":250},"obj":"http://purl.obolibrary.org/obo/GO_0009405"},{"id":"T5","span":{"begin":241,"end":250},"obj":"http://purl.obolibrary.org/obo/GO_0016032"},{"id":"T6","span":{"begin":978,"end":986},"obj":"http://purl.obolibrary.org/obo/GO_0007349"},{"id":"T7","span":{"begin":1139,"end":1160},"obj":"http://purl.obolibrary.org/obo/GO_0006486"},{"id":"T8","span":{"begin":1147,"end":1160},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T9","span":{"begin":1240,"end":1249},"obj":"http://purl.obolibrary.org/obo/GO_0009058"}],"text":"The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving novel GDP-linked precursors.\nThe sialic acid-like sugar 5,7-diacetamido-3,5,7,9-tetradeoxy-D-glycero-D-galacto-nonulosonic acid, or legion-aminic acid, is found as a virulence-associated cell-surface glycoconjugate in the Gram-negative bacteria Legionella pneumophila and Campylobacter coli. L. pneumophila serogroup 1 strains, causative agents of Legionnaire's disease, contain an alpha2,4-linked homopolymer of legionaminic acid within their lipopolysaccharide O-chains, whereas the gastrointestinal pathogen C. coli modifies its flagellin with this monosaccharide via O-linkage. In this work, we have purified and biochemically characterized 11 candidate biosynthetic enzymes from Campylobacter jejuni, thereby fully reconstituting the biosynthesis of legionaminic acid and its CMP-activated form, starting from fructose-6-P. This pathway involves unique GDP-linked intermediates, likely providing a cellular mechanism for differentiating between this and similar UDP-linked pathways, such as UDP-2,4-diacetamido-bacillosamine biosynthesis involved in N-linked protein glycosylation. Importantly, these findings provide a facile method for efficient large-scale synthesis of legionaminic acid, and since legionaminic acid and sialic acid share the same D-glycero-D-galacto absolute configuration, this sugar may now be evaluated for its potential as a sialic acid mimic."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":251,"end":266},"obj":"http://purl.obolibrary.org/obo/GO_0009986"},{"id":"T2","span":{"begin":262,"end":266},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T3","span":{"begin":262,"end":274},"obj":"http://purl.obolibrary.org/obo/GO_0009986"}],"text":"The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving novel GDP-linked precursors.\nThe sialic acid-like sugar 5,7-diacetamido-3,5,7,9-tetradeoxy-D-glycero-D-galacto-nonulosonic acid, or legion-aminic acid, is found as a virulence-associated cell-surface glycoconjugate in the Gram-negative bacteria Legionella pneumophila and Campylobacter coli. L. pneumophila serogroup 1 strains, causative agents of Legionnaire's disease, contain an alpha2,4-linked homopolymer of legionaminic acid within their lipopolysaccharide O-chains, whereas the gastrointestinal pathogen C. coli modifies its flagellin with this monosaccharide via O-linkage. In this work, we have purified and biochemically characterized 11 candidate biosynthetic enzymes from Campylobacter jejuni, thereby fully reconstituting the biosynthesis of legionaminic acid and its CMP-activated form, starting from fructose-6-P. This pathway involves unique GDP-linked intermediates, likely providing a cellular mechanism for differentiating between this and similar UDP-linked pathways, such as UDP-2,4-diacetamido-bacillosamine biosynthesis involved in N-linked protein glycosylation. Importantly, these findings provide a facile method for efficient large-scale synthesis of legionaminic acid, and since legionaminic acid and sialic acid share the same D-glycero-D-galacto absolute configuration, this sugar may now be evaluated for its potential as a sialic acid mimic."}

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":1234,"end":1239},"obj":"http://purl.obolibrary.org/obo/UBERON_0002542"}],"text":"The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving novel GDP-linked precursors.\nThe sialic acid-like sugar 5,7-diacetamido-3,5,7,9-tetradeoxy-D-glycero-D-galacto-nonulosonic acid, or legion-aminic acid, is found as a virulence-associated cell-surface glycoconjugate in the Gram-negative bacteria Legionella pneumophila and Campylobacter coli. L. pneumophila serogroup 1 strains, causative agents of Legionnaire's disease, contain an alpha2,4-linked homopolymer of legionaminic acid within their lipopolysaccharide O-chains, whereas the gastrointestinal pathogen C. coli modifies its flagellin with this monosaccharide via O-linkage. In this work, we have purified and biochemically characterized 11 candidate biosynthetic enzymes from Campylobacter jejuni, thereby fully reconstituting the biosynthesis of legionaminic acid and its CMP-activated form, starting from fructose-6-P. This pathway involves unique GDP-linked intermediates, likely providing a cellular mechanism for differentiating between this and similar UDP-linked pathways, such as UDP-2,4-diacetamido-bacillosamine biosynthesis involved in N-linked protein glycosylation. Importantly, these findings provide a facile method for efficient large-scale synthesis of legionaminic acid, and since legionaminic acid and sialic acid share the same D-glycero-D-galacto absolute configuration, this sugar may now be evaluated for its potential as a sialic acid mimic."}

{"project":"GlyTouCan-IUPAC","denotations":[{"id":"GlycanIUPAC_T1","span":{"begin":125,"end":130},"obj":"\"http://rdf.glycoinfo.org/glycan/G59665TO\""},{"id":"GlycanIUPAC_T2","span":{"begin":1380,"end":1385},"obj":"\"http://rdf.glycoinfo.org/glycan/G59665TO\""},{"id":"GlycanIUPAC_T3","span":{"begin":125,"end":130},"obj":"\"http://rdf.glycoinfo.org/glycan/G32915EI\""},{"id":"GlycanIUPAC_T4","span":{"begin":1380,"end":1385},"obj":"\"http://rdf.glycoinfo.org/glycan/G32915EI\""},{"id":"GlycanIUPAC_T5","span":{"begin":125,"end":130},"obj":"\"http://rdf.glycoinfo.org/glycan/G60625TS\""},{"id":"GlycanIUPAC_T6","span":{"begin":1380,"end":1385},"obj":"\"http://rdf.glycoinfo.org/glycan/G60625TS\""}],"text":"The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving novel GDP-linked precursors.\nThe sialic acid-like sugar 5,7-diacetamido-3,5,7,9-tetradeoxy-D-glycero-D-galacto-nonulosonic acid, or legion-aminic acid, is found as a virulence-associated cell-surface glycoconjugate in the Gram-negative bacteria Legionella pneumophila and Campylobacter coli. L. pneumophila serogroup 1 strains, causative agents of Legionnaire's disease, contain an alpha2,4-linked homopolymer of legionaminic acid within their lipopolysaccharide O-chains, whereas the gastrointestinal pathogen C. coli modifies its flagellin with this monosaccharide via O-linkage. In this work, we have purified and biochemically characterized 11 candidate biosynthetic enzymes from Campylobacter jejuni, thereby fully reconstituting the biosynthesis of legionaminic acid and its CMP-activated form, starting from fructose-6-P. This pathway involves unique GDP-linked intermediates, likely providing a cellular mechanism for differentiating between this and similar UDP-linked pathways, such as UDP-2,4-diacetamido-bacillosamine biosynthesis involved in N-linked protein glycosylation. Importantly, these findings provide a facile method for efficient large-scale synthesis of legionaminic acid, and since legionaminic acid and sialic acid share the same D-glycero-D-galacto absolute configuration, this sugar may now be evaluated for its potential as a sialic acid mimic."}

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":1234,"end":1239},"obj":"http://purl.obolibrary.org/obo/UBERON_0002542"}],"text":"The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving novel GDP-linked precursors.\nThe sialic acid-like sugar 5,7-diacetamido-3,5,7,9-tetradeoxy-D-glycero-D-galacto-nonulosonic acid, or legion-aminic acid, is found as a virulence-associated cell-surface glycoconjugate in the Gram-negative bacteria Legionella pneumophila and Campylobacter coli. L. pneumophila serogroup 1 strains, causative agents of Legionnaire's disease, contain an alpha2,4-linked homopolymer of legionaminic acid within their lipopolysaccharide O-chains, whereas the gastrointestinal pathogen C. coli modifies its flagellin with this monosaccharide via O-linkage. In this work, we have purified and biochemically characterized 11 candidate biosynthetic enzymes from Campylobacter jejuni, thereby fully reconstituting the biosynthesis of legionaminic acid and its CMP-activated form, starting from fructose-6-P. This pathway involves unique GDP-linked intermediates, likely providing a cellular mechanism for differentiating between this and similar UDP-linked pathways, such as UDP-2,4-diacetamido-bacillosamine biosynthesis involved in N-linked protein glycosylation. Importantly, these findings provide a facile method for efficient large-scale synthesis of legionaminic acid, and since legionaminic acid and sialic acid share the same D-glycero-D-galacto absolute configuration, this sugar may now be evaluated for its potential as a sialic acid mimic."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":320,"end":330},"obj":"Disease"},{"id":"T2","span":{"begin":423,"end":444},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0005824"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0005824"}],"text":"The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving novel GDP-linked precursors.\nThe sialic acid-like sugar 5,7-diacetamido-3,5,7,9-tetradeoxy-D-glycero-D-galacto-nonulosonic acid, or legion-aminic acid, is found as a virulence-associated cell-surface glycoconjugate in the Gram-negative bacteria Legionella pneumophila and Campylobacter coli. L. pneumophila serogroup 1 strains, causative agents of Legionnaire's disease, contain an alpha2,4-linked homopolymer of legionaminic acid within their lipopolysaccharide O-chains, whereas the gastrointestinal pathogen C. coli modifies its flagellin with this monosaccharide via O-linkage. In this work, we have purified and biochemically characterized 11 candidate biosynthetic enzymes from Campylobacter jejuni, thereby fully reconstituting the biosynthesis of legionaminic acid and its CMP-activated form, starting from fructose-6-P. This pathway involves unique GDP-linked intermediates, likely providing a cellular mechanism for differentiating between this and similar UDP-linked pathways, such as UDP-2,4-diacetamido-bacillosamine biosynthesis involved in N-linked protein glycosylation. Importantly, these findings provide a facile method for efficient large-scale synthesis of legionaminic acid, and since legionaminic acid and sialic acid share the same D-glycero-D-galacto absolute configuration, this sugar may now be evaluated for its potential as a sialic acid mimic."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":37,"end":50},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":311,"end":319},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":320,"end":342},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":347,"end":365},"obj":"OrganismTaxon"},{"id":"T6","span":{"begin":759,"end":779},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"194"},{"id":"A2","pred":"db_id","subj":"T2","obj":"2"},{"id":"A3","pred":"db_id","subj":"T2","obj":"629395"},{"id":"A4","pred":"db_id","subj":"T4","obj":"446"},{"id":"A5","pred":"db_id","subj":"T5","obj":"195"},{"id":"A6","pred":"db_id","subj":"T6","obj":"197"}],"text":"The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving novel GDP-linked precursors.\nThe sialic acid-like sugar 5,7-diacetamido-3,5,7,9-tetradeoxy-D-glycero-D-galacto-nonulosonic acid, or legion-aminic acid, is found as a virulence-associated cell-surface glycoconjugate in the Gram-negative bacteria Legionella pneumophila and Campylobacter coli. L. pneumophila serogroup 1 strains, causative agents of Legionnaire's disease, contain an alpha2,4-linked homopolymer of legionaminic acid within their lipopolysaccharide O-chains, whereas the gastrointestinal pathogen C. coli modifies its flagellin with this monosaccharide via O-linkage. In this work, we have purified and biochemically characterized 11 candidate biosynthetic enzymes from Campylobacter jejuni, thereby fully reconstituting the biosynthesis of legionaminic acid and its CMP-activated form, starting from fructose-6-P. This pathway involves unique GDP-linked intermediates, likely providing a cellular mechanism for differentiating between this and similar UDP-linked pathways, such as UDP-2,4-diacetamido-bacillosamine biosynthesis involved in N-linked protein glycosylation. Importantly, these findings provide a facile method for efficient large-scale synthesis of legionaminic acid, and since legionaminic acid and sialic acid share the same D-glycero-D-galacto absolute configuration, this sugar may now be evaluated for its potential as a sialic acid mimic."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":1234,"end":1239},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0002542"}],"text":"The CMP-legionaminic acid pathway in Campylobacter: biosynthesis involving novel GDP-linked precursors.\nThe sialic acid-like sugar 5,7-diacetamido-3,5,7,9-tetradeoxy-D-glycero-D-galacto-nonulosonic acid, or legion-aminic acid, is found as a virulence-associated cell-surface glycoconjugate in the Gram-negative bacteria Legionella pneumophila and Campylobacter coli. L. pneumophila serogroup 1 strains, causative agents of Legionnaire's disease, contain an alpha2,4-linked homopolymer of legionaminic acid within their lipopolysaccharide O-chains, whereas the gastrointestinal pathogen C. coli modifies its flagellin with this monosaccharide via O-linkage. In this work, we have purified and biochemically characterized 11 candidate biosynthetic enzymes from Campylobacter jejuni, thereby fully reconstituting the biosynthesis of legionaminic acid and its CMP-activated form, starting from fructose-6-P. This pathway involves unique GDP-linked intermediates, likely providing a cellular mechanism for differentiating between this and similar UDP-linked pathways, such as UDP-2,4-diacetamido-bacillosamine biosynthesis involved in N-linked protein glycosylation. Importantly, these findings provide a facile method for efficient large-scale synthesis of legionaminic acid, and since legionaminic acid and sialic acid share the same D-glycero-D-galacto absolute configuration, this sugar may now be evaluated for its potential as a sialic acid mimic."}