PubMed:21768350 JSON TXT

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LitCoin-PubTator-for-Tuning

LitCoin-Disease-Tuning-1

{"project":"LitCoin-Disease-Tuning-1","denotations":[{"id":"T1","span":{"begin":350,"end":359},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T2","span":{"begin":533,"end":540},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T3","span":{"begin":870,"end":882},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T5","span":{"begin":1077,"end":1089},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T7","span":{"begin":1094,"end":1104},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T8","span":{"begin":1324,"end":1329},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T9","span":{"begin":1413,"end":1423},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T10","span":{"begin":1511,"end":1531},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T11","span":{"begin":1577,"end":1589},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T13","span":{"begin":1606,"end":1612},"obj":"DiseaseOrPhenotypicFeature"}],"attributes":[{"id":"A7","pred":"ID:","subj":"T7","obj":"D009369"},{"id":"A5","pred":"ID:","subj":"T5","obj":"DISEASE"},{"id":"A6","pred":"ID:","subj":"T5","obj":"D007249"},{"id":"A1","pred":"ID:","subj":"T1","obj":"DISEASE"},{"id":"A8","pred":"ID:","subj":"T8","obj":"D003643"},{"id":"A13","pred":"ID:","subj":"T13","obj":"D013180"},{"id":"A9","pred":"ID:","subj":"T9","obj":"D007239"},{"id":"A11","pred":"ID:","subj":"T11","obj":"DISEASE"},{"id":"A12","pred":"ID:","subj":"T11","obj":"D007249"},{"id":"A2","pred":"ID:","subj":"T2","obj":"D013180"},{"id":"A3","pred":"ID:","subj":"T3","obj":"DISEASE"},{"id":"A4","pred":"ID:","subj":"T3","obj":"D007249"},{"id":"A10","pred":"ID:","subj":"T10","obj":"D007637"}],"text":"Serine protease autotransporters from Shigella flexneri and pathogenic Escherichia coli target a broad range of leukocyte glycoproteins.\nThe serine protease autotransporters of Enterobacteriaceae (SPATEs) are secreted by pathogenic Gram-negative bacteria through the autotransporter pathway. We previously classified SPATE proteins into two classes: cytotoxic (class 1) and noncytotoxic (class 2). Here, we show that Pic, a class 2 SPATE protein produced by Shigella flexneri 2a, uropathogenic and enteroaggregative Escherichia coli strains, targets a broad range of human leukocyte adhesion proteins. Substrate specificity was restricted to glycoproteins rich in O-linked glycans, including CD43, CD44, CD45, CD93, CD162 (PSGL-1; P-selectin glycoprotein ligand 1), and the surface-attached chemokine fractalkine, all implicated in leukocyte trafficking, migration, and inflammation. N-terminal sequencing of proteolytic products revealed Pic (protease involved in colonization) cleavage sites to occur before Thr or Ser residues. The purified carbohydrate sLewis-X implied in inflammation and malignancy inhibited cleavage of PSGL-1 by Pic. Exposure of human leukocytes to purified Pic resulted in polymorphonuclear cell activation, but impaired chemotaxis and transmigration; Pic-treated T cells underwent programmed cell death. We also show that the Pic-related protease Tsh/Hbp, implicated in extraintestinal infections, exhibited a spectrum of substrates similar to those cleaved by Pic. In the guinea pig keratoconjunctivitis model, a Shigella pic mutant induced greater inflammation than its parent strain. We suggest that the class-2 SPATEs represent unique immune-modulating bacterial virulence factors."}

LitEisuke

{"project":"LitEisuke","denotations":[{"id":"T1","span":{"begin":350,"end":359},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T2","span":{"begin":870,"end":882},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T3","span":{"begin":1077,"end":1089},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T4","span":{"begin":1094,"end":1104},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T5","span":{"begin":1511,"end":1531},"obj":"DiseaseOrPhenotypicFeature"},{"id":"T6","span":{"begin":1577,"end":1589},"obj":"DiseaseOrPhenotypicFeature"}],"attributes":[{"id":"A2","pred":"#label","subj":"T2","obj":"D007249"},{"id":"A6","pred":"#label","subj":"T6","obj":"D007249"},{"id":"A3","pred":"#label","subj":"T3","obj":"D007249"},{"id":"A5","pred":"#label","subj":"T5","obj":"D007637"},{"id":"A4","pred":"#label","subj":"T4","obj":"D009369"},{"id":"A1","pred":"#label","subj":"T1","obj":"DISEASE"}],"text":"Serine protease autotransporters from Shigella flexneri and pathogenic Escherichia coli target a broad range of leukocyte glycoproteins.\nThe serine protease autotransporters of Enterobacteriaceae (SPATEs) are secreted by pathogenic Gram-negative bacteria through the autotransporter pathway. We previously classified SPATE proteins into two classes: cytotoxic (class 1) and noncytotoxic (class 2). Here, we show that Pic, a class 2 SPATE protein produced by Shigella flexneri 2a, uropathogenic and enteroaggregative Escherichia coli strains, targets a broad range of human leukocyte adhesion proteins. Substrate specificity was restricted to glycoproteins rich in O-linked glycans, including CD43, CD44, CD45, CD93, CD162 (PSGL-1; P-selectin glycoprotein ligand 1), and the surface-attached chemokine fractalkine, all implicated in leukocyte trafficking, migration, and inflammation. N-terminal sequencing of proteolytic products revealed Pic (protease involved in colonization) cleavage sites to occur before Thr or Ser residues. The purified carbohydrate sLewis-X implied in inflammation and malignancy inhibited cleavage of PSGL-1 by Pic. Exposure of human leukocytes to purified Pic resulted in polymorphonuclear cell activation, but impaired chemotaxis and transmigration; Pic-treated T cells underwent programmed cell death. We also show that the Pic-related protease Tsh/Hbp, implicated in extraintestinal infections, exhibited a spectrum of substrates similar to those cleaved by Pic. In the guinea pig keratoconjunctivitis model, a Shigella pic mutant induced greater inflammation than its parent strain. We suggest that the class-2 SPATEs represent unique immune-modulating bacterial virulence factors."}

Inflammaging

{"project":"Inflammaging","denotations":[{"id":"T1","span":{"begin":0,"end":136},"obj":"Sentence"},{"id":"T2","span":{"begin":137,"end":291},"obj":"Sentence"},{"id":"T3","span":{"begin":292,"end":397},"obj":"Sentence"},{"id":"T4","span":{"begin":398,"end":601},"obj":"Sentence"},{"id":"T5","span":{"begin":602,"end":883},"obj":"Sentence"},{"id":"T6","span":{"begin":884,"end":1030},"obj":"Sentence"},{"id":"T7","span":{"begin":1031,"end":1141},"obj":"Sentence"},{"id":"T8","span":{"begin":1142,"end":1330},"obj":"Sentence"},{"id":"T9","span":{"begin":1331,"end":1492},"obj":"Sentence"},{"id":"T10","span":{"begin":1493,"end":1613},"obj":"Sentence"},{"id":"T11","span":{"begin":1614,"end":1712},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":136},"obj":"Sentence"},{"id":"T2","span":{"begin":137,"end":291},"obj":"Sentence"},{"id":"T3","span":{"begin":292,"end":397},"obj":"Sentence"},{"id":"T4","span":{"begin":398,"end":601},"obj":"Sentence"},{"id":"T5","span":{"begin":602,"end":883},"obj":"Sentence"},{"id":"T6","span":{"begin":884,"end":1030},"obj":"Sentence"},{"id":"T7","span":{"begin":1031,"end":1141},"obj":"Sentence"},{"id":"T8","span":{"begin":1142,"end":1330},"obj":"Sentence"},{"id":"T9","span":{"begin":1331,"end":1492},"obj":"Sentence"},{"id":"T10","span":{"begin":1493,"end":1613},"obj":"Sentence"},{"id":"T11","span":{"begin":1614,"end":1712},"obj":"Sentence"}],"text":"Serine protease autotransporters from Shigella flexneri and pathogenic Escherichia coli target a broad range of leukocyte glycoproteins.\nThe serine protease autotransporters of Enterobacteriaceae (SPATEs) are secreted by pathogenic Gram-negative bacteria through the autotransporter pathway. We previously classified SPATE proteins into two classes: cytotoxic (class 1) and noncytotoxic (class 2). Here, we show that Pic, a class 2 SPATE protein produced by Shigella flexneri 2a, uropathogenic and enteroaggregative Escherichia coli strains, targets a broad range of human leukocyte adhesion proteins. Substrate specificity was restricted to glycoproteins rich in O-linked glycans, including CD43, CD44, CD45, CD93, CD162 (PSGL-1; P-selectin glycoprotein ligand 1), and the surface-attached chemokine fractalkine, all implicated in leukocyte trafficking, migration, and inflammation. N-terminal sequencing of proteolytic products revealed Pic (protease involved in colonization) cleavage sites to occur before Thr or Ser residues. The purified carbohydrate sLewis-X implied in inflammation and malignancy inhibited cleavage of PSGL-1 by Pic. Exposure of human leukocytes to purified Pic resulted in polymorphonuclear cell activation, but impaired chemotaxis and transmigration; Pic-treated T cells underwent programmed cell death. We also show that the Pic-related protease Tsh/Hbp, implicated in extraintestinal infections, exhibited a spectrum of substrates similar to those cleaved by Pic. In the guinea pig keratoconjunctivitis model, a Shigella pic mutant induced greater inflammation than its parent strain. We suggest that the class-2 SPATEs represent unique immune-modulating bacterial virulence factors."}

DisGeNET

{"project":"DisGeNET","denotations":[{"id":"T0","span":{"begin":1127,"end":1133},"obj":"gene:6404"},{"id":"T1","span":{"begin":1094,"end":1104},"obj":"disease:C0006826"},{"id":"T2","span":{"begin":1127,"end":1133},"obj":"gene:6404"},{"id":"T3","span":{"begin":1094,"end":1104},"obj":"disease:C1306459"}],"relations":[{"id":"R1","pred":"associated_with","subj":"T0","obj":"T1"},{"id":"R2","pred":"associated_with","subj":"T2","obj":"T3"}],"namespaces":[{"prefix":"gene","uri":"http://www.ncbi.nlm.nih.gov/gene/"},{"prefix":"disease","uri":"http://purl.bioontology.org/ontology/MEDLINEPLUS/"}],"text":"Serine protease autotransporters from Shigella flexneri and pathogenic Escherichia coli target a broad range of leukocyte glycoproteins.\nThe serine protease autotransporters of Enterobacteriaceae (SPATEs) are secreted by pathogenic Gram-negative bacteria through the autotransporter pathway. We previously classified SPATE proteins into two classes: cytotoxic (class 1) and noncytotoxic (class 2). Here, we show that Pic, a class 2 SPATE protein produced by Shigella flexneri 2a, uropathogenic and enteroaggregative Escherichia coli strains, targets a broad range of human leukocyte adhesion proteins. Substrate specificity was restricted to glycoproteins rich in O-linked glycans, including CD43, CD44, CD45, CD93, CD162 (PSGL-1; P-selectin glycoprotein ligand 1), and the surface-attached chemokine fractalkine, all implicated in leukocyte trafficking, migration, and inflammation. N-terminal sequencing of proteolytic products revealed Pic (protease involved in colonization) cleavage sites to occur before Thr or Ser residues. The purified carbohydrate sLewis-X implied in inflammation and malignancy inhibited cleavage of PSGL-1 by Pic. Exposure of human leukocytes to purified Pic resulted in polymorphonuclear cell activation, but impaired chemotaxis and transmigration; Pic-treated T cells underwent programmed cell death. We also show that the Pic-related protease Tsh/Hbp, implicated in extraintestinal infections, exhibited a spectrum of substrates similar to those cleaved by Pic. In the guinea pig keratoconjunctivitis model, a Shigella pic mutant induced greater inflammation than its parent strain. We suggest that the class-2 SPATEs represent unique immune-modulating bacterial virulence factors."}

Allie

{"project":"Allie","denotations":[{"id":"SS1_21768350_1_0","span":{"begin":141,"end":195},"obj":"expanded"},{"id":"SS2_21768350_1_0","span":{"begin":197,"end":203},"obj":"abbr"}],"relations":[{"id":"AE1_21768350_1_0","pred":"abbreviatedTo","subj":"SS1_21768350_1_0","obj":"SS2_21768350_1_0"}],"text":"Serine protease autotransporters from Shigella flexneri and pathogenic Escherichia coli target a broad range of leukocyte glycoproteins.\nThe serine protease autotransporters of Enterobacteriaceae (SPATEs) are secreted by pathogenic Gram-negative bacteria through the autotransporter pathway. We previously classified SPATE proteins into two classes: cytotoxic (class 1) and noncytotoxic (class 2). Here, we show that Pic, a class 2 SPATE protein produced by Shigella flexneri 2a, uropathogenic and enteroaggregative Escherichia coli strains, targets a broad range of human leukocyte adhesion proteins. Substrate specificity was restricted to glycoproteins rich in O-linked glycans, including CD43, CD44, CD45, CD93, CD162 (PSGL-1; P-selectin glycoprotein ligand 1), and the surface-attached chemokine fractalkine, all implicated in leukocyte trafficking, migration, and inflammation. N-terminal sequencing of proteolytic products revealed Pic (protease involved in colonization) cleavage sites to occur before Thr or Ser residues. The purified carbohydrate sLewis-X implied in inflammation and malignancy inhibited cleavage of PSGL-1 by Pic. Exposure of human leukocytes to purified Pic resulted in polymorphonuclear cell activation, but impaired chemotaxis and transmigration; Pic-treated T cells underwent programmed cell death. We also show that the Pic-related protease Tsh/Hbp, implicated in extraintestinal infections, exhibited a spectrum of substrates similar to those cleaved by Pic. In the guinea pig keratoconjunctivitis model, a Shigella pic mutant induced greater inflammation than its parent strain. We suggest that the class-2 SPATEs represent unique immune-modulating bacterial virulence factors."}