BB-rel@ldeleger:BB-rel-24837294 JSONTXT

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bionlp-ost-19-BB-rel-test

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Id Subject Object Predicate Lexical cue
T1 0-115 Title denotes Modification of Streptococcus mutans Cnm by PgfS contributes to adhesion, endothelial cell invasion, and virulence.
T3 16-36 Microorganism denotes Streptococcus mutans
T4 64-72 Phenotype denotes adhesion
T6 74-90 Habitat denotes endothelial cell
T5 74-85 Habitat denotes endothelial
T7 105-114 Phenotype denotes virulence
T2 116-1926 Paragraph denotes Expression of the surface protein Cnm has been directly implicated in the ability of certain strains of Streptococcus mutans to bind to collagen and to invade human coronary artery endothelial cells (HCAEC) and in the killing of Galleria mellonella. Sequencing analysis of Cnm(+) strains revealed that cnm is located between the core genes SMU.2067 and SMU.2069. Reverse transcription-PCR (RT-PCR) analysis showed that cnm is cotranscribed with SMU.2067, encoding a putative glycosyltransferase referred to here as PgfS (protein glycosyltransferase of streptococci). Notably, Cnm contains a threonine-rich domain predicted to undergo O-linked glycosylation. The previously shown abnormal migration pattern of Cnm, the presence of the threonine-rich domain, and the molecular linkage of cnm with pgfS lead us to hypothesize that PgfS modifies Cnm. A ΔpgfS strain showed defects in several traits associated with Cnm expression, including collagen binding, HCAEC invasion, and killing of G. mellonella. Western blot analysis revealed that Cnm from the ΔpgfS mutant migrated at a lower molecular weight than that from the parent strain. In addition, Cnm produced by ΔpgfS was highly susceptible to proteinase K degradation, in contrast to the high-molecular-weight Cnm version found in the parent strain. Lectin-binding analyses confirmed the glycosylated nature of Cnm and strongly suggested the presence of N-acetylglucosamine residues attached to Cnm. Based on these findings, the phenotypes observed in ΔpgfS are most likely associated with defects in Cnm glycosylation that affects protein function, stability, or both. In conclusion, this study demonstrates that Cnm is a glycoprotein and that posttranslational modification mediated by PgfS contributes to the virulence-associated phenotypes linked to Cnm.
T8-0 190-197 _FRAGMENT denotes ability
T8-1 241-248 Phenotype denotes to bind
T9 220-240 Microorganism denotes Streptococcus mutans
T11 275-314 Habitat denotes human coronary artery endothelial cells
T10 275-280 Habitat denotes human
T12 281-296 Habitat denotes coronary artery
T13 297-308 Habitat denotes endothelial
T14 316-321 Habitat denotes HCAEC
T15 334-341 Phenotype denotes killing
T16 345-364 Habitat denotes Galleria mellonella
T17 668-680 Microorganism denotes streptococci
T18 965-970 Microorganism denotes ΔpgfS
T19 1053-1069 Phenotype denotes collagen binding
T20 1071-1076 Habitat denotes HCAEC
T21 1091-1098 Phenotype denotes killing
T22 1102-1115 Habitat denotes G. mellonella
T23 1166-1171 Microorganism denotes ΔpgfS
T24 1172-1178 Phenotype denotes mutant
T25 1279-1284 Microorganism denotes ΔpgfS
T26 1620-1625 Microorganism denotes ΔpgfS
T27 1658-1686 Phenotype denotes defects in Cnm glycosylation
T28 1880-1889 Phenotype denotes virulence
C-T8-0 T8-1 T8-0 _lexicallyChainedTo to bind,ability