PubMed:18180300
Annnotations
PubMed_ArguminSci
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 141-368 | DRI_Challenge | denotes | Serum opacity factor (SOF) is a unique multifunctional virulence determinant expressed at the surface of Streptococcus pyogenes and has been shown to elicit protective immunity against GAS infection in a murine challenge model. |
| T2 | 369-560 | DRI_Approach | denotes | SOF consists of two distinct domains with different binding capacities: an N-terminal domain that binds apolipoprotein AI and a C-terminal repeat domain that binds fibronectin and fibrinogen. |
| T3 | 561-707 | DRI_Approach | denotes | The capacity of SOF to opacify serum by disrupting the structure of high density lipoproteins may preclude its use as a vaccine antigen in humans. |
| T4 | 708-856 | DRI_Approach | denotes | This study generated mutant forms of recombinant SOF with reduced (100-fold) or abrogated opacity factor (OF) activity, for use as vaccine antigens. |
| T5 | 857-1077 | DRI_Approach | denotes | However, alterations introduced into the N-terminal SOF peptide (SOFDeltaFn) by mutagenesis to abrogate OF activity, abolish the capacity of SOF to protect against lethal systemic S. pyogenes challenge in a murine model. |
| T6 | 1078-1242 | DRI_Background | denotes | Mutant forms of purified SOFDeltaFn peptide were also used to assess the contribution of OF activity to the pathogenic processes of cell adhesion and cell invasion. |
| T7 | 1243-1451 | DRI_Approach | denotes | Using latex beads coated with full-length SOF, SOFDeltaFn peptide, or a peptide encompassing the C-terminal repeats (FnBD), we demonstrate that adhesion to HEp-2 cells is mediated by both SOFDeltaFn and FnBD. |
| T8 | 1452-1552 | DRI_Background | denotes | The HEp-2 cell binding displayed by the N-terminal SOFDeltaFn peptide is independent of OF activity. |
| T9 | 1553-1774 | DRI_Outcome | denotes | We demonstrate that while the N terminus of SOF does not directly mediate intracellular uptake by epithelial cells, this domain enhances epithelial cell uptake mediated by full-length SOF, in comparison to the FnBD alone. |
sentences
| Id | Subject | Object | Predicate | Lexical cue |
|---|---|---|---|---|
| T1 | 0-140 | Sentence | denotes | Opacity factor activity and epithelial cell binding by the serum opacity factor protein of Streptococcus pyogenes are functionally discrete. |
| T2 | 141-368 | Sentence | denotes | Serum opacity factor (SOF) is a unique multifunctional virulence determinant expressed at the surface of Streptococcus pyogenes and has been shown to elicit protective immunity against GAS infection in a murine challenge model. |
| T3 | 369-560 | Sentence | denotes | SOF consists of two distinct domains with different binding capacities: an N-terminal domain that binds apolipoprotein AI and a C-terminal repeat domain that binds fibronectin and fibrinogen. |
| T4 | 561-707 | Sentence | denotes | The capacity of SOF to opacify serum by disrupting the structure of high density lipoproteins may preclude its use as a vaccine antigen in humans. |
| T5 | 708-856 | Sentence | denotes | This study generated mutant forms of recombinant SOF with reduced (100-fold) or abrogated opacity factor (OF) activity, for use as vaccine antigens. |
| T6 | 857-1077 | Sentence | denotes | However, alterations introduced into the N-terminal SOF peptide (SOFDeltaFn) by mutagenesis to abrogate OF activity, abolish the capacity of SOF to protect against lethal systemic S. pyogenes challenge in a murine model. |
| T7 | 1078-1242 | Sentence | denotes | Mutant forms of purified SOFDeltaFn peptide were also used to assess the contribution of OF activity to the pathogenic processes of cell adhesion and cell invasion. |
| T8 | 1243-1451 | Sentence | denotes | Using latex beads coated with full-length SOF, SOFDeltaFn peptide, or a peptide encompassing the C-terminal repeats (FnBD), we demonstrate that adhesion to HEp-2 cells is mediated by both SOFDeltaFn and FnBD. |
| T9 | 1452-1552 | Sentence | denotes | The HEp-2 cell binding displayed by the N-terminal SOFDeltaFn peptide is independent of OF activity. |
| T10 | 1553-1774 | Sentence | denotes | We demonstrate that while the N terminus of SOF does not directly mediate intracellular uptake by epithelial cells, this domain enhances epithelial cell uptake mediated by full-length SOF, in comparison to the FnBD alone. |
mondo_disease
| Id | Subject | Object | Predicate | Lexical cue | mondo_id |
|---|---|---|---|---|---|
| T1 | 330-339 | Disease | denotes | infection | http://purl.obolibrary.org/obo/MONDO_0005550 |
NCBITAXON
| Id | Subject | Object | Predicate | Lexical cue | db_id |
|---|---|---|---|---|---|
| T1 | 91-113 | OrganismTaxon | denotes | Streptococcus pyogenes | 1314 |
| T2 | 246-268 | OrganismTaxon | denotes | Streptococcus pyogenes | 1314 |
Anatomy-UBERON
| Id | Subject | Object | Predicate | Lexical cue | uberon_id |
|---|---|---|---|---|---|
| T1 | 28-43 | Body_part | denotes | epithelial cell | http://purl.obolibrary.org/obo/CL_0000066 |
| T2 | 1627-1640 | Body_part | denotes | intracellular | http://purl.obolibrary.org/obo/GO_0005622 |
| T3 | 1651-1667 | Body_part | denotes | epithelial cells | http://purl.obolibrary.org/obo/CL_0000066 |
| T4 | 1690-1705 | Body_part | denotes | epithelial cell | http://purl.obolibrary.org/obo/CL_0000066 |
CL-cell
| Id | Subject | Object | Predicate | Lexical cue | cl_id |
|---|---|---|---|---|---|
| T1 | 28-43 | Cell | denotes | epithelial cell | http://purl.obolibrary.org/obo/CL:0000066 |
| T2 | 1651-1667 | Cell | denotes | epithelial cells | http://purl.obolibrary.org/obo/CL:0000066 |
| T3 | 1690-1705 | Cell | denotes | epithelial cell | http://purl.obolibrary.org/obo/CL:0000066 |