| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-122 |
Sentence |
denotes |
Autodisplay: functional display of active beta-lactamase on the surface of Escherichia coli by the AIDA-I autotransporter. |
| T2 |
123-414 |
Sentence |
denotes |
Members of the protein family of immunoglobulin A1 protease-like autotransporters comprise multidomain precursors consisting of a C-terminal autotransporter domain that promotes the translocation of N-terminally attached passenger domains across the cell envelopes of gram-negative bacteria. |
| T3 |
415-615 |
Sentence |
denotes |
Several autotransporter domains have recently been shown to efficiently promote the export of heterologous passenger domains, opening up an effective tool for surface display of heterologous proteins. |
| T4 |
616-886 |
Sentence |
denotes |
Here we report on the autotransporter domain of the Escherichia coli adhesin involved in diffuse adherence (AIDA-I), which was genetically fused to the C terminus of the periplasmic enzyme beta-lactamase, leading to efficient expression of the fusion protein in E. coli. |
| T5 |
887-1070 |
Sentence |
denotes |
The beta-lactamase moiety of the fusion protein was presented on the bacterial surface in a stable manner, and the surface-located beta-lactamase was shown to be enzymatically active. |
| T6 |
1071-1210 |
Sentence |
denotes |
Enzymatic activity was completely removed by protease treatment, indicating that surface display of beta-lactamase was almost quantitative. |
| T7 |
1211-1457 |
Sentence |
denotes |
The periplasmic domain of the outer membrane protein OmpA was not affected by externally added proteases, demonstrating that the outer membranes of E. coli cells expressing the beta-lactamase AIDA-I fusion protein remained physiologically intact. |
