Phage Hunters Spring 2017
My Annotations
| Status | Page | Date/Time | GO Term (Aspect) | Reference | Evidence | Notes | Links |
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| BACAN:Q81WA9 | 2017-05-09 13:36:18 CDT | GO:0019835 cytolysis (P) | PMID:16103125 | ECO:0000315 mutant phenotype evidence used in manual assertion | In Figure 4, an assay of lytic enzyme activity of PlyL and its mutant, Ply21 was conducted on the cell wall of five bacterial hosts. The mutant Ply21 is described as the full-length protein of PlyL with the removal of the C-terminal domain involved in cell wall binding, leaving behind only the presence of the N-terminal catalytic domain. In Panel B, the lysing abilities of Ply21 are shown, and the removal of the C-terminal cell wall binding domain did not have a significant effect on the lysing of the bacterial hosts. However, the N-terminal catalytic domain displayed a higher percent absorbance over time as compared to Panel A, (which displayed the lysing abilities of the full length protein). Furthermore, B. subtilis (yellow-orange line) displayed the highest lysing ability than all of the bacterial hosts, with the absorbance rate being higher in the graph of Panel B than Panel A. This concludes that the mutant PlyL 21, also known as the N-terminal catalytic domain of the full length PlyL protein with the C-terminal binding domain removed, is most efficient in cytolysis and that the removal of the C-terminal cell wall binding domain does not inhibit nor improve the lysing ability of PlyL on the cell wall of bacterial hosts.
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| flagged | BACSU:XLYA | 2017-04-30 22:50:35 CDT | GO:0019835 cytolysis (P) | PMID:21816821 | ECO:0000250 sequence similarity evidence used in manual assertion | In Figure 2, the structures and desirable behaviors were compared between PlyL and XlyA, concluding them to be homologous amidase lysins. Specifically in Panel A of Figure 2, the lysing abilities of the strains were compared on their effect on host cell B. Subtilis. The full-length protein of XlyA was similar to its lysing abilities of the catalytic domain of PlyL, which is responsible for producing amidase, an enzyme that cleaves peptidoglycan in the cell walls of the bacterial host cells.
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| Status | Author,Group | Page | GO Term (Aspect) | Reference | Evidence | Links | Page history |
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