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PMID:17054440
| Citation |
Donovan, DM, Lardeo, M and Foster-Frey, J (2006) Lysis of staphylococcal mastitis pathogens by bacteriophage phi11 endolysin. FEMS Microbiol. Lett. 265:133-9 |
|---|---|
| Abstract |
The Staphylococcus aureus bacteriophage phi11 endolysin has two peptidoglycan hydrolase domains (endopeptidase and amidase) and an SH3b cell wall-binding domain. In turbidity reduction assays, the purified protein can lyse untreated staphylococcal mastitis pathogens, Staphylococcus aureus and coagulase-negative staphylococci (Staphylococcus chronogenes, Staphylococcus epidermidis, Staphylococcus hyicus, Staphylococcus simulans, Staphylococcus warneri and Staphylococcus xylosus), making it a strong candidate protein antimicrobial. This lytic activity is maintained at the pH (6.7), and the "free" calcium concentration (3 mM) of milk. Truncated endolysin-derived proteins containing only the endopeptidase domain also lyse staphylococci in the absence of the SH3b-binding domain. |
| Links |
PubMed Online version:10.1111/j.1574-6968.2006.00483.x |
| Keywords |
Animals; Calcium/metabolism; Cattle; Endopeptidases/genetics; Endopeptidases/pharmacology; Hydrogen-Ion Concentration; Mastitis, Bovine/microbiology; Milk/metabolism; Staphylococcus Phages/genetics; Staphylococcus Phages/metabolism; Staphylococcus aureus/drug effects; Staphylococcus aureus/enzymology; Staphylococcus aureus/metabolism |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0001897: cytolysis by symbiont of host cells |
ECO:0000314: |
P |
Figure 2B shows the full length protein (phi11 481 in the figure) is able to lyse S aureus. |
complete | ||||
|
involved_in |
GO:0001897: cytolysis by symbiont of host cells |
ECO:0000314: direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
See also
References
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