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PMID:22729533
| Citation |
Rodríguez-Rubio, L, Gutiérrez, D, Martínez, B, Rodríguez, A, Götz, F and García, P (2012) The tape measure protein of the Staphylococcus aureus bacteriophage vB_SauS-phiIPLA35 has an active muramidase domain. Appl. Environ. Microbiol. 78:6369-71 |
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| Abstract |
Tailed double-stranded DNA (dsDNA) bacteriophages frequently harbor structural proteins displaying peptidoglycan hydrolytic activities. The tape measure protein from Staphylococcus aureus bacteriophage vB_SauS-phiIPLA35 has a lysozyme-like and a peptidase_M23 domain. This report shows that the lysozyme-like domain (TG1) has muramidase activity and exhibits in vitro lytic activity against live S. aureus cells, an activity that could eventually find use in the treatment of infections. |
| Links |
PubMed PMC3416594 Online version:10.1128/AEM.01236-12 |
| Keywords |
Bacteriolysis; Muramidase/genetics; Protein Structure, Tertiary; Staphylococcus Phages/genetics; Staphylococcus aureus/virology; Viral Proteins/genetics |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0003796: lysozyme activity |
ECO:0000314: |
F |
FIGURE 1 shows that the lysozyme-like domain (TG1) of Tape Measure Protein (TMP) of Staphylococcus aureus bacteriophage vB_SauS-phiIPLA35 has peptidoglycan muramidase activity and is most likely a muramidase that can digest MurNAc-GlcNAc linkages. The lytic activity TG1 protein against S. aureus is shown in Figure 2. |
complete | ||||
Notes
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References
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