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PMID:29495305
| Citation |
Fujiki, J, Nakamura, T, Furusawa, T, Ohno, H, Takahashi, H, Kitana, J, Usui, M, Higuchi, H, Tanji, Y, Tamura, Y and Iwano, H (2018) Characterization of the Lytic Capability of a LysK-Like Endolysin, Lys-phiSA012, Derived from a Polyvalent Staphylococcus aureus Bacteriophage. Pharmaceuticals (Basel) 11 |
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| Abstract |
Antibiotic-resistant bacteria (ARB) have spread widely and rapidly, with their increased occurrence corresponding with the increased use of antibiotics. Infections caused byhave a considerable negative impact on human and livestock health. Bacteriophages and their peptidoglycan hydrolytic enzymes (endolysins) have received significant attention as novel approaches against ARB, including. In the present study, we purified an endolysin, Lys-phiSA012, which harbors a cysteine/histidine-dependent amidohydrolase/peptidase (CHAP) domain, an amidase domain, and a SH3b cell wall binding domain, derived from a polyvalentbacteriophage which we reported previously. We demonstrate that Lys-phiSA012 exhibits high lytic activity towards staphylococcal strains, including methicillin-resistant(MRSA). Analysis of deletion mutants showed that only mutants possessing the CHAP and SH3b domains could lyse, indicating that lytic activity of the CHAP domain depended on the SH3b domain. The presence of at least 1 mM Caand 100 µM Znenhanced the lytic activity of Lys-phiSA012 in a turbidity reduction assay. Furthermore, a minimum inhibitory concentration (MIC) assay showed that the addition of Lys-phiSA012 decreased the MIC of oxacillin. Our results suggest that endolysins are a promising approach for replacing current antimicrobial agents and may contribute to the proper use of antibiotics, leading to the reduction of ARB. |
| Links |
PubMed Online version:10.3390/ph11010025 |
| Keywords |
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Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0019835: cytolysis |
ECO:0000315: |
P |
Figure 3: Lys-phiSA012 deletion mutants were tested for lytic activity towards SA003. Turbidity Reduction Assays using deletion mutants demonstrated that Lys-phiSA012∆mt2 showed high lytic activity comparable to the wild-type. Other mutants showed no lytic activity towards SA003 |
complete | ||||
Notes
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