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PMID:27656173
| Citation |
Thummeepak, R, Kitti, T, Kunthalert, D and Sitthisak, S (2016) Enhanced Antibacterial Activity of Acinetobacter baumannii Bacteriophage ØABP-01 Endolysin (LysABP-01) in Combination with Colistin. Front Microbiol 7:1402 |
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| Abstract |
Endolysins are lytic enzymes produced by bacteriophages with their ability to degrade the cell wall of bacterial hosts. Endolysin (LysABP-01) from Acinetobacter baumannii bacteriophage ØABP-01 was cloned, overexpressed and characterized. Endolysin LysABP-01 has a globular structure consisting of lysozyme-like (N-acetyl-β-D-muramidase) catalytic domain. It contains 185 amino acids which correspond to a 21.1 kDa protein. The lytic activity of the recombinant endolysin protein was determined by a plate lysis assay for its ability to lyse the autoclaved cell (crude cell wall) of the different bacterial species. LysABP-01 can degrade the crude cell wall of A. baumannii strains, Escherichia coli and Pseudomonas aeruginosa but not of Staphylococcus aureus. The antibacterial activity of LysABP-01 and its synergism with various antibiotics were tested. The results exhibited elevated antibacterial activity in a combination of the sub-MIC LysABP-01 and colistin. The checkerboard assay for measuring antibiotic synergy of LysABP-01 and colistin was performed. This combination was synergistic against various drug-resistant strains of A. baumannii (FIC index < 0.5). In summary, our study highlights the ability of LysABP-01 endolysin to hydrolyze the A. baumannii cell wall and its synergistic interaction with colistin. |
| Links |
PubMed PMC5013039 Online version:10.3389/fmicb.2016.01402 |
| Keywords |
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Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0003796: lysozyme activity |
ECO:0000314: |
F |
Figure 3 shows antibacterial (lytic) activity of LysABP-01 |
complete | ||||
| GO:0003796: lysozyme activity |
ECO:0000247: |
UniProtKB:F1BCP4
|
F |
Figure 1 shows that PlyAB1 (R4IQ32) is a homologue of LysABP-01 (accession no: W0M2E9) and LysAB2 (accession no: F1BCP4) whose endolysin activity have been demonstrated in PMID:27656173[1] [LysABP-01 (accession no: W0M2E9)] and PMID:21264466[2] [LysAB2 (accession no: F1BCP4)] |
complete | |||
Notes
See also
References
See Help:References for how to manage references in GONUTS.
- ↑ Thummeepak, R et al. (2016) Enhanced Antibacterial Activity of Acinetobacter baumannii Bacteriophage ØABP-01 Endolysin (LysABP-01) in Combination with Colistin. Front Microbiol 7 1402 PubMed GONUTS page
- ↑ Lai, MJ et al. (2011) Antibacterial activity of Acinetobacter baumannii phage ϕAB2 endolysin (LysAB2) against both gram-positive and gram-negative bacteria. Appl. Microbiol. Biotechnol. 90 529-39 PubMed GONUTS page
