Enhanced antibacterial activity of Acinetobacter baumannii bacteriophage ØABP-01 endolysin (LysABP-01) in combination with colistin
Endolysins are lytic enzymes produced by bacteriophages with their ability to degrade the cell wall of bacterial hosts. Endolysin (LysABP-01) from A. baumannii bacteriophage ØABP-01 was cloned, overexpressed and characterized. Endolysin LysABP-01 has a modular structure consisting of lysozyme-like (...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2016-09-01
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| Series: | Frontiers in Microbiology |
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| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fmicb.2016.01402/full |
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| author | Rapee Thummeepak Thawatchai Kitti Duangkamol Kunthalert Duangkamol Kunthalert Sutthirat Sitthisak Sutthirat Sitthisak |
| author_facet | Rapee Thummeepak Thawatchai Kitti Duangkamol Kunthalert Duangkamol Kunthalert Sutthirat Sitthisak Sutthirat Sitthisak |
| author_sort | Rapee Thummeepak |
| collection | DOAJ |
| description | Endolysins are lytic enzymes produced by bacteriophages with their ability to degrade the cell wall of bacterial hosts. Endolysin (LysABP-01) from A. baumannii bacteriophage ØABP-01 was cloned, overexpressed and characterized. Endolysin LysABP-01 has a modular 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. |
| first_indexed | 2024-12-22T12:31:19Z |
| format | Article |
| id | doaj.art-db4038d4d1c14842b7844d997d79a11b |
| institution | Directory Open Access Journal |
| issn | 1664-302X |
| language | English |
| last_indexed | 2024-12-22T12:31:19Z |
| publishDate | 2016-09-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Microbiology |
| spelling | doaj.art-db4038d4d1c14842b7844d997d79a11b2022-12-21T18:25:40ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2016-09-01710.3389/fmicb.2016.01402198829Enhanced antibacterial activity of Acinetobacter baumannii bacteriophage ØABP-01 endolysin (LysABP-01) in combination with colistinRapee Thummeepak0Thawatchai Kitti1Duangkamol Kunthalert2Duangkamol Kunthalert3Sutthirat Sitthisak4Sutthirat Sitthisak5Naresuan UniversityChiang Rai CollegeNaresuan UniversityNaresuan UniversityNaresuan UniversityNaresuan UniversityEndolysins are lytic enzymes produced by bacteriophages with their ability to degrade the cell wall of bacterial hosts. Endolysin (LysABP-01) from A. baumannii bacteriophage ØABP-01 was cloned, overexpressed and characterized. Endolysin LysABP-01 has a modular 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.http://journal.frontiersin.org/Journal/10.3389/fmicb.2016.01402/fullAcinetobacter baumanniiColistinAntibacterial activityBacteriophageendolysin |
| spellingShingle | Rapee Thummeepak Thawatchai Kitti Duangkamol Kunthalert Duangkamol Kunthalert Sutthirat Sitthisak Sutthirat Sitthisak Enhanced antibacterial activity of Acinetobacter baumannii bacteriophage ØABP-01 endolysin (LysABP-01) in combination with colistin Frontiers in Microbiology Acinetobacter baumannii Colistin Antibacterial activity Bacteriophage endolysin |
| title | Enhanced antibacterial activity of Acinetobacter baumannii bacteriophage ØABP-01 endolysin (LysABP-01) in combination with colistin |
| title_full | Enhanced antibacterial activity of Acinetobacter baumannii bacteriophage ØABP-01 endolysin (LysABP-01) in combination with colistin |
| title_fullStr | Enhanced antibacterial activity of Acinetobacter baumannii bacteriophage ØABP-01 endolysin (LysABP-01) in combination with colistin |
| title_full_unstemmed | Enhanced antibacterial activity of Acinetobacter baumannii bacteriophage ØABP-01 endolysin (LysABP-01) in combination with colistin |
| title_short | Enhanced antibacterial activity of Acinetobacter baumannii bacteriophage ØABP-01 endolysin (LysABP-01) in combination with colistin |
| title_sort | enhanced antibacterial activity of acinetobacter baumannii bacteriophage 216 abp 01 endolysin lysabp 01 in combination with colistin |
| topic | Acinetobacter baumannii Colistin Antibacterial activity Bacteriophage endolysin |
| url | http://journal.frontiersin.org/Journal/10.3389/fmicb.2016.01402/full |
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