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The endolysin of the Acinetobacter baumannii phage vB_AbaP_D2 shows broad antibacterial activity
The emergence and rapid spread of multidrug‐resistant bacteria has induced intense research for novel therapeutic approaches. In this study, the Acinetobacter baumannii bacteriophage D2 (vB_AbaP_D2) was isolated, characterized and sequenced. The endolysin of bacteriophage D2, namely Abtn‐4, contains...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7936296/ https://www.ncbi.nlm.nih.gov/pubmed/32519416 http://dx.doi.org/10.1111/1751-7915.13594 |
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author | Yuan, Yuyu Li, Xiaoyu Wang, Lili Li, Gen Cong, Cong Li, Ruihua Cui, Huijing Murtaza, Bilal Xu, Yongping |
author_facet | Yuan, Yuyu Li, Xiaoyu Wang, Lili Li, Gen Cong, Cong Li, Ruihua Cui, Huijing Murtaza, Bilal Xu, Yongping |
author_sort | Yuan, Yuyu |
collection | PubMed |
description | The emergence and rapid spread of multidrug‐resistant bacteria has induced intense research for novel therapeutic approaches. In this study, the Acinetobacter baumannii bacteriophage D2 (vB_AbaP_D2) was isolated, characterized and sequenced. The endolysin of bacteriophage D2, namely Abtn‐4, contains an amphipathic helix and was found to have activity against multidrug‐resistant Gram‐negative strains. By more than 3 log units, A. baumannii were killed by Abtn‐4 (5 µM) in 2 h. In absence of outer membrane permeabilizers, Abtn‐4 exhibited broad antimicrobial activity against several Gram‐positive and Gram‐negative bacteria, such as Staphylococcus aureus, Pseudomonas aeruginosa, Klebsiella pneumonia, Enterococcus and Salmonella. Furthermore, Abtn‐4 had the ability to reduce biofilm formation. Interestingly, Abtn‐4 showed antimicrobial activity against phage‐resistant bacterial mutants. Based on these results, endolysin Abtn‐4 may be a promising candidate therapeutic agent for multidrug‐resistant bacterial infections. |
format | Online Article Text |
id | pubmed-7936296 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-79362962021-03-16 The endolysin of the Acinetobacter baumannii phage vB_AbaP_D2 shows broad antibacterial activity Yuan, Yuyu Li, Xiaoyu Wang, Lili Li, Gen Cong, Cong Li, Ruihua Cui, Huijing Murtaza, Bilal Xu, Yongping Microb Biotechnol Research Articles The emergence and rapid spread of multidrug‐resistant bacteria has induced intense research for novel therapeutic approaches. In this study, the Acinetobacter baumannii bacteriophage D2 (vB_AbaP_D2) was isolated, characterized and sequenced. The endolysin of bacteriophage D2, namely Abtn‐4, contains an amphipathic helix and was found to have activity against multidrug‐resistant Gram‐negative strains. By more than 3 log units, A. baumannii were killed by Abtn‐4 (5 µM) in 2 h. In absence of outer membrane permeabilizers, Abtn‐4 exhibited broad antimicrobial activity against several Gram‐positive and Gram‐negative bacteria, such as Staphylococcus aureus, Pseudomonas aeruginosa, Klebsiella pneumonia, Enterococcus and Salmonella. Furthermore, Abtn‐4 had the ability to reduce biofilm formation. Interestingly, Abtn‐4 showed antimicrobial activity against phage‐resistant bacterial mutants. Based on these results, endolysin Abtn‐4 may be a promising candidate therapeutic agent for multidrug‐resistant bacterial infections. John Wiley and Sons Inc. 2020-06-10 /pmc/articles/PMC7936296/ /pubmed/32519416 http://dx.doi.org/10.1111/1751-7915.13594 Text en © 2020 The Authors. Microbial Biotechnology published by Society for Applied Microbiology and John Wiley & Sons Ltd This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made. |
spellingShingle | Research Articles Yuan, Yuyu Li, Xiaoyu Wang, Lili Li, Gen Cong, Cong Li, Ruihua Cui, Huijing Murtaza, Bilal Xu, Yongping The endolysin of the Acinetobacter baumannii phage vB_AbaP_D2 shows broad antibacterial activity |
title | The endolysin of the Acinetobacter baumannii phage vB_AbaP_D2 shows broad antibacterial activity |
title_full | The endolysin of the Acinetobacter baumannii phage vB_AbaP_D2 shows broad antibacterial activity |
title_fullStr | The endolysin of the Acinetobacter baumannii phage vB_AbaP_D2 shows broad antibacterial activity |
title_full_unstemmed | The endolysin of the Acinetobacter baumannii phage vB_AbaP_D2 shows broad antibacterial activity |
title_short | The endolysin of the Acinetobacter baumannii phage vB_AbaP_D2 shows broad antibacterial activity |
title_sort | endolysin of the acinetobacter baumannii phage vb_abap_d2 shows broad antibacterial activity |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7936296/ https://www.ncbi.nlm.nih.gov/pubmed/32519416 http://dx.doi.org/10.1111/1751-7915.13594 |
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