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Antibacterial properties of Acinetobacter baumanniiphage Abp1 endolysin (PlyAB1)

BACKGROUND: Acinetobacter baumannii has emerged as one of the most important hospital-acquired pathogens in the world, because of its resistance to almost all available antibiotic drugs. Endolysins from phages are attracting increasing interest as potential antimicrobial agents, especially for drug-...

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Autores principales: Huang, Guangtao, Shen, Xiaodong, Gong, Yali, Dong, Zhiwei, Zhao, Xia, Shen, Wei, Wang, Jing, Hu, Fuquan, Peng, Yizhi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4274762/
https://www.ncbi.nlm.nih.gov/pubmed/25495514
http://dx.doi.org/10.1186/s12879-014-0681-2
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author Huang, Guangtao
Shen, Xiaodong
Gong, Yali
Dong, Zhiwei
Zhao, Xia
Shen, Wei
Wang, Jing
Hu, Fuquan
Peng, Yizhi
author_facet Huang, Guangtao
Shen, Xiaodong
Gong, Yali
Dong, Zhiwei
Zhao, Xia
Shen, Wei
Wang, Jing
Hu, Fuquan
Peng, Yizhi
author_sort Huang, Guangtao
collection PubMed
description BACKGROUND: Acinetobacter baumannii has emerged as one of the most important hospital-acquired pathogens in the world, because of its resistance to almost all available antibiotic drugs. Endolysins from phages are attracting increasing interest as potential antimicrobial agents, especially for drug-resistant bacteria. We previously isolated and characterized Abp1, a virulent phage targeting the multidrug-resistant A. baumannii strain, AB1. METHODS: To evaluate the antimicrobial potential of endolysin from the Abp1 phage, the endolysin gene plyAB1 was cloned and over-expressed in Escherichia coli, and the lytic activity of the recombinant protein (PlyAB1) was tested by turbidity assessment and bacteria counting assays. RESULTS: PlyAB1 exhibits a marked lytic activity against A. baumannii AB1, as shown by a decrease in the number of live bacteria following treatment with the enzyme. Moreover, PlyAB1 displayed a highly specific lytic effect against all of the 48 hospital-derived pandrug-resistant A. baumannii isolates that were tested. These isolates were shown to belong to different ST clones by multilocus sequence typing. CONCLUSIONS: The results presented here show that PlyAB1 has potential as an antibiotic against drug-resistant A. baumannii. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12879-014-0681-2) contains supplementary material, which is available to authorized users.
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spelling pubmed-42747622014-12-24 Antibacterial properties of Acinetobacter baumanniiphage Abp1 endolysin (PlyAB1) Huang, Guangtao Shen, Xiaodong Gong, Yali Dong, Zhiwei Zhao, Xia Shen, Wei Wang, Jing Hu, Fuquan Peng, Yizhi BMC Infect Dis Research Article BACKGROUND: Acinetobacter baumannii has emerged as one of the most important hospital-acquired pathogens in the world, because of its resistance to almost all available antibiotic drugs. Endolysins from phages are attracting increasing interest as potential antimicrobial agents, especially for drug-resistant bacteria. We previously isolated and characterized Abp1, a virulent phage targeting the multidrug-resistant A. baumannii strain, AB1. METHODS: To evaluate the antimicrobial potential of endolysin from the Abp1 phage, the endolysin gene plyAB1 was cloned and over-expressed in Escherichia coli, and the lytic activity of the recombinant protein (PlyAB1) was tested by turbidity assessment and bacteria counting assays. RESULTS: PlyAB1 exhibits a marked lytic activity against A. baumannii AB1, as shown by a decrease in the number of live bacteria following treatment with the enzyme. Moreover, PlyAB1 displayed a highly specific lytic effect against all of the 48 hospital-derived pandrug-resistant A. baumannii isolates that were tested. These isolates were shown to belong to different ST clones by multilocus sequence typing. CONCLUSIONS: The results presented here show that PlyAB1 has potential as an antibiotic against drug-resistant A. baumannii. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12879-014-0681-2) contains supplementary material, which is available to authorized users. BioMed Central 2014-12-12 /pmc/articles/PMC4274762/ /pubmed/25495514 http://dx.doi.org/10.1186/s12879-014-0681-2 Text en © Huang et al.; licensee BioMed Central. 2014 This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Research Article
Huang, Guangtao
Shen, Xiaodong
Gong, Yali
Dong, Zhiwei
Zhao, Xia
Shen, Wei
Wang, Jing
Hu, Fuquan
Peng, Yizhi
Antibacterial properties of Acinetobacter baumanniiphage Abp1 endolysin (PlyAB1)
title Antibacterial properties of Acinetobacter baumanniiphage Abp1 endolysin (PlyAB1)
title_full Antibacterial properties of Acinetobacter baumanniiphage Abp1 endolysin (PlyAB1)
title_fullStr Antibacterial properties of Acinetobacter baumanniiphage Abp1 endolysin (PlyAB1)
title_full_unstemmed Antibacterial properties of Acinetobacter baumanniiphage Abp1 endolysin (PlyAB1)
title_short Antibacterial properties of Acinetobacter baumanniiphage Abp1 endolysin (PlyAB1)
title_sort antibacterial properties of acinetobacter baumanniiphage abp1 endolysin (plyab1)
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4274762/
https://www.ncbi.nlm.nih.gov/pubmed/25495514
http://dx.doi.org/10.1186/s12879-014-0681-2
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