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Characterization of a novel Achromobacter xylosoxidans specific siphoviruse: phiAxp-1
Bacteriophages have recently been considered as an alternative biocontrol tool because of the widespread occurrence of antimicrobial-resistant Achromobacter xylosoxidans. Herein, we isolated a virulent bacteriophage (phiAxp-1) from a water sample of the Bohai sea of China that specifically infects A...
Autores principales: | , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4764938/ https://www.ncbi.nlm.nih.gov/pubmed/26908262 http://dx.doi.org/10.1038/srep21943 |
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author | Li, Erna Zhao, Jiangtao Ma, Yanyan Wei, Xiao Li, Huan Lin, Weishi Wang, Xuesong Li, Chao Shen, Zhiqiang Zhao, Ruixiang Jiang, Aimin Yang, Huiying Yuan, Jing Zhao, Xiangna |
author_facet | Li, Erna Zhao, Jiangtao Ma, Yanyan Wei, Xiao Li, Huan Lin, Weishi Wang, Xuesong Li, Chao Shen, Zhiqiang Zhao, Ruixiang Jiang, Aimin Yang, Huiying Yuan, Jing Zhao, Xiangna |
author_sort | Li, Erna |
collection | PubMed |
description | Bacteriophages have recently been considered as an alternative biocontrol tool because of the widespread occurrence of antimicrobial-resistant Achromobacter xylosoxidans. Herein, we isolated a virulent bacteriophage (phiAxp-1) from a water sample of the Bohai sea of China that specifically infects A. xylosoxidans. Transmission electron microscopy revealed that phage phiAxp-1 belongs to the Siphoviridae. We sequenced the genome of phiAxp-1, which comprises 45,045 bp with 64 open reading frames. Most of the proteins encoded by phiAxp-1 have no similarity to sequences in the public databases. Twenty-one proteins with assigned functions share weak homology with those of other dsDNA bacteriophages infecting diverse hosts, such as Burkholderia phage KL1, Pseudomonas phage 73, Pseudomonas phage vB_Pae-Kakheti25, Pseudomonas phage vB_PaeS_SCH_Ab26, Acinetobacter phage IME_AB3 and Achromobacter phage JWX. The genome can be divided into different clusters for the head and tail structure, DNA replication and mazG. The sequence and genomic organization of bacteriophage phiAxp-1 are clearly distinct from other known Siphoviridae phages; therefore, we propose that it is a member of a novel genus of the Siphoviridae family. Furthermore, one-step growth curve and stability studies of the phage were performed, and the specific receptor of phiAxp-1 was identified as the lipopolysaccharide of A. xylosoxidans. |
format | Online Article Text |
id | pubmed-4764938 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-47649382016-03-02 Characterization of a novel Achromobacter xylosoxidans specific siphoviruse: phiAxp-1 Li, Erna Zhao, Jiangtao Ma, Yanyan Wei, Xiao Li, Huan Lin, Weishi Wang, Xuesong Li, Chao Shen, Zhiqiang Zhao, Ruixiang Jiang, Aimin Yang, Huiying Yuan, Jing Zhao, Xiangna Sci Rep Article Bacteriophages have recently been considered as an alternative biocontrol tool because of the widespread occurrence of antimicrobial-resistant Achromobacter xylosoxidans. Herein, we isolated a virulent bacteriophage (phiAxp-1) from a water sample of the Bohai sea of China that specifically infects A. xylosoxidans. Transmission electron microscopy revealed that phage phiAxp-1 belongs to the Siphoviridae. We sequenced the genome of phiAxp-1, which comprises 45,045 bp with 64 open reading frames. Most of the proteins encoded by phiAxp-1 have no similarity to sequences in the public databases. Twenty-one proteins with assigned functions share weak homology with those of other dsDNA bacteriophages infecting diverse hosts, such as Burkholderia phage KL1, Pseudomonas phage 73, Pseudomonas phage vB_Pae-Kakheti25, Pseudomonas phage vB_PaeS_SCH_Ab26, Acinetobacter phage IME_AB3 and Achromobacter phage JWX. The genome can be divided into different clusters for the head and tail structure, DNA replication and mazG. The sequence and genomic organization of bacteriophage phiAxp-1 are clearly distinct from other known Siphoviridae phages; therefore, we propose that it is a member of a novel genus of the Siphoviridae family. Furthermore, one-step growth curve and stability studies of the phage were performed, and the specific receptor of phiAxp-1 was identified as the lipopolysaccharide of A. xylosoxidans. Nature Publishing Group 2016-02-24 /pmc/articles/PMC4764938/ /pubmed/26908262 http://dx.doi.org/10.1038/srep21943 Text en Copyright © 2016, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Li, Erna Zhao, Jiangtao Ma, Yanyan Wei, Xiao Li, Huan Lin, Weishi Wang, Xuesong Li, Chao Shen, Zhiqiang Zhao, Ruixiang Jiang, Aimin Yang, Huiying Yuan, Jing Zhao, Xiangna Characterization of a novel Achromobacter xylosoxidans specific siphoviruse: phiAxp-1 |
title | Characterization of a novel Achromobacter xylosoxidans specific siphoviruse: phiAxp-1 |
title_full | Characterization of a novel Achromobacter xylosoxidans specific siphoviruse: phiAxp-1 |
title_fullStr | Characterization of a novel Achromobacter xylosoxidans specific siphoviruse: phiAxp-1 |
title_full_unstemmed | Characterization of a novel Achromobacter xylosoxidans specific siphoviruse: phiAxp-1 |
title_short | Characterization of a novel Achromobacter xylosoxidans specific siphoviruse: phiAxp-1 |
title_sort | characterization of a novel achromobacter xylosoxidans specific siphoviruse: phiaxp-1 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4764938/ https://www.ncbi.nlm.nih.gov/pubmed/26908262 http://dx.doi.org/10.1038/srep21943 |
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