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A novel vibriophage exhibits inhibitory activity against host protein synthesis machinery
Since the emergence of deadly pathogens and multidrug-resistant bacteria at an alarmingly increased rate, bacteriophages have been developed as a controlling bioagent to prevent the spread of pathogenic bacteria. One of these pathogens, disease-causing Vibrio parahaemolyticus (VP(AHPND)) which induc...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7012835/ https://www.ncbi.nlm.nih.gov/pubmed/32047244 http://dx.doi.org/10.1038/s41598-020-59396-3 |
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author | Thammatinna, Khrongkhwan Egan, MacKennon E. Htoo, Htut Htut Khanna, Kanika Sugie, Joseph Nideffer, Jason F. Villa, Elizabeth Tassanakajon, Anchalee Pogliano, Joe Nonejuie, Poochit Chaikeeratisak, Vorrapon |
author_facet | Thammatinna, Khrongkhwan Egan, MacKennon E. Htoo, Htut Htut Khanna, Kanika Sugie, Joseph Nideffer, Jason F. Villa, Elizabeth Tassanakajon, Anchalee Pogliano, Joe Nonejuie, Poochit Chaikeeratisak, Vorrapon |
author_sort | Thammatinna, Khrongkhwan |
collection | PubMed |
description | Since the emergence of deadly pathogens and multidrug-resistant bacteria at an alarmingly increased rate, bacteriophages have been developed as a controlling bioagent to prevent the spread of pathogenic bacteria. One of these pathogens, disease-causing Vibrio parahaemolyticus (VP(AHPND)) which induces acute hepatopancreatic necrosis, is considered one of the deadliest shrimp pathogens, and has recently become resistant to various classes of antibiotics. Here, we discovered a novel vibriophage that specifically targets the vibrio host, VP(AHPND). The vibriophage, designated Seahorse, was classified in the family Siphoviridae because of its icosahedral capsid surrounded by head fibers and a non-contractile long tail. Phage Seahorse was able to infect the host in a broad range of pH and temperatures, and it had a relatively short latent period (nearly 30 minutes) in which it produced progeny at 72 particles per cell at the end of its lytic cycle. Upon phage infection, the host nucleoid condensed and became toroidal, similar to the bacterial DNA morphology seen during tetracycline treatment, suggesting that phage Seahorse hijacked host biosynthesis pathways through protein translation. As phage Seahorse genome encodes 48 open reading frames with many hypothetical proteins, this genome could be a potential untapped resource for the discovery of phage-derived therapeutic proteins. |
format | Online Article Text |
id | pubmed-7012835 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-70128352020-02-21 A novel vibriophage exhibits inhibitory activity against host protein synthesis machinery Thammatinna, Khrongkhwan Egan, MacKennon E. Htoo, Htut Htut Khanna, Kanika Sugie, Joseph Nideffer, Jason F. Villa, Elizabeth Tassanakajon, Anchalee Pogliano, Joe Nonejuie, Poochit Chaikeeratisak, Vorrapon Sci Rep Article Since the emergence of deadly pathogens and multidrug-resistant bacteria at an alarmingly increased rate, bacteriophages have been developed as a controlling bioagent to prevent the spread of pathogenic bacteria. One of these pathogens, disease-causing Vibrio parahaemolyticus (VP(AHPND)) which induces acute hepatopancreatic necrosis, is considered one of the deadliest shrimp pathogens, and has recently become resistant to various classes of antibiotics. Here, we discovered a novel vibriophage that specifically targets the vibrio host, VP(AHPND). The vibriophage, designated Seahorse, was classified in the family Siphoviridae because of its icosahedral capsid surrounded by head fibers and a non-contractile long tail. Phage Seahorse was able to infect the host in a broad range of pH and temperatures, and it had a relatively short latent period (nearly 30 minutes) in which it produced progeny at 72 particles per cell at the end of its lytic cycle. Upon phage infection, the host nucleoid condensed and became toroidal, similar to the bacterial DNA morphology seen during tetracycline treatment, suggesting that phage Seahorse hijacked host biosynthesis pathways through protein translation. As phage Seahorse genome encodes 48 open reading frames with many hypothetical proteins, this genome could be a potential untapped resource for the discovery of phage-derived therapeutic proteins. Nature Publishing Group UK 2020-02-11 /pmc/articles/PMC7012835/ /pubmed/32047244 http://dx.doi.org/10.1038/s41598-020-59396-3 Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Thammatinna, Khrongkhwan Egan, MacKennon E. Htoo, Htut Htut Khanna, Kanika Sugie, Joseph Nideffer, Jason F. Villa, Elizabeth Tassanakajon, Anchalee Pogliano, Joe Nonejuie, Poochit Chaikeeratisak, Vorrapon A novel vibriophage exhibits inhibitory activity against host protein synthesis machinery |
title | A novel vibriophage exhibits inhibitory activity against host protein synthesis machinery |
title_full | A novel vibriophage exhibits inhibitory activity against host protein synthesis machinery |
title_fullStr | A novel vibriophage exhibits inhibitory activity against host protein synthesis machinery |
title_full_unstemmed | A novel vibriophage exhibits inhibitory activity against host protein synthesis machinery |
title_short | A novel vibriophage exhibits inhibitory activity against host protein synthesis machinery |
title_sort | novel vibriophage exhibits inhibitory activity against host protein synthesis machinery |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7012835/ https://www.ncbi.nlm.nih.gov/pubmed/32047244 http://dx.doi.org/10.1038/s41598-020-59396-3 |
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