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The Proteome of Biologically Active Membrane Vesicles from Piscirickettsia salmonis LF-89 Type Strain Identifies Plasmid-Encoded Putative Toxins
Piscirickettsia salmonis is the predominant bacterial pathogen affecting the Chilean salmonid industry. This bacterium is the etiological agent of piscirickettsiosis, a significant fish disease. Membrane vesicles (MVs) released by P. salmonis deliver several virulence factors to host cells. To impro...
Autores principales: | , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5625009/ https://www.ncbi.nlm.nih.gov/pubmed/29034215 http://dx.doi.org/10.3389/fcimb.2017.00420 |
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author | Oliver, Cristian Hernández, Mauricio A. Tandberg, Julia I. Valenzuela, Karla N. Lagos, Leidy X. Haro, Ronie E. Sánchez, Patricio Ruiz, Pamela A. Sanhueza-Oyarzún, Constanza Cortés, Marcos A. Villar, María T. Artigues, Antonio Winther-Larsen, Hanne C. Avendaño-Herrera, Ruben Yáñez, Alejandro J. |
author_facet | Oliver, Cristian Hernández, Mauricio A. Tandberg, Julia I. Valenzuela, Karla N. Lagos, Leidy X. Haro, Ronie E. Sánchez, Patricio Ruiz, Pamela A. Sanhueza-Oyarzún, Constanza Cortés, Marcos A. Villar, María T. Artigues, Antonio Winther-Larsen, Hanne C. Avendaño-Herrera, Ruben Yáñez, Alejandro J. |
author_sort | Oliver, Cristian |
collection | PubMed |
description | Piscirickettsia salmonis is the predominant bacterial pathogen affecting the Chilean salmonid industry. This bacterium is the etiological agent of piscirickettsiosis, a significant fish disease. Membrane vesicles (MVs) released by P. salmonis deliver several virulence factors to host cells. To improve on existing knowledge for the pathogenicity-associated functions of P. salmonis MVs, we studied the proteome of purified MVs from the P. salmonis LF-89 type strain using multidimensional protein identification technology. Initially, the cytotoxicity of different MV concentration purified from P. salmonis LF-89 was confirmed in an in vivo adult zebrafish infection model. The cumulative mortality of zebrafish injected with MVs showed a dose-dependent pattern. Analyses identified 452 proteins of different subcellular origins; most of them were associated with the cytoplasmic compartment and were mainly related to key functions for pathogen survival. Interestingly, previously unidentified putative virulence-related proteins were identified in P. salmonis MVs, such as outer membrane porin F and hemolysin. Additionally, five amino acid sequences corresponding to the Bordetella pertussis toxin subunit 1 and two amino acid sequences corresponding to the heat-labile enterotoxin alpha chain of Escherichia coli were located in the P. salmonis MV proteome. Curiously, these putative toxins were located in a plasmid region of P. salmonis LF-89. Based on the identified proteins, we propose that the protein composition of P. salmonis LF-89 MVs could reflect total protein characteristics of this P. salmonis type strain. |
format | Online Article Text |
id | pubmed-5625009 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-56250092017-10-13 The Proteome of Biologically Active Membrane Vesicles from Piscirickettsia salmonis LF-89 Type Strain Identifies Plasmid-Encoded Putative Toxins Oliver, Cristian Hernández, Mauricio A. Tandberg, Julia I. Valenzuela, Karla N. Lagos, Leidy X. Haro, Ronie E. Sánchez, Patricio Ruiz, Pamela A. Sanhueza-Oyarzún, Constanza Cortés, Marcos A. Villar, María T. Artigues, Antonio Winther-Larsen, Hanne C. Avendaño-Herrera, Ruben Yáñez, Alejandro J. Front Cell Infect Microbiol Microbiology Piscirickettsia salmonis is the predominant bacterial pathogen affecting the Chilean salmonid industry. This bacterium is the etiological agent of piscirickettsiosis, a significant fish disease. Membrane vesicles (MVs) released by P. salmonis deliver several virulence factors to host cells. To improve on existing knowledge for the pathogenicity-associated functions of P. salmonis MVs, we studied the proteome of purified MVs from the P. salmonis LF-89 type strain using multidimensional protein identification technology. Initially, the cytotoxicity of different MV concentration purified from P. salmonis LF-89 was confirmed in an in vivo adult zebrafish infection model. The cumulative mortality of zebrafish injected with MVs showed a dose-dependent pattern. Analyses identified 452 proteins of different subcellular origins; most of them were associated with the cytoplasmic compartment and were mainly related to key functions for pathogen survival. Interestingly, previously unidentified putative virulence-related proteins were identified in P. salmonis MVs, such as outer membrane porin F and hemolysin. Additionally, five amino acid sequences corresponding to the Bordetella pertussis toxin subunit 1 and two amino acid sequences corresponding to the heat-labile enterotoxin alpha chain of Escherichia coli were located in the P. salmonis MV proteome. Curiously, these putative toxins were located in a plasmid region of P. salmonis LF-89. Based on the identified proteins, we propose that the protein composition of P. salmonis LF-89 MVs could reflect total protein characteristics of this P. salmonis type strain. Frontiers Media S.A. 2017-09-28 /pmc/articles/PMC5625009/ /pubmed/29034215 http://dx.doi.org/10.3389/fcimb.2017.00420 Text en Copyright © 2017 Oliver, Hernández, Tandberg, Valenzuela, Lagos, Haro, Sánchez, Ruiz, Sanhueza-Oyarzún, Cortés, Villar, Artigues, Winther-Larsen, Avendaño-Herrera and Yáñez. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Microbiology Oliver, Cristian Hernández, Mauricio A. Tandberg, Julia I. Valenzuela, Karla N. Lagos, Leidy X. Haro, Ronie E. Sánchez, Patricio Ruiz, Pamela A. Sanhueza-Oyarzún, Constanza Cortés, Marcos A. Villar, María T. Artigues, Antonio Winther-Larsen, Hanne C. Avendaño-Herrera, Ruben Yáñez, Alejandro J. The Proteome of Biologically Active Membrane Vesicles from Piscirickettsia salmonis LF-89 Type Strain Identifies Plasmid-Encoded Putative Toxins |
title | The Proteome of Biologically Active Membrane Vesicles from Piscirickettsia salmonis LF-89 Type Strain Identifies Plasmid-Encoded Putative Toxins |
title_full | The Proteome of Biologically Active Membrane Vesicles from Piscirickettsia salmonis LF-89 Type Strain Identifies Plasmid-Encoded Putative Toxins |
title_fullStr | The Proteome of Biologically Active Membrane Vesicles from Piscirickettsia salmonis LF-89 Type Strain Identifies Plasmid-Encoded Putative Toxins |
title_full_unstemmed | The Proteome of Biologically Active Membrane Vesicles from Piscirickettsia salmonis LF-89 Type Strain Identifies Plasmid-Encoded Putative Toxins |
title_short | The Proteome of Biologically Active Membrane Vesicles from Piscirickettsia salmonis LF-89 Type Strain Identifies Plasmid-Encoded Putative Toxins |
title_sort | proteome of biologically active membrane vesicles from piscirickettsia salmonis lf-89 type strain identifies plasmid-encoded putative toxins |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5625009/ https://www.ncbi.nlm.nih.gov/pubmed/29034215 http://dx.doi.org/10.3389/fcimb.2017.00420 |
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