Bibliographic Details
| Title: |
The Proteome of Biologically Active Membrane Vesicles from Piscirickettsia salmonis LF-89 Type Strain Identifies Plasmid-Encoded Putative Toxins |
| Authors: |
Cristian Oliver, Mauricio A. Hernández, Julia I. Tandberg, Karla N. Valenzuela, Leidy X. Lagos, Ronie E. Haro, Patricio Sánchez, Pamela A. Ruiz, Constanza Sanhueza-Oyarzún, Marcos A. Cortés, María T. Villar, Antonio Artigues, Hanne C. Winther-Larsen, Ruben Avendaño-Herrera, Alejandro J. Yáñez |
| Source: |
Frontiers in Cellular and Infection Microbiology, Vol 7 (2017) |
| Publisher Information: |
Frontiers Media S.A., 2017. |
| Publication Year: |
2017 |
| Collection: |
LCC:Microbiology |
| Subject Terms: |
Piscirickettsia salmonis, SRS, bacterial toxins, mass spectrometry, MudPIT, zebrafish, Microbiology, QR1-502 |
| More Details: |
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. |
| Document Type: |
article |
| File Description: |
electronic resource |
| Language: |
English |
| ISSN: |
2235-2988 |
| Relation: |
http://journal.frontiersin.org/article/10.3389/fcimb.2017.00420/full; https://doaj.org/toc/2235-2988 |
| DOI: |
10.3389/fcimb.2017.00420 |
| Access URL: |
https://doaj.org/article/61229a396f434c13b6a2e4196f8460cb |
| Accession Number: |
edsdoj.61229a396f434c13b6a2e4196f8460cb |
| Database: |
Directory of Open Access Journals |
