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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.

The Proteome of Biologically Active Membrane Vesicles from Piscirickettsia salmonis LF-89 Type Strain Identifies Plasmid-Encoded Putative Toxins