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

Frontiers in Cellular and Infection Microbiology

Sanhueza-Oyarzú¹  Villar, Marí²  n, Constanza²  Corté³  a T.³  Haro, Ronie E.⁴  Artigues, Antonio⁴  o-Herrera, Ruben⁴  ez, Alejandro J.⁵  Ruiz, Pamela A.⁵  Oliver, Cristian⁶  s, Marcos A.⁷  Tandberg, Julia I.⁸  Herná⁹  nchez, Patricio^1,10  ñ^1,10  Avendañ^1,10  Valenzuela, Karla N.^1,11  Winther-Larsen, Hanne C.^1,12  Sá^1,12  Yá^1,12  Lagos, Leidy X.^1,13  ndez, Mauricio A.^1,14 

[1] Austral-OMICS, Facultad de Ciencias, Universidad Austral de Chile, Chile;Center of Integrative Microbiology and Evolution, University of Oslo, Norway;Department of Pharmaceutical Biosciences, School of Pharmacy, University of Oslo, Norway;Facultad de Ciencias, Instituto de BioquíInterdisciplinary Center for Aquaculture Research, Chile;Laboratorio de PatologíMicrobiology and Immunology Department, Dalhousie University, Canada;a Acuía de Organismos Acuáa, Universidad Austral de Chile, Chile;cola, Universidad Andrémica y Microbiologís Bello, Chile;ticos y Biotecnologí

关键词: Piscirickettsia salmonis;    SRS;    Bacterial Toxins;    Mass Spectrometry;    MudPIT;    Zebrafish;   

DOI  :  10.3389/fcimb.2017.00420

学科分类：生物科学（综合）

来源: Frontiers

【 摘 要 】

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.

【 授权许可】

CC BY