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

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dc.contributor.authorOliver, C.
dc.contributor.authorHernández, M.A.
dc.contributor.authorTandberg, J.I.
dc.contributor.authorValenzuela, K.N.
dc.contributor.authorLagos, L.X.
dc.contributor.authorHaro, R.E.
dc.contributor.authorSánchez, P.
dc.contributor.authorRuiz, P.A.
dc.contributor.authorSanhueza-Oyarzún, C.
dc.contributor.authorCortés, M.A.
dc.contributor.authorVillar, M.T.
dc.contributor.authorArtigues, A.
dc.contributor.authorWinther-Larsen, H.C.
dc.contributor.authorAvendaño-Herrera, R.
dc.contributor.authorYáñez, A.J.
dc.date.accessioned2018-03-14T19:57:45Z
dc.date.available2018-03-14T19:57:45Z
dc.date.issued2017-09
dc.descriptionIndexación: Scopus.es_ES
dc.description.abstractPiscirickettsia 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. © 2017 Oliver, Hernández, Tandberg, Valenzuela, Lagos, Haro, Sánchez, Ruiz, Sanhueza-Oyarzún, Cortés, Villar, Artigues, Winther-Larsen, Avendaño-Herrera and Yáñez.es_ES
dc.description.urihttps://www.frontiersin.org/articles/10.3389/fcimb.2017.00420/full
dc.identifier.citationFrontiers in Cellular and Infection Microbiology, 7(SEP), art. no. 420.es_ES
dc.identifier.issn2235-2988
dc.identifier.otherhttps://doi.org/10.3389/fcimb.2017.00420
dc.identifier.urihttp://repositorio.unab.cl/xmlui/handle/ria/5441
dc.language.isoenes_ES
dc.publisherFrontiers Mediaes_ES
dc.subjectBacterial toxinses_ES
dc.subjectMass spectrometryes_ES
dc.subjectMudPITes_ES
dc.subjectPiscirickettsia salmonises_ES
dc.subjectSRSes_ES
dc.subjectZebrafishes_ES
dc.titleThe Proteome of Biologically Active Membrane Vesicles from Piscirickettsia salmonis LF-89 Type Strain Identifies Plasmid-Encoded Putative Toxinses_ES
dc.typeArtículoes_ES
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