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The infection process of Piscirickettsia salmonis in fish macrophages is dependent upon interaction with host-cell clathrin and actin

Piscirickettsia salmonis is an aggressive fish pathogen that causes Piscirickettsiosis, a systemic disease that threatens the sustainability of salmon production in Chile. To date, the infection strategies of this bacterium are poorly characterized, a Dot/Icm Type IV Secretion System homolog for int...

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Published in:FEMS microbiology letters 2015-01, Vol.362 (1), p.1-8
Main Authors: Ramírez, Ramón, Gómez, Fernando A., Marshall, Sergio H.
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description Piscirickettsia salmonis is an aggressive fish pathogen that causes Piscirickettsiosis, a systemic disease that threatens the sustainability of salmon production in Chile. To date, the infection strategies of this bacterium are poorly characterized, a Dot/Icm Type IV Secretion System homolog for intracellular multiplication and survival in macrophages is suggested. Since an invading pathogen and its host develop a complex interaction in which the pathogen strives to survive and replicate, while the host tries to eliminate infected cells and the invading pathogen, we decided to evaluate how the bacterium enters macrophages, its preferred target in vivo, and to follow its fate while struggling with its host using actin cytoskeleton as a molecular marker. We were able to demonstrate that clathrin is required for internalization and that actin cytoskeleton plays a demonstrative role throughout the infective process. Indeed, unlike other fish pathogens, P. salmonis fully exploits the actin monomers both from the disorganized cytoskeleton and an apparently pathogen-induced de novo synthesis of actin, generating tridimensional vacuoles that are increasingly detected at later stages of infection. We expect our results to contribute to a better understanding of the pathogenesis of this important fish pathogen. In this work was able to confirm that P. salmonis, an important fish pathogen of salmon industry, require host-cell actin and clathrin to infect macrophages. Clathrin is required for inicial internalization and the actin participes in the formation of a replicative vacuole.
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To date, the infection strategies of this bacterium are poorly characterized, a Dot/Icm Type IV Secretion System homolog for intracellular multiplication and survival in macrophages is suggested. Since an invading pathogen and its host develop a complex interaction in which the pathogen strives to survive and replicate, while the host tries to eliminate infected cells and the invading pathogen, we decided to evaluate how the bacterium enters macrophages, its preferred target in vivo, and to follow its fate while struggling with its host using actin cytoskeleton as a molecular marker. We were able to demonstrate that clathrin is required for internalization and that actin cytoskeleton plays a demonstrative role throughout the infective process. Indeed, unlike other fish pathogens, P. salmonis fully exploits the actin monomers both from the disorganized cytoskeleton and an apparently pathogen-induced de novo synthesis of actin, generating tridimensional vacuoles that are increasingly detected at later stages of infection. We expect our results to contribute to a better understanding of the pathogenesis of this important fish pathogen. In this work was able to confirm that P. salmonis, an important fish pathogen of salmon industry, require host-cell actin and clathrin to infect macrophages. 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identifier ISSN: 1574-6968
ispartof FEMS microbiology letters, 2015-01, Vol.362 (1), p.1-8
issn 1574-6968
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1574-6968
language eng
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source Oxford Journals Online
subjects Actin
Actins - metabolism
Animals
Bacteria
Cell Line
Chile
Clathrin
Clathrin - metabolism
Cytoskeleton
Endocytosis
Fish
Homology
Host-Pathogen Interactions
Infections
Internalization
Macrophages
Macrophages - microbiology
Microbiology
Monomers
Multiplication
Pathogenesis
Pathogens
Piscirickettsia - physiology
Piscirickettsia salmonis
Salmon
Secretion
Vacuoles
title The infection process of Piscirickettsia salmonis in fish macrophages is dependent upon interaction with host-cell clathrin and actin
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