Salmonella enterica serovar Typhimurium utilizes the ClpPX and Lon proteases for optimal fitness in the ceca of chickens

Salmonella enterica serovar Typhimurium (S. Typhimurium) is a leading cause of salmonellosis. Poultry and poultry products are implicated in transmission of Salmonella to humans. In 2013, an outbreak of S. Typhimurium occurred that comprised 39 states within the United States and was associated with...

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Main Author: Troxell, Bryan
Format: Online
Language:English
Published: Poultry Science Association, Inc. 2016
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4957304/
id pubmed-4957304
recordtype oai_dc
spelling pubmed-49573042016-09-01 Salmonella enterica serovar Typhimurium utilizes the ClpPX and Lon proteases for optimal fitness in the ceca of chickens Troxell, Bryan Microbiology and Food Safety Salmonella enterica serovar Typhimurium (S. Typhimurium) is a leading cause of salmonellosis. Poultry and poultry products are implicated in transmission of Salmonella to humans. In 2013, an outbreak of S. Typhimurium occurred that comprised 39 states within the United States and was associated with backyard flocks of chickens. Colonization of the avian host by S. Typhimurium requires numerous genetic factors encoded within the bacterium. Of particular interest are genetic factors induced by alternative sigma factors within S. Typhimurium since these genetic elements are important for adaptation to different environmental stresses. The heat shock response is a dedicated change in gene regulation within bacteria in response to several stresses, specifically growth at 42°C. Because chickens have a higher body temperature than other animals (42°C) the hypothesis was tested that components of the heat shock response are important for optimal fitness within the chicken. To this end, deletion of the heat shock proteases clpPX (BTNC0022) or lon (BTNC0021) was accomplished and the bacterial fitness in vivo was compared to the “wild-type” strain (NC1040) using a competition assay. One-day-old chicks were orally gavaged with an equal mixture of NC1040 and either BTNC0022 or BTNC0021. Quantification of viable bacteria over time by using plate counts indicated that deletion of either heat shock protease resulted in significantly reduced colonization of the chicken ceca compared to the wild-type strain. To satisfy the molecular Koch's postulates, clpPX and lon mutants were complemented in trans using a low-copy number plasmid for additional in vivo experiments. Complementation studies confirmed the importance of either heat shock protease to colonization of the chicken ceca. This report demonstrated that both ClpPX and Lon were important for optimal fitness within chickens. Moreover, these results suggested that components of the heat shock may be critical factors used by S. Typhimurium for colonization of poultry. The use of feed additives or other treatments that inactivate or inhibit ClpPX or Lon may reduce the bacterial burden of S. Typhimurium in poultry. Poultry Science Association, Inc. 2016-03-18 2016-07 /pmc/articles/PMC4957304/ /pubmed/26994203 http://dx.doi.org/10.3382/ps/pew103 Text en © The Author 2016. Published by Oxford University Press on behalf of Poultry Science Association. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com.
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Troxell, Bryan
spellingShingle Troxell, Bryan
Salmonella enterica serovar Typhimurium utilizes the ClpPX and Lon proteases for optimal fitness in the ceca of chickens
author_facet Troxell, Bryan
author_sort Troxell, Bryan
title Salmonella enterica serovar Typhimurium utilizes the ClpPX and Lon proteases for optimal fitness in the ceca of chickens
title_short Salmonella enterica serovar Typhimurium utilizes the ClpPX and Lon proteases for optimal fitness in the ceca of chickens
title_full Salmonella enterica serovar Typhimurium utilizes the ClpPX and Lon proteases for optimal fitness in the ceca of chickens
title_fullStr Salmonella enterica serovar Typhimurium utilizes the ClpPX and Lon proteases for optimal fitness in the ceca of chickens
title_full_unstemmed Salmonella enterica serovar Typhimurium utilizes the ClpPX and Lon proteases for optimal fitness in the ceca of chickens
title_sort salmonella enterica serovar typhimurium utilizes the clppx and lon proteases for optimal fitness in the ceca of chickens
description Salmonella enterica serovar Typhimurium (S. Typhimurium) is a leading cause of salmonellosis. Poultry and poultry products are implicated in transmission of Salmonella to humans. In 2013, an outbreak of S. Typhimurium occurred that comprised 39 states within the United States and was associated with backyard flocks of chickens. Colonization of the avian host by S. Typhimurium requires numerous genetic factors encoded within the bacterium. Of particular interest are genetic factors induced by alternative sigma factors within S. Typhimurium since these genetic elements are important for adaptation to different environmental stresses. The heat shock response is a dedicated change in gene regulation within bacteria in response to several stresses, specifically growth at 42°C. Because chickens have a higher body temperature than other animals (42°C) the hypothesis was tested that components of the heat shock response are important for optimal fitness within the chicken. To this end, deletion of the heat shock proteases clpPX (BTNC0022) or lon (BTNC0021) was accomplished and the bacterial fitness in vivo was compared to the “wild-type” strain (NC1040) using a competition assay. One-day-old chicks were orally gavaged with an equal mixture of NC1040 and either BTNC0022 or BTNC0021. Quantification of viable bacteria over time by using plate counts indicated that deletion of either heat shock protease resulted in significantly reduced colonization of the chicken ceca compared to the wild-type strain. To satisfy the molecular Koch's postulates, clpPX and lon mutants were complemented in trans using a low-copy number plasmid for additional in vivo experiments. Complementation studies confirmed the importance of either heat shock protease to colonization of the chicken ceca. This report demonstrated that both ClpPX and Lon were important for optimal fitness within chickens. Moreover, these results suggested that components of the heat shock may be critical factors used by S. Typhimurium for colonization of poultry. The use of feed additives or other treatments that inactivate or inhibit ClpPX or Lon may reduce the bacterial burden of S. Typhimurium in poultry.
publisher Poultry Science Association, Inc.
publishDate 2016
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4957304/
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