SarA plays a predominant role in controlling the production of extracellular proteases in the diverse clinical isolates of Staphylococcus aureus LAC and UAMS-1

Using DNA affinity chromatography we demonstrate that the S. aureus regulatory proteins MgrA, Rot, SarA, and SarS bind DNA baits derived from the promoter regions associated with the genes encoding aureolysin, ScpAB, SspABC, and SplA-F. Three of four baits also bound SarR and SarZ, the exception in...

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Autores principales: Aura M. Ramirez, Karen E. Beenken, Stephanie D. Byrum, Alan J. Tackett, Lindsey N. Shaw, Brittney D. Gimza, Mark S. Smeltzer
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Lenguaje:EN
Publicado: Taylor & Francis Group 2020
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Acceso en línea:https://doaj.org/article/40cc6068c73e432795025640766a5025
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spelling oai:doaj.org-article:40cc6068c73e432795025640766a50252021-11-17T14:21:59ZSarA plays a predominant role in controlling the production of extracellular proteases in the diverse clinical isolates of Staphylococcus aureus LAC and UAMS-12150-55942150-560810.1080/21505594.2020.1855923https://doaj.org/article/40cc6068c73e432795025640766a50252020-12-01T00:00:00Zhttp://dx.doi.org/10.1080/21505594.2020.1855923https://doaj.org/toc/2150-5594https://doaj.org/toc/2150-5608Using DNA affinity chromatography we demonstrate that the S. aureus regulatory proteins MgrA, Rot, SarA, and SarS bind DNA baits derived from the promoter regions associated with the genes encoding aureolysin, ScpAB, SspABC, and SplA-F. Three of four baits also bound SarR and SarZ, the exception in both cases being the ScpAB-associated bait. Using the USA300, methicillin-resistant strain LAC and the USA200, methicillin-sensitive strain UAMS-1, we generated mutations in the genes encoding each of these proteins alone and in combination with sarA and examined the impact on protease production, the accumulation of high molecular weight proteins, and biofilm formation. These studies confirmed that multiple regulatory loci are involved in limiting protease production to a degree that impacts all of these phenotypes, but also demonstrate that sarA plays a predominant role in this regard. Using sarA mutants unable to produce individual proteases alone and in combination with each other, we also demonstrate that the increased production of aureolysin and ScpA is particularly important in defining the biofilm-deficient phenotype of LAC and UAMS-1 sarA mutants, while aureolysin alone plays a key role in defining the reduced accumulation of alpha toxin and overall cytotoxicity as assessed using both osteoblasts and osteoclasts.Aura M. RamirezKaren E. BeenkenStephanie D. ByrumAlan J. TackettLindsey N. ShawBrittney D. GimzaMark S. SmeltzerTaylor & Francis Grouparticlestaphylococcus aureusextracellular proteaseregulationbiofilmsararotmgrasarssarzsarrInfectious and parasitic diseasesRC109-216ENVirulence, Vol 11, Iss 1, Pp 1738-1762 (2020)
institution DOAJ
collection DOAJ
language EN
topic staphylococcus aureus
extracellular protease
regulation
biofilm
sara
rot
mgra
sars
sarz
sarr
Infectious and parasitic diseases
RC109-216
spellingShingle staphylococcus aureus
extracellular protease
regulation
biofilm
sara
rot
mgra
sars
sarz
sarr
Infectious and parasitic diseases
RC109-216
Aura M. Ramirez
Karen E. Beenken
Stephanie D. Byrum
Alan J. Tackett
Lindsey N. Shaw
Brittney D. Gimza
Mark S. Smeltzer
SarA plays a predominant role in controlling the production of extracellular proteases in the diverse clinical isolates of Staphylococcus aureus LAC and UAMS-1
description Using DNA affinity chromatography we demonstrate that the S. aureus regulatory proteins MgrA, Rot, SarA, and SarS bind DNA baits derived from the promoter regions associated with the genes encoding aureolysin, ScpAB, SspABC, and SplA-F. Three of four baits also bound SarR and SarZ, the exception in both cases being the ScpAB-associated bait. Using the USA300, methicillin-resistant strain LAC and the USA200, methicillin-sensitive strain UAMS-1, we generated mutations in the genes encoding each of these proteins alone and in combination with sarA and examined the impact on protease production, the accumulation of high molecular weight proteins, and biofilm formation. These studies confirmed that multiple regulatory loci are involved in limiting protease production to a degree that impacts all of these phenotypes, but also demonstrate that sarA plays a predominant role in this regard. Using sarA mutants unable to produce individual proteases alone and in combination with each other, we also demonstrate that the increased production of aureolysin and ScpA is particularly important in defining the biofilm-deficient phenotype of LAC and UAMS-1 sarA mutants, while aureolysin alone plays a key role in defining the reduced accumulation of alpha toxin and overall cytotoxicity as assessed using both osteoblasts and osteoclasts.
format article
author Aura M. Ramirez
Karen E. Beenken
Stephanie D. Byrum
Alan J. Tackett
Lindsey N. Shaw
Brittney D. Gimza
Mark S. Smeltzer
author_facet Aura M. Ramirez
Karen E. Beenken
Stephanie D. Byrum
Alan J. Tackett
Lindsey N. Shaw
Brittney D. Gimza
Mark S. Smeltzer
author_sort Aura M. Ramirez
title SarA plays a predominant role in controlling the production of extracellular proteases in the diverse clinical isolates of Staphylococcus aureus LAC and UAMS-1
title_short SarA plays a predominant role in controlling the production of extracellular proteases in the diverse clinical isolates of Staphylococcus aureus LAC and UAMS-1
title_full SarA plays a predominant role in controlling the production of extracellular proteases in the diverse clinical isolates of Staphylococcus aureus LAC and UAMS-1
title_fullStr SarA plays a predominant role in controlling the production of extracellular proteases in the diverse clinical isolates of Staphylococcus aureus LAC and UAMS-1
title_full_unstemmed SarA plays a predominant role in controlling the production of extracellular proteases in the diverse clinical isolates of Staphylococcus aureus LAC and UAMS-1
title_sort sara plays a predominant role in controlling the production of extracellular proteases in the diverse clinical isolates of staphylococcus aureus lac and uams-1
publisher Taylor & Francis Group
publishDate 2020
url https://doaj.org/article/40cc6068c73e432795025640766a5025
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