Impact of individual extracellular proteases on Staphylococcus aureus biofilm formation in diverse clinical isolates and their isogenic sarA mutants. Issue 6 (25th September 2014)
- Record Type:
- Journal Article
- Title:
- Impact of individual extracellular proteases on Staphylococcus aureus biofilm formation in diverse clinical isolates and their isogenic sarA mutants. Issue 6 (25th September 2014)
- Main Title:
- Impact of individual extracellular proteases on Staphylococcus aureus biofilm formation in diverse clinical isolates and their isogenic sarA mutants
- Authors:
- Loughran, Allister J.
Atwood, Danielle N.
Anthony, Allison C.
Harik, Nada S.
Spencer, Horace J.
Beenken, Karen E.
Smeltzer, Mark S. - Abstract:
- <abstract abstract-type="main" id="mbo3214-abs-0001"> <title>Abstract</title> <p>We demonstrate that the purified <italic>Staphylococcus aureus</italic> extracellular proteases aureolysin, ScpA, SspA, and SspB limit biofilm formation, with aureolysin having the greatest impact. Using protease‐deficient derivatives of LAC, we confirmed that this is due to the individual proteases themselves. Purified aureolysin, and to a lesser extent ScpA and SspB, also promoted dispersal of an established biofilm. Mutation of the genes encoding these proteases also only partially restored biofilm formation in an FPR3757 <italic>sarA</italic> mutant and had little impact on restoring virulence in a murine bacteremia model. In contrast, eliminating the production of all of these proteases fully restored both biofilm formation and virulence in a <italic>sarA</italic> mutant generated in the closely related USA300 strain LAC. These results confirm an important role for multiple extracellular proteases in <italic>S. aureus</italic> pathogenesis and the importance of <italic>sarA</italic> in repressing their production. Moreover, purified aureolysin limited biofilm formation in 14 of 15 methicillin‐resistant isolates and 11 of 15 methicillin‐susceptible isolates, while dispersin B had little impact in UAMS‐1, LAC, or 29 of 30 contemporary isolates of <italic>S. aureus</italic>. This suggests that the role of <italic>sarA</italic> and its impact on protease production is important in diverse<abstract abstract-type="main" id="mbo3214-abs-0001"> <title>Abstract</title> <p>We demonstrate that the purified <italic>Staphylococcus aureus</italic> extracellular proteases aureolysin, ScpA, SspA, and SspB limit biofilm formation, with aureolysin having the greatest impact. Using protease‐deficient derivatives of LAC, we confirmed that this is due to the individual proteases themselves. Purified aureolysin, and to a lesser extent ScpA and SspB, also promoted dispersal of an established biofilm. Mutation of the genes encoding these proteases also only partially restored biofilm formation in an FPR3757 <italic>sarA</italic> mutant and had little impact on restoring virulence in a murine bacteremia model. In contrast, eliminating the production of all of these proteases fully restored both biofilm formation and virulence in a <italic>sarA</italic> mutant generated in the closely related USA300 strain LAC. These results confirm an important role for multiple extracellular proteases in <italic>S. aureus</italic> pathogenesis and the importance of <italic>sarA</italic> in repressing their production. Moreover, purified aureolysin limited biofilm formation in 14 of 15 methicillin‐resistant isolates and 11 of 15 methicillin‐susceptible isolates, while dispersin B had little impact in UAMS‐1, LAC, or 29 of 30 contemporary isolates of <italic>S. aureus</italic>. This suggests that the role of <italic>sarA</italic> and its impact on protease production is important in diverse strains of <italic>S. aureus</italic> irrespective of their methicillin resistance status.</p> </abstract> … (more)
- Is Part Of:
- MicrobiologyOpen. Volume 3:Issue 6(2014:Dec.)
- Journal:
- MicrobiologyOpen
- Issue:
- Volume 3:Issue 6(2014:Dec.)
- Issue Display:
- Volume 3, Issue 6 (2014)
- Year:
- 2014
- Volume:
- 3
- Issue:
- 6
- Issue Sort Value:
- 2014-0003-0006-0000
- Page Start:
- 897
- Page End:
- 909
- Publication Date:
- 2014-09-25
- Subjects:
- Microbiology -- Periodicals
579 - Journal URLs:
- http://onlinelibrary.wiley.com/ ↗
http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)2045-8827 ↗ - DOI:
- 10.1002/mbo3.214 ↗
- Languages:
- English
- ISSNs:
- 2045-8827
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 3438.xml