Flavonols Inhibit Sortases and Sortase-Mediated Staphylococcus aureus Clumping to Fibrinogen

Sortases are a family of Gram-positive transpeptidases responsible for anchoring surface protein virulence factors to the peptidoglycan cell wall layer. In Staphylococcus aureus, deletion of the sortase isoforms results in marked reduction in virulence and infection potential, making it an important...

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Bibliographic Details
Published in:Biological & Pharmaceutical Bulletin 2006, Vol.29(8), pp.1751-1755
Main Authors: Kang, Sam Sik, Kim, Jae-Gyu, Lee, Tae-Hoon, Oh, Ki-Bong
Format: Article
Language:English
Subjects:
Base Sequence
Cell Adhesion - drug effects
DNA Primers
Enzyme Inhibitors - pharmacology
fibrinogen
Fibrinogen - metabolism
flavonol
Flavonols - pharmacology
Peptidyl Transferases - antagonists & inhibitors
Peptidyl Transferases - metabolism
sortase
Staphylococcus aureus
Staphylococcus aureus - metabolism
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Summary:Sortases are a family of Gram-positive transpeptidases responsible for anchoring surface protein virulence factors to the peptidoglycan cell wall layer. In Staphylococcus aureus, deletion of the sortase isoforms results in marked reduction in virulence and infection potential, making it an important antivirulence target. We examined the effects of naturally occurring flavonols on recombinant sortase A (SrtA) and B (SrtB) prepared from S. aureus ATCC6538p and found that these compounds inhibited the activity of sortases, without exhibiting antibacterial activities. Among the flavonols tested, morin, myricetin, and quercetin exhibited strong sortase inhibitory activities (SrtA IC50: 37.39—52.70 μM, SrtB IC50: 8.54—36.89 μM). The fibrinogen cell-clumping activity data highlight the potential of flavonols for the treatment of S. aureus infections via inhibition of sortase.
ISSN:0918-6158
1347-5215
DOI:10.1248/bpb.29.1751