Inhibition of sortase-mediated Staphylococcus aureus adhesion to fibronectin via fibronectin-binding protein by sortase inhibitors |
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Authors: | Ki-Bong Oh Mi-Na Oh Jae-Gyu Kim Dong-Sun Shin Jongheon Shin |
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Institution: | (1) School of Agricultural Biotechnology, Seoul National University, San 56-1, Sillim, Gwanak, Seoul, 151-921, South Korea;(2) Center for Agricultural Biomaterials, Seoul National University, San 56-1, Sillim, Gwanak, Seoul, 151-921, South Korea;(3) Natural Products Research Institute, College of Pharmacy, Seoul National University, Yungun 28, Jongro, Seoul, 110-460, South Korea |
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Abstract: | The sortase enzymes 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. Recombinant sortase A (SrtA) and sortase B (SrtB) were incubated with peptide substrate containing either
the LPETG or NPQTN motifs. (Z)-3-(2,5-dimethoxyphenyl)-2-(4-methoxyphenyl) acrylonitrile, β-sitosterol-3-O-glucopyranoside, berberine chloride, and psammaplin A1 showed potent inhibitory activity against SrtA and SrtB. These compounds
also exhibited potent inhibitory activity against S. aureus cell adhesion to fibronectin. The fibronectin-binding activity data highlight the potential of these compounds for the treatment
of S. aureus infections via inhibition of sortase activity. |
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