Inhibition of Sortase, a Bacterial Surface Protein Anchoring Transpeptidase, by β-Sitosterol-3-O-glucopyranoside from Fritillaria verticillata

Abstract

  A glucosylsterol, β-sitosterol-3-O-glucopyranoside, has been isolated as an active principle with sortase inhibitory effect from the bulbs of Fritillaria verticillata by bioassay-guided chromatographic fractionation. The isolate was a potent inhibitor of sortase, with an IC₅₀ value of 18.3 μg/ml and had antibacterial activity against Bacillus subtilis, Staphylococcus aureus, and Micrococcus leuteus with MIC values of 50, 200, and 400 μg/ml, respectively, indicating that this compound is a possible candidate for the development of a bacterial sortase inhibitor. In addition, sitosterol was found to be inactive upon sortase and bacterial cell growth. These results suggest that the inhibitory potency of β-sitosterol-3-O-glucopyranoside is sensitively dependent upon the glucopyranoside side chain moiety.