Inhibitory Effects of sp. MBTH32 Metabolites on Sortase A and Sortase A-Mediated Cell Clumping of to Fibrinogen.

Sortase A (SrtA), a type of transpeptidase responsible for anchoring surface proteins to the peptidoglycan cell wall, is important in the virulence of gram-positive bacteria. Three compounds were isolated from marine-derived sp. MBTH32 using various chromatography techniques. The structures of these compounds were determined based on spectroscopic data and comparisons with previously reported data. Among the metabolites tested, lumichrome showed strong inhibitory activity against SrtA without affecting cell viability. The results of cell clumping activity assessment suggest the potential for using this compound to treat infection by inhibiting SrtA activity.