Abstract
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 Streptomyces 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 Staphylococcus aureus SrtA without affecting cell viability. The results of cell clumping activity assessment suggest the potential for using this compound to treat S. aureus infection by inhibiting SrtA activity.
Keywords:
Marine Streptomyces; Staphylococcus aureus; cell clumping; lumichrome; sortase A.
MeSH terms
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Aminoacyltransferases / antagonists & inhibitors*
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Aminoacyltransferases / genetics
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Aminoacyltransferases / metabolism
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Bacterial Adhesion / drug effects
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Bacterial Proteins / antagonists & inhibitors*
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Cysteine Endopeptidases / genetics
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Cysteine Endopeptidases / metabolism
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Enzyme Inhibitors / chemistry
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Enzyme Inhibitors / isolation & purification
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Enzyme Inhibitors / pharmacology*
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Fibrinogen / metabolism*
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Flavins / chemistry
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Flavins / isolation & purification
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Flavins / pharmacology
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Inhibitory Concentration 50
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Molecular Structure
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Mutation
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Staphylococcus aureus / enzymology
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Staphylococcus aureus / pathogenicity*
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Streptomyces / chemistry*
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Streptomyces / metabolism
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Virulence / drug effects
Substances
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Bacterial Proteins
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Enzyme Inhibitors
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Flavins
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7,8-dimethylalloxazine
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Fibrinogen
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Aminoacyltransferases
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sortase A
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Cysteine Endopeptidases