Epoxypeptide antibiotic tetaine mimics peptides in transport to bacteria.

Tetaine induced the lysis of Escherichia coli cells. Several di- and tripeptides were found to protect this cells against tetaine action. Certain peptides are able to diminish the inhibition by tetaine of diaminopimelic acid incorporation into peptidoglycan and the extent of this corresponds to the protection of the cells against the tetaine-induced lysis. The data indicate that tetaine enters E. coli cells predominantly by dipeptide permease and in part by one or more oligopeptide permease system. A number of di- and tripeptides diminished the inhibitory effect of tetaine on the incorporation of lysine into peptidoglycan of Staphylococcus aureus Oxford. In contrast to E. coli, tetaine seems to be transported into S. aureus by a single transport system.