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Insight into Invertebrate Defensin Mechanism of Action OYSTER DEFENSINS INHIBIT PEPTIDOGLYCAN BIOSYNTHESIS BY BINDING TO LIPID II ArchiMer
Schmitt, Paulina; Wilmes, Miriam; Pugniere, Martine; Aumelas, Andre; Bachere, Evelyne; Sahl, Hans-georg; Schneider, Tanja; Destoumieux-garzon, Delphine.
Three oyster defensin variants (Cg-Defh1, Cg-Defh2, and Cg-Defm) were produced as recombinant peptides and characterized in terms of activities and mechanism of action. In agreement with their spectrum of activity almost specifically directed against Gram-positive bacteria, oyster defensins were shown here to be specific inhibitors of a bacterial biosynthesis pathway rather than mere membrane-active agents. Indeed, at lethal concentrations, the three defensins did not compromise Staphylococcus aureus membrane integrity but inhibited the cell wall biosynthesis as indicated by the accumulation of the UDP-N-acetylmuramyl-pentapeptide cell wall precursor. In addition, a combination of antagonization assays, thin layer chromatography, and surface plasmon...
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Ano: 2010 URL: http://archimer.ifremer.fr/doc/00014/12503/9369.pdf
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