Domain requirement of moenomycin binding to bifunctional transglycosylases and development of high-throughput discovery of antibiotics

Proceedings of the National Academy of Sciences of the United States of America
Ting-Jen Rachel ChengWei-Chieh Cheng

Abstract

Moenomycin inhibits bacterial growth by blocking the transglycosylase activity of class A penicillin-binding proteins (PBPs), which are key enzymes in bacterial cell wall synthesis. We compared the binding affinities of moenomycin A with various truncated PBPs by using surface plasmon resonance analysis and found that the transmembrane domain is important for moenomycin binding. Full-length class A PBPs from 16 bacterial species were produced, and their binding activities showed a correlation with the antimicrobial activity of moenomycin against Enterococcus faecalis and Staphylococcus aureus. On the basis of these findings, a fluorescence anisotropy-based high-throughput assay was developed and used successfully for identification of transglycosylase inhibitors.

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Aug 24, 2010·Natural Product Reports·Bohdan Ostash, Suzanne Walker
May 22, 2009·Proceedings of the National Academy of Sciences of the United States of America·Ming-Ta SungChe Ma
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