2. Academic Validation
  3. Domain requirement of moenomycin binding to bifunctional transglycosylases and development of high-throughput discovery of antibiotics

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

  • Proc Natl Acad Sci U S A. 2008 Jan 15;105(2):431-6. doi: 10.1073/pnas.0710868105.
Ting-Jen Rachel Cheng 1,  Ming-Ta Sung,  Hsin-Yu Liao,  Yi-Fan Chang,  Chia-Wei Chen,  Chia-Ying Huang,  Lien-Yang Chou,  Yen-Da Wu,  Yin-Hsuan Chen,  Yih-Shyun E Cheng,  Chi-Huey Wong,  Che Ma,  Wei-Chieh Cheng
Affiliations

Affiliation

  • 1 Genomics Research Center, Academia Sinica, Sec. 2, 128 Academia Road, Nangang, Taipei 115, Taiwan.
PMID: 18182485 DOI: 10.1073/pnas.0710868105
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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