Domain requirement of moenomycin binding to bifunctional transglycosylases and development of high-throughput discovery of antibiotics
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 anal...
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| Published in | Proceedings of the National Academy of Sciences - PNAS Vol. 105; no. 2; pp. 431 - 436 |
|---|---|
| Main Authors | , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
National Academy of Sciences
15.01.2008
National Acad Sciences |
| Subjects | |
| Online Access | Get full text |
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| 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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| AbstractList | 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. 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. penicillin-binding proteins transglycosylase inhibitors fluorescence anisotropy 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.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. 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. 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. [PUBLICATION ABSTRACT] |
| Author | Wu, Yen-Da Cheng, Ting-Jen Rachel Cheng, Wei-Chieh Huang, Chia-Ying Chen, Chia-Wei Chen, Yin-Hsuan Chang, Yi-Fan Chou, Lien-Yang Sung, Ming-Ta Liao, Hsin-Yu Ma, Che Wong, Chi-Huey Cheng, Yih-Shyun E |
| Author_xml | – sequence: 1 fullname: Cheng, Ting-Jen Rachel – sequence: 2 fullname: Sung, Ming-Ta – sequence: 3 fullname: Liao, Hsin-Yu – sequence: 4 fullname: Chang, Yi-Fan – sequence: 5 fullname: Chen, Chia-Wei – sequence: 6 fullname: Huang, Chia-Ying – sequence: 7 fullname: Chou, Lien-Yang – sequence: 8 fullname: Wu, Yen-Da – sequence: 9 fullname: Chen, Yin-Hsuan – sequence: 10 fullname: Cheng, Yih-Shyun E – sequence: 11 fullname: Wong, Chi-Huey – sequence: 12 fullname: Ma, Che – sequence: 13 fullname: Cheng, Wei-Chieh |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/18182485$$D View this record in MEDLINE/PubMed |
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| SubjectTerms | Anisotropy anti-infective properties Antibacterials Antibiotics Antimicrobials bacteria binding capacity Binding sites Biological Sciences Cell growth Cell Wall - metabolism Cell walls Chemistry, Pharmaceutical - methods Correlation analysis Drug Design Enterococcus faecalis Enterococcus faecalis - metabolism Enzymes Escherichia coli fluorescence Glycosyltransferases - chemistry Inhibitory Concentration 50 Kinetics Lipids microbial growth Models, Chemical Molecules NMR Nuclear magnetic resonance Oligosaccharides - chemistry Oligosaccharides - pharmacology Penicillin-Binding Proteins - chemistry Physical Sciences Protease inhibitors Proteins Spectrometry, Fluorescence - methods Staphylococcus aureus Staphylococcus aureus - metabolism Staphylococcus infections surface plasmon resonance Surface Plasmon Resonance - methods Technology, Pharmaceutical - methods |
| Title | Domain requirement of moenomycin binding to bifunctional transglycosylases and development of high-throughput discovery of antibiotics |
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