The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Ribosomally Synthesized Thiopeptide Antibiotics Targeting Elongation Factor Tu
Abstract
We identified the thiomuracins, a novel family of thiopeptides produced by a rare-actinomycete bacterium typed as a Nonomuraea species, via a screen for inhibition of growth of the bacterial pathogen Staphylococcus aureus. Thiopeptides are a class of macrocyclic, highly modified peptides that are decorated by thiazoles and defined by a central six-membered heterocyclic ring system. Mining the genomes of thiopeptide-producing strains revealed the elusive biosynthetic route for this class of antibiotics. The thiopeptides are chromosomally encoded, ribosomally synthesized proteins, and isolation of gene clusters for production of thiomuracin and the related thiopeptide GE2270A revealed the post-translational machinery required for maturation. The target of the thiomuracins was identified as bacterial Elongation Factor Tu (EF-Tu). In addition to potently inhibiting a target that is unexploited by marketed human therapeutics, the thiomuracins have a low propensity for selecting for antibiotic resistance and confer no measurable cross-resistance to antibiotics in clinical use.
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Schmidt, E. W., Nelson, J. T., Rasko, D. A., Sudek, S., Eisen, J. A., Haygood, M. G., & Ravel, J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0501424102 · Cited by 567
Cited by
Arnison, P. G., Bibb, M. J., Bierbaum, G., Bowers, A. A., Bugni, T. S., Bulaj, G., Camarero, J. A., Campopiano, D. J., Challis, G. L., Clardy, J., et al. (2013) · Nat. Prod. Rep. · doi:10.1039/c2np20085f · Cited by 2,076
Bacteriocins—A viable alternative to antibiotics?
Cotter, P. D., Ross, R. P., & Hill, C. (2013) · Nature Reviews Microbiology · doi:10.1038/nrmicro2937 · Cited by 1,793
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Broderick, J. B., Duffus, B. R., Duschene, K. S., & Shepard, E. M. (2014) · Chemical Reviews · doi:10.1021/cr4004709 · Cited by 830
Genomic basis for natural product biosynthetic diversity in the actinomycetes
Nett, M., Ikeda, H., & Moore, B. S. (2009) · Natural Product Reports · doi:10.1039/b817069j · Cited by 757
Natural Products Version 2.0: Connecting Genes to Molecules
Walsh, C. T., & Fischbach, M. A. (2010) · Journal of the American Chemical Society · doi:10.1021/ja909118a · Cited by 468
Follow the leader: the use of leader peptides to guide natural product biosynthesis
Oman, T. J., & van der Donk, W. A. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.286 · Cited by 408
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Burkhart, B. J., Hudson, G. A., Dunbar, K. L., & Mitchell, D. A. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1856 · Cited by 374
Acker, M. G., Bowers, A. A., & Walsh, C. T. (2009) · Journal of the American Chemical Society · doi:10.1021/ja908777t · Cited by 91
Metadata
- Authors
- Morris, R. P., Leeds, J. A., Naegeli, H. U., Oberer, L., Memmert, K., Weber, E., LaMarche, M. J., Parker, C. N., Burrer, N., Esterow, S., Hein, A. E., Schmitt, E. K., & Krastel, P.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2009-04-01
- Volume
- 131
- Issue
- 16
- Pages
- 5946-5955
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W2082578459
- Cited by
- 166
- References
- 1
- FWCI
- 13.02
- Type
- journal article
- Language
- en
- Open access
- closed
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