The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Structures of proline-rich peptides bound to the ribosome reveal a common mechanism of protein synthesis inhibition
Open accessAbstract
With bacterial resistance becoming a serious threat to global public health, antimicrobial peptides (AMPs) have become a promising area of focus in antibiotic research. AMPs are derived from a diverse range of species, from prokaryotes to humans, with a mechanism of action that often involves disruption of the bacterial cell membrane. Proline-rich antimicrobial peptides (PrAMPs) are instead actively transported inside the bacterial cell where they bind and inactivate specific targets. Recently, it was reported that some PrAMPs, such as Bac71 -35, oncocins and apidaecins, bind and inactivate the bacterial ribosome. Here we report the crystal structures of Bac71 -35, Pyrrhocoricin, Metalnikowin and two oncocin derivatives, bound to the Thermus thermophilus 70S ribosome. Each of the PrAMPs blocks the peptide exit tunnel of the ribosome by simultaneously occupying three well characterized antibiotic-binding sites and interferes with the initiation step of translation, thereby revealing a common mechanism of action used by these PrAMPs to inactivate protein synthesis. Our study expands the repertoire of PrAMPs and provides a framework for designing new-generation therapeutics.
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Overview of the CCP 4 suite and current developments
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Self-citationStructural Studies on the Forward and Reverse Binding Modes of Peptides to the Chaperone DnaK
Zahn, M., Berthold, N., Kieslich, B., Knappe, D., Hoffmann, R., & Sträter, N. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.03.041 · Cited by 126 · cited 1×
“The primary intra-cellular target for PrAMPs has long been thought to be the chaperone DnaK because PrAMPs can bind to DnaK and inhibit its activity (33,38,55,65).”
Negamycin interferes with decoding and translocation by simultaneous interaction with rRNA and tRNA
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Cited by
Roy, R., Tiwari, M., Donelli, G., & Tiwari, V. (2018) · Virulence · doi:10.1080/21505594.2017.1313372 · Cited by 1,523
Self-citationAntimicrobial peptides: Application informed by evolution
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Identification of antimicrobial peptides from the human gut microbiome using deep learning
Ma, Y., Guo, Z., Xia, B., Zhang, Y., Liu, X., Yu, Y., Tang, N., Tong, X., Wang, M., Ye, X., et al. (2022) · Nature Biotechnology · doi:10.1038/s41587-022-01226-0 · Cited by 490
Antimicrobial peptides (AMPs): A promising class of antimicrobial compounds
Erdem Büyükkiraz, M., & Kesmen, Z. (2022) · Journal of Applied Microbiology · doi:10.1111/jam.15314 · Cited by 454
Host defense antimicrobial peptides as antibiotics: design and application strategies
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Metadata
- Authors
- Gagnon, M. G., Roy, R. N., Lomakin, I. B., Florin, T., Mankin, A. S., & Steitz, T. A.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2016-01-24
- Volume
- 44
- Issue
- 5
- Pages
- 2439-2450
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- OpenAlex
- W2257180174
- Cited by
- 186
- References
- 6
- FWCI
- 13.58
- Type
- journal article
- Language
- en
- Open access
- gold
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- Gagnon, M. G., Roy, R. N., Lomakin, I. B., Florin, T., Mankin, A. S., & Steitz, T. A. (2016). Structures of proline-rich peptides bound to the ribosome reveal a common mechanism of protein synthesis inhibition. Nucleic Acids Research. https://doi.org/10.1093/nar/gkw018
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