Cited by 19Microbial Natural Products and BiosynthesisAntimicrobial Peptides and ActivitiesRNA and protein synthesis mechanisms

Translation-Targeting RiPPs and Where to Find Them

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Travin, Dmitrii Y., Bikmetov, Dmitry, Severinov, Konstantin·2020·Frontiers in Genetics

Abstract

Prokaryotic translation is among the major targets of diverse natural products with antibacterial activity including several classes of clinically relevant antibiotics. In this review, we summarize the information about the structure, biosynthesis, and modes of action of translation inhibiting ribosomally synthesized and post-translationally modified peptides (RiPPs). Azol(in)e-containing RiPPs are known to target translation, and several new compounds inhibiting the ribosome have been characterized recently. We performed a systematic search for biosynthetic gene clusters (BGCs) of azol(in)e-containing RiPPs. This search uncovered several groups of clusters that likely direct the synthesis of novel compounds, some of which may be targeting the ribosome.

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Crossref · 10.3389/fgene.2020.00226

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  • Class IV lanthipeptides are characterized by multiple lanthionine rings and exert strong antimicrobial activity against several Gram-positive bacteria, including Streptococcus spp, Clostridium difficile, and Bacillus spp.

    “class IV lanthipeptides are characterized by multiple lanthionine rings and exert strong antimicrobial activity against several Gram-positive bacteria, including Streptococcus spp, Clostridium difficile, and Bacillus spp. [80, 81].”

    From Bile Salt Hydrolase Activity in the Food-Derived Strain Levilactobacillus brevis M3R3: Genomic and Functional Characterization (2026) · cites this paper as [80]

    The Introduction’s Thiopeptides section mentions class I lanthipeptides only in passing; it does not describe class IV lanthipeptides or lanthionine rings. It reports activity against Clostridium difficile for a thiopeptide derivative, not a class IV lanthipeptide. Searches for class IV, lanthionine rings, and the named bacteria found no passage supporting the attributed claim; the indexed copy has no page numbers. (LLM, conf=0.76)

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Authors
Travin, D. Y., Bikmetov, D., & Severinov, K.
Affiliations
  • Skolkovo Institute of Science and Technology (RU)
  • Russian Academy of Sciences (RU)
  • Rutgers, The State University of New Jersey (US)
Corresponding author
Travin, Dmitrii Y.
Venue
Frontiers in Genetics
Published
2020-03-31
Volume
11
Pages
226-226
ISSN
1664-8021 (ISSN-L)
OpenAlex
W3014119863
Cited by
19
References
99
Citations by year
2026: 2 · 2025: 5 · 2024: 2 · 2023: 2 · 2022: 4 · 2021: 3 · 2020: 1
FWCI
0.33
Type
journal article
Language
en
Open access
Locations
  • Frontiers in Genetics (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
Russian Science Foundation (19-14-00266)
Topics
  • Health Sciences › Medicine › Pharmacology › Microbial Natural Products and Biosynthesis
  • Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Keywords
ribosomally synthesized and post-translationally modified peptides, protein synthesis inhibition, biosynthetic gene clusters, antibiotic biosynthesis, antibacterial natural products, prokaryotic translation

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