Abstract
The ribosomally synthesized and posttranslationally modified peptides (RiPPs), also called ribosomal peptide natural products (RPNPs), form a growing superfamily of natural products that are produced by many different organisms and particularly by bacteria. They are derived from precursor polypeptides whose modification by various dedicated enzymes helps to establish a vast array of chemical motifs. RiPPs have attracted much interest as a source of potential therapeutic agents, and in particular as alternatives to conventional antibiotics to address the bacterial resistance crisis. However, their ecological roles in nature are poorly understood and explored. The present review describes major RiPP actors in competition within microbial communities, the main ecological and physiological functions currently evidenced for RiPPs, and the microbial ecosystems that are the sites for these functions. We envision that the study of RiPPs may lead to discoveries of new biological functions and highlight that a better knowledge of how bacterial RiPPs mediate inter-/intraspecies and interkingdom interactions will hold promise for devising alternative strategies in antibiotic development.
Highlights
The ribosomally synthesized and posttranslationally modified peptides (RiPPs), called ribosomal peptide natural products (RPNPs), form a growing superfamily of natural products that are produced by many different organisms and by bacteria
Microbial RiPPs are the most documented among known RiPPs, with a huge number of studies on their structures, structure/activity relationships, mechanisms of action, and biosynthesis, concerning in particular the posttranslational modifications and their dedicated enzymes
RiPPs’ antibiotic properties and biosynthesis pathways are currently well-studied with the purpose of identifying alternative strategies to the use of conventional antibiotics in the context of the microbial resistance crisis and the One Health context approved by the World Health Organization, RiPPs’ ecological roles remain poorly documented
Summary
X Yanyan Li (李 艳艳) and X Sylvie Rebuffat From the Laboratory Molecules of Communication and Adaptation of Microorganisms (MCAM, UMR 7245 CNRS-MNHN), National Museum of Natural History (MNHN), CNRS, CP 54, 57 rue Cuvier 75005 Paris, France. The ribosomally synthesized and posttranslationally modified peptides (RiPPs), called ribosomal peptide natural products (RPNPs), form a growing superfamily of natural products that are produced by many different organisms and by bacteria They are derived from precursor polypeptides whose modification by various dedicated enzymes helps to establish a vast array of chemical motifs. A large number of these natural products (NPs) originate from large multifunctional enzymatic complexes, nonribosomal peptide synthetases (NRPSs), polyketide synthases (PKSs), or hybrid PKS/NRPS systems [18, 19] Another broad and diverse class of natural products consists of the superfamily of ribosomally derived molecules, the so-called ribosomally synthe-. The scope of this review will cover different classes of bacterial RiPPs and summarize current knowledge of their natural functions, in the context of interactions within microbial communities and with their hosts
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