Rearrangement of Thiodepsipeptides by S → N Acyl Shift Delivers Homodetic Autoinducing Peptides
Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
Dokumenter
- Fulltext
Accepteret manuskript, 1,28 MB, PDF-dokument
Group behavior in many bacteria relies on chemically induced communication called quorum sensing (QS), which plays important roles in the regulation of colonization, biofilm formation, and virulence. In Gram-positive bacteria, QS is often mediated by cyclic ribosomally synthesized and posttranslationally modified peptides (RiPPs). In staphylococci, for example, most of these so-called autoinducing peptides (AIPs) contain a conserved thiolactone functionality, which has also been predicted to constitute a structural feature of AIPs from other genera. Here, we show that pentameric AIPs from Lactiplantibacillus plantarum, Clostridium perfringens, and Listeria monocytogenes that were previously presumed to be thiolactone-containing structures readily rearrange to become homodetic cyclopeptides. This finding has implications for the developing understanding of cross-species and potential cross-genus communication of bacteria and may help guide the discovery of peptide ligands to perturb their function.
Originalsprog | Engelsk |
---|---|
Tidsskrift | Journal of the American Chemical Society |
Vol/bind | 143 |
Udgave nummer | 28 |
Sider (fra-til) | 10514–10518 |
ISSN | 0002-7863 |
DOI | |
Status | Udgivet - 2021 |
Bibliografisk note
Funding Information:
This work was supported by the Danish Independent Research Council–Natural Sciences (Grant No. 0135-00427B; C.A.O.) and the LEO Foundation Open Competition Grant (LF-OC-19-000039; C.A.O.).
Publisher Copyright:
© 2021 American Chemical Society.
Antal downloads er baseret på statistik fra Google Scholar og www.ku.dk
ID: 275827995