Autor: |
Gless, Bengt H., Bejder, Benjamin S., Monda, Fabrizio, Bojer, Martin S., Ingmer, Hanne, Olsen, Christian A. |
Zdroj: |
Journal of the American Chemical Society; 20210101, Issue: Preprints |
Abstrakt: |
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 monocytogenesthat 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. |
Databáze: |
Supplemental Index |
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