A Pyranose-2-Phosphate Motif Is Responsible for Both Antibiotic Import and Quorum-Sensing Regulation in

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We succeeded in understanding how the periplasmic protein AccA from the pathogen A. tumefaciens can bind both the plant compound agrocinopine and the antibiotic agrocin 84. Whereas agrocinopine acts as a nutrient and regulatory signal in A. tumefaciens, agrocin 84 is lethal once degraded by the enzyme AccF into a toxic moiety. We identified the pyranose-2-phosphate-like moiety shared by these two ligands as the key recognition template for AccA. We hypothesized that agrocin 84 would kill all agrobacteria possessing AccA and AccF and that AccA would be a gateway allowing the importation of any compound possessing a pyranose-2-phosphate motif. We experimentally confirmed this, using synthetic derivative compounds of agrocinopine. Furthermore, using affinity and in vivo assays, we showed that arabinose-2-phosphate, resulting from the cleavage of agrocinopine by AccF, is the effector of the transcriptional repressor AccR, that controls quorum-sensing and virulence plasmid propagation. Therefore, we have identified an original and specific key molecular motif (pyranose-2-phosphate) allowing a selective passage of active compounds into the pathogen cells and acting as signals once the active compounds are cleaved into this key motif. Our work opens up new opportunities to rationally design novel antibiotics.

Vyšlo v časopise: A Pyranose-2-Phosphate Motif Is Responsible for Both Antibiotic Import and Quorum-Sensing Regulation in. PLoS Pathog 11(8): e32767. doi:10.1371/journal.ppat.1005071
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.ppat.1005071

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