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A Trojan-Horse Peptide-Carboxymethyl-Cytidine Antibiotic from Bacillus amyloliquefaciens

Marina Serebryakova1,2, Darya Tsibulskaya1, Olga Mokina1,3

  • 1Institute of Gene Biology, Russian Academy of Science , 34/5 Vavilov str., 119334 Moscow, Russia.

Journal of the American Chemical Society
|December 10, 2016
PubMed

Insights

Researchers discovered a new microcin C-like antibiotic from Bacillus amyloliquefaciens. This novel compound targets aspartyl-tRNA synthetase and features carboxymethylation to prevent bacterial resistance.

Area of Science:

  • Microbiology
  • Biochemistry
  • Molecular Biology

Background:

  • Microcin C is a Trojan-horse peptide-adenylate antibiotic.
  • It inhibits aspartyl-tRNA synthetase after intracellular processing.
  • Adenylation of peptide precursors is catalyzed by MccB THIF-type NAD/FAD adenylyltransferases.

Purpose of the Study:

  • To characterize a novel microcin C-like compound from Bacillus amyloliquefaciens.
  • To investigate the enzymatic modifications involved in its synthesis.
  • To assess its biological activity and potential for overcoming resistance.

Main Methods:

  • In vitro and cellular assays using Bacillus amyloliquefaciens.
  • Enzymatic assays to study MccB and MccS activity.
  • Analysis of microcin structure and function.

Main Results:

  • Bacillus amyloliquefaciens MccB attaches a terminal cytidine monophosphate to precursor peptides.
  • The cytosine moiety is further modified by carboxymethylation, mediated by MccB and MccS.
  • These modified microcin C-like compounds are active against aspartyl-tRNA synthetase and resist common resistance mechanisms.

Conclusions:

  • A novel class of microcin C-like antibiotics with terminal cytosine modifications has been identified.
  • Carboxymethylation of the cytosine moiety is a key modification that enhances biological activity and prevents resistance.
  • These findings expand the known repertoire of peptide modifications for developing new antibiotics.

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