Evidence map›Paper›PMID 27934031›Full record

ArticleJournal of the American Chemical Society2016

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

Marina Serebryakova, Darya Tsibulskaya, Olga Mokina, Alexey Kulikovsky, Manesh Nautiyal, Arthur Van Aerschot, Konstantin Severinov, Svetlana Dubiley

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.7field-weighted citation impact, top 15% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 30 citations in OpenAlex.

  1. Late-Stage Posttranslational Assembly of Fosfazinomycins.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. ThiF-Like Enzyme Chemistry in Primary and Secondary Metabolism.Chembiochem : a European journal of chemical biology · 2025
    Review
  4. Review
  5. Indolylamide Macrocyclization by aOrganic letters · 2025
    Article
  6. Article
  7. Natural product reports · 2023
    Review
  8. Review
  9. Article
  10. Article
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  14. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 4 institutions in 2 countries.

Marina SerebryakovaInstitute of Gene Biology, Russian Academy of Science , 34/5 Vavilov str., 119334 Moscow, Russia.
Darya TsibulskayaInstitute of Gene Biology, Russian Academy of Science , 34/5 Vavilov str., 119334 Moscow, Russia.
Olga MokinaInstitute of Gene Biology, Russian Academy of Science , 34/5 Vavilov str., 119334 Moscow, Russia.
Alexey KulikovskyInstitute of Gene Biology, Russian Academy of Science , 34/5 Vavilov str., 119334 Moscow, Russia.
Manesh NautiyalKU Leuven , O&N Rega, Medicinal Chemistry, Herestraat 49 10, B-3000 Leuven, Belgium.
Arthur Van AerschotKU Leuven , O&N Rega, Medicinal Chemistry, Herestraat 49 10, B-3000 Leuven, Belgium.
Konstantin SeverinovInstitute of Gene Biology, Russian Academy of Science , 34/5 Vavilov str., 119334 Moscow, Russia.
Svetlana DubileyInstitute of Gene Biology, Russian Academy of Science , 34/5 Vavilov str., 119334 Moscow, Russia.
Skolkovo Institute of Science and Technology · RUInstitute of Gene Biology · RUKU Leuven · BELomonosov Moscow State University · RU

Funding

Exploring Peptide Conjugates as Trojan Horse Systems for Drug Design and DiscoveryR01AI117210 · NIAID · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI NAIR, SATISH K · 2016 to 2020
$2.2M
NIAID NIH HHS R01 AI117210
6 · The paper itself

Abstract

Microcin C and related antibiotics are Trojan-horse peptide-adenylates. The peptide part is responsible for facilitated transport inside the sensitive cell, where it gets processed to release a toxic warhead-a nonhydrolyzable aspartyl-adenylate, which inhibits aspartyl-tRNA synthetase. Adenylation of peptide precursors is carried out by MccB THIF-type NAD/FAD adenylyltransferases. Here, we describe a novel microcin C-like compound from Bacillus amyloliquefaciens. The B. amyloliquefaciens MccB demonstrates an unprecedented ability to attach a terminal cytidine monophosphate to cognate precursor peptide in cellular and cell free systems. The cytosine moiety undergoes an additional modification-carboxymethylation-that is carried out by the C-terminal domain of MccB and the MccS enzyme that produces carboxy-SAM, which serves as a donor of the carboxymethyl group. We show that microcin C-like compounds carrying terminal cytosines are biologically active and target aspartyl-tRNA synthetase, and that the carboxymethyl group prevents resistance that can occur due to modification of the warhead. The results expand the repertoire of known enzymatic modifications of peptides that can be used to obtain new biological activities while avoiding or limiting bacterial resistance.

Indexed as

Anti-Bacterial AgentsAspartate-tRNA LigaseBacillus amyloliquefaciensBacteriocinsComputational BiologyEnzyme InhibitorsMolecular StructureAnti-Bacterial AgentsAspartate-tRNA LigaseBacteriocinsEnzyme Inhibitorsmicrocin

Identifiers

PMID27934031
PMCPMC5152938
OpenAlexW2549596586

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.