Evidence map›Paper›PMID 29483640›Full record

ArticleNature chemical biology2018

Resistance to nonribosomal peptide antibiotics mediated by D-stereospecific peptidases.

Yong-Xin Li, Zheng Zhong, Peng Hou, Wei-Peng Zhang, Pei-Yuan Qian

Erratum issuedAbstract read
PubMed Publisher
In one paragraph

Article in Nature chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
–field-weighted citation impact
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

30 citing papers in PubMed.

  1. Article
  2. Multicyclic D-Stereospecific Hydrolase Dimer With High Sustained Activity.Angewandte Chemie (International ed. in English) · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Natural Products That Contain Higher Homologated Amino Acids.Chembiochem : a European journal of chemical biology · 2024
    Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Frontiers in microbiology · 2022
    Article
  15. Article
  16. Review
  17. Natural products that target the cell envelope.Current opinion in microbiology · 2021
    Review
  18. Review
  19. Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Yong-Xin LiDepartment of Ocean Science and Division of Life Science, Hong Kong University of Science and Technology, Clear Water Bay, Hong Kong, China.
Zheng ZhongDepartment of Ocean Science and Division of Life Science, Hong Kong University of Science and Technology, Clear Water Bay, Hong Kong, China.ORCID 0000-0002-1262-4115
Peng HouDepartment of Ocean Science and Division of Life Science, Hong Kong University of Science and Technology, Clear Water Bay, Hong Kong, China.
Wei-Peng ZhangDepartment of Ocean Science and Division of Life Science, Hong Kong University of Science and Technology, Clear Water Bay, Hong Kong, China.
Pei-Yuan QianDepartment of Ocean Science and Division of Life Science, Hong Kong University of Science and Technology, Clear Water Bay, Hong Kong, China. boqianpy@ust.hk.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nonribosomal peptide antibiotics, including polymyxin, vancomycin, and teixobactin, most of which contain D-amino acids, are highly effective against multidrug-resistant bacteria. However, overusing antibiotics while ignoring the risk of resistance arising has inexorably led to widespread emergence of resistant bacteria. Therefore, elucidation of the emerging mechanisms of resistance to nonribosomal peptide antibiotics is critical to their implementation. Here we describe a networking-associated genome-mining platform for linking biosynthetic building blocks to resistance components associated with biosynthetic gene clusters. By applying this approach to 5,585 complete bacterial genomes spanning the entire domain of bacteria, with subsequent chemical and enzymatic analyses, we demonstrate a mechanism of resistance toward nonribosomal peptide antibiotics that is based on hydrolytic cleavage by D-stereospecific peptidases. Our finding reveals both the widespread distribution and broad-spectrum resistance potential of D-stereospecific peptidases, providing a potential early indicator of antibiotic resistance to nonribosomal peptide antibiotics.

Indexed as

Anti-Bacterial AgentsAntimicrobial Cationic PeptidesBacteriaComputational BiologyDrug Resistance, BacterialDrug Resistance, Multiple, BacterialGenome, BacterialHydrolysisKineticsMultigene FamilyMutationPeptide HydrolasesPeptidesProtein BindingRibosomesStereoisomerismAnti-Bacterial AgentsAntimicrobial Cationic Peptidesbogorol APeptide HydrolasesPeptides

Identifiers

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.