Evidence map›Paper›PMID 36121287›Full record

ArticleMicrobiology spectrum2022

Structural Basis of Peptide-Based Antimicrobial Inhibition of a Resistance-Nodulation-Cell Division Multidrug Efflux Pump.

Meinan Lyu, Julio C Ayala, Isabella Chirakos, Chih-Chia Su, William M Shafer, Edward W Yu

Open access · goldAbstract read
In one paragraph

Article in Microbiology spectrum, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. A One Health Perspective onMicroorganisms · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Review
  9. Article
  10. Structural analysis of resistance-nodulation cell division transporters.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Exploring the inhibitory potential ofFrontiers in molecular biosciences · 2023
    Article
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

6 authors at 2 institutions in 1 country.

Meinan LyuDepartment of Pharmacology, Case Western Reserve Universitygrid.67105.35 School of Medicine, Cleveland, Ohio, USA.
Julio C AyalaDepartment of Microbiology and Immunology, Emory University School of Medicinegrid.471395.d, Atlanta, Georgia, USA.
Isabella ChirakosDepartment of Pharmacology, Case Western Reserve Universitygrid.67105.35 School of Medicine, Cleveland, Ohio, USA.
Chih-Chia SuDepartment of Pharmacology, Case Western Reserve Universitygrid.67105.35 School of Medicine, Cleveland, Ohio, USA.
William M ShaferDepartment of Microbiology and Immunology, Emory University School of Medicinegrid.471395.d, Atlanta, Georgia, USA.ORCID 0000-0001-9303-8777
Edward W YuDepartment of Pharmacology, Case Western Reserve Universitygrid.67105.35 School of Medicine, Cleveland, Ohio, USA.ORCID 0000-0001-5912-1227
University School · USEmory University · US

Funding

GONOCOCCI: GENETICS OF RESISTANCE TO PMN PROTEINSR01AI021150 · NIAID · EMORY UNIVERSITY · PI SHAFER, WILLIAM MAURICE · 1985 to 2025
$5.5M
Emerging antibiotic resistance in Gram-negative pathogensR01AI145069 · NIAID · CASE WESTERN RESERVE UNIVERSITY · PI YU, EDWARD W · 2019 to 2023
$3.3M
BLRD VA IK6 BX005390NIAID NIH HHS R01 AI021150NIAID NIH HHS R01 AI145069
6 · The paper itself

Abstract

Bacterial efflux pumps in the resistance-nodulation-cell division (RND) family of Gram-negative bacteria contribute significantly to the development of antimicrobial resistance by many pathogens. In this study, we selected the MtrD transporter protein of Neisseria gonorrhoeae as it is the sole RND pump possessed by this strictly human pathogen and can export multiple antimicrobials, including antibiotics, bile salts, detergents, dyes, and antimicrobial peptides. Using knowledge from our previously published structures of MtrD in the presence or absence of bound antibiotics as a model and the known ability of MtrCDE to export cationic antimicrobial peptides, we hypothesized that cationic peptides could be accommodated within MtrD binding sites. Furthermore, we thought that MtrD-bound peptides lacking antibacterial action could sensitize bacteria to an antibiotic normally exported by the MtrCDE efflux pump or other similar RND-type pumps possessed by different Gram-negative bacteria. We now report the identification of a novel nonantimicrobial cyclic cationic antimicrobial peptide, which we termed CASP (

Indexed as

Anti-Infective AgentsColistinAmino AcidsAnti-Bacterial AgentsBacterial ProteinsBile Acids and SaltsCell DivisionColoring AgentsCryoelectron MicroscopyDetergentsDrug Resistance, Multiple, BacterialHumansNeisseria gonorrhoeaeNovobiocinAmino AcidsAnti-Bacterial AgentsAnti-Infective AgentsBacterial ProteinsBile Acids and SaltsColistinColoring AgentsDetergentsNovobiocinmembrane proteinsMtrDmultidrug effluxmultidrug resistanceNeisseria gonorrhoeaesecondary transporter mechanism

Identifiers

PMID36121287
PMCPMC9603588
OpenAlexW4296323066

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.