Evidence map›Paper›PMID 37289051›Full record

ArticleMicrobiology spectrum2023

Cryo-Electron Microscopy Structures of a Campylobacter Multidrug Efflux Pump Reveal a Novel Mechanism of Drug Recognition and Resistance.

Zhemin Zhang, Nicholas Lizer, Zuowei Wu, Christopher E Morgan, Yuqi Yan, Qijing Zhang, Edward W Yu

Open access · goldAbstract read
In one paragraph

Article in Microbiology spectrum, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

14 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Review
  3. Phenotypic Resistance of Ciprofloxacin and Azithromycin ResistantbioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Emerging antibiotic resistance by various novel proteins/enzymes.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2025
    Review
  8. Article
  9. Mutation-based mechanism and evolution of the potent multidrug efflux pump RE-CmeABC inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Review
  11. Structural analysis of resistance-nodulation cell division transporters.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  12. Article
  13. Article
  14. Review
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

7 authors at 2 institutions in 1 country.

Zhemin ZhangDepartment of Pharmacology, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA.
Nicholas LizerDepartment of Veterinary Microbiology, College of Veterinary Medicine, Iowa State University, Ames, Iowa, USA.
Zuowei WuDepartment of Veterinary Microbiology, College of Veterinary Medicine, Iowa State University, Ames, Iowa, USA.ORCID 0000-0003-2153-5816
Christopher E MorganDepartment of Pharmacology, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA.
Yuqi YanDepartment of Pharmacology, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA.
Qijing ZhangDepartment of Veterinary Microbiology, College of Veterinary Medicine, Iowa State University, Ames, Iowa, USA.
Edward W YuDepartment of Pharmacology, Case Western Reserve University School of Medicine, Cleveland, Ohio, USA.ORCID 0000-0001-5912-1227
University School · USIowa State University · US

Funding

Emerging antibiotic resistance in Gram-negative pathogensR01AI145069 · NIAID · CASE WESTERN RESERVE UNIVERSITY · PI YU, EDWARD W · 2019 to 2023
$3.3M
Emerging multidrug resistance mechanisms in CampylobacterR01AI140669 · NIAID · IOWA STATE UNIVERSITY · PI YU, EDWARD W, ZHANG, QIJING · 2020 to 2024
$3.2M
NIAID NIH HHS R01 AI140669NIAID NIH HHS R01 AI145069
6 · The paper itself

Abstract

Campylobacter jejuni is a bacterium that is commonly present in the intestinal tracts of animals. It is also a major foodborne pathogen that causes gastroenteritis in humans. The most predominant and clinically important multidrug efflux system in C. jejuni is the CmeABC (Campylobacter multidrug efflux) pump, a tripartite system that includes an inner membrane transporter (CmeB), a periplasmic fusion protein (CmeA), and an outer membrane channel protein (CmeC). This efflux protein machinery mediates resistance to a number of structurally diverse antimicrobial agents. A recently identified CmeB variant, termed resistance enhancing CmeB (RE-CmeB), can increase its multidrug efflux pump activity, likely by influencing antimicrobial recognition and extrusion. Here, we report structures of RE-CmeB in its apo form as well as in the presence of four different drugs by using single-particle cryo-electron microscopy (cryo-EM). Coupled with mutagenesis and functional studies, this structural information allows us to identify critical amino acids that are important for drug resistance. We also report that RE-CmeB utilizes a somewhat unique subset of residues to bind different drugs, thereby optimizing its ability to accommodate different compounds with distinct scaffolds. These findings provide insights into the structure-function relationship of this newly emerged antibiotic efflux transporter variant in Campylobacter.

Indexed as

CampylobacterCampylobacter jejuniAnimalsAnti-Bacterial AgentsBacterial ProteinsCryoelectron MicroscopyDrug Resistance, Multiple, BacterialHumansMembrane Transport ProteinsMicrobial Sensitivity TestsAnti-Bacterial AgentsBacterial ProteinsMembrane Transport ProteinsCampylobacter jejunicryo-EMmultidrug efflux pumpmultidrug resistanceRE-CmeB

Identifiers

PMID37289051
PMCPMC10434076
OpenAlexW4379769140

What OpenQuestion holds

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LicenceCC BY
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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.