Evidence map›Paper›PMID 35115684›Full record

ArticleCommunications biology2022

Cell density-dependent antibiotic tolerance to inhibition of the elongation machinery requires fully functional PBP1B.

Addison Grinnell, Ryan Sloan, Randy M Morgenstein

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

8 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Genetic basis of cefiderocol resistance inMicrobiology spectrum · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. 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

3 authors at 1 institution in 1 country.

Addison GrinnellDepartment of Microbiology and Molecular Genetics, Oklahoma State University, Stillwater, OK, USA.
Ryan SloanDepartment of Microbiology and Molecular Genetics, Oklahoma State University, Stillwater, OK, USA.
Randy M MorgensteinDepartment of Microbiology and Molecular Genetics, Oklahoma State University, Stillwater, OK, USA. randy.morgenstein@okstate.edu.ORCID http://orcid.org/0000-0003-0749-6830
Oklahoma State University · US

Funding

Beyond cell shape: A novel role for the bacterial actin MreB in chemotaxisR15GM129636 · NIGMS · OKLAHOMA STATE UNIVERSITY STILLWATER · PI MORGENSTEIN, RANDY M · 2020 to 2023
$875k
NIGMS NIH HHS R15 GM129636U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) 1R15GM129636-01A1
6 · The paper itself

Abstract

The peptidoglycan (PG) cell wall provides shape and structure to most bacteria. There are two systems to build PG in rod shaped organisms: the elongasome and divisome, which are made up of many proteins including the essential MreB and PBP2, or FtsZ and PBP3, respectively. The elongasome is responsible for PG insertion during cell elongation, while the divisome is responsible for septal PG insertion during division. We found that the main elongasome proteins, MreB and PBP2, can be inhibited without affecting growth rate in a quorum sensing-independent density-dependent manner. Before cells reach a particular cell density, inhibition of the elongasome results in different physiological responses, including intracellular vesicle formation and an increase in cell size. This inhibition of MreB or PBP2 can be compensated for by the presence of the class A penicillin binding protein, PBP1B. Furthermore, we found this density-dependent growth resistance to be specific for elongasome inhibition and was consistent across multiple Gram-negative rods, providing new areas of research into antibiotic treatment.

Indexed as

Cell CountCephalexinDose-Response Relationship, DrugDrug Resistance, BacterialEscherichia coliEscherichia coli ProteinsGene Expression Regulation, BacterialPenicillin-Binding ProteinsPeptidoglycan GlycosyltransferaseSerine-Type D-Ala-D-Ala CarboxypeptidaseThiourea2,6-dichlorobenzylthiopseudoureaCephalexinEscherichia coli Proteinspenicillin-binding protein 1B, E coliPenicillin-Binding ProteinsPeptidoglycan GlycosyltransferaseSerine-Type D-Ala-D-Ala CarboxypeptidaseThiourea

Identifiers

PMID35115684
PMCPMC8813938
OpenAlexW4210770690

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.