Evidence map›Paper›PMID 26195528›Full record

ArticleAntimicrobial agents and chemotherapy2015

Differential Effects of Penicillin Binding Protein Deletion on the Susceptibility of Enterococcus faecium to Cationic Peptide Antibiotics.

George Sakoulas, Monika Kumaraswamy, Poochit Nonejuie, Brian J Werth, Micahel J Rybak, Joseph Pogliano, Louis B Rice, Victor Nizet

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

3 citing papers in PubMed, 5 citations in OpenAlex.

  1. Characteristics ofBioMed research international · 2018
    Article
  2. 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 1 country.

George SakoulasDepartment of Pediatrics, University of California San Diego School of Medicine, La Jolla, California, USA gsakoulas@ucsd.edu.
Monika KumaraswamyDepartment of Internal Medicine, University of California San Diego School of Medicine, La Jolla, California, USA.
Poochit NonejuieDepartment of Biological Sciences, University of California San Diego School of Medicine, La Jolla, California, USA.
Brian J WerthAnti-Infective Research Laboratory, Eugene Applebaum College of Pharmacy and Health Sciences, School of Medicine, Wayne State University, Detroit, Michigan, USA.
Micahel J RybakAnti-Infective Research Laboratory, Eugene Applebaum College of Pharmacy and Health Sciences, School of Medicine, Wayne State University, Detroit, Michigan, USA.
Joseph PoglianoDepartment of Biological Sciences, University of California San Diego School of Medicine, La Jolla, California, USA.
Louis B RiceDepartment of Internal Medicine, Warren Alpert Medical School, Brown University, Providence, Rhode Island, USA.
Victor NizetDepartment of Pediatrics, University of California San Diego School of Medicine, La Jolla, California, USA.
University of California, San Diego · USBrown University · USEugene Applebaum College of Pharmacy and Health Sciences · USWayne State University · US

Funding

TRAINING & OUTREACH COREU54HD071600 · NICHD · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BEST, BROOKIE MANNING · 2011 to 2015
$3.6M
NICHD NIH HHS U54 HD071600NICHD NIH HHS U54 HD071600-01
6 · The paper itself

Abstract

Beta-lactam antibiotics sensitize Enterococcus faecium to killing by endogenous antimicrobial peptides (AMPs) of the innate immune system and daptomycin through mechanisms yet to be elucidated. It has been speculated that beta-lactam inactivation of select E. faecium penicillin binding proteins (PBPs) may play a pivotal role in this sensitization process. To characterize the specific PBP inactivation that may be responsible for these phenotypes, we utilized a previously characterized set of E. faecium PBP knockout mutants to determine the effects of such mutations on the activity of daptomycin and the AMP human cathelicidin (LL-37). Enhanced susceptibility to daptomycin was dependent more on a cumulative effect of multiple PBP deletions than on inactivation of any single specific PBP. Selective knockout of PBPZ rendered E. faecium more vulnerable to killing by both recombinant LL-37 and human neutrophils, which produce the antimicrobial peptide in high quantities. Pharmacotherapy targeting multiple PBPs may be used as adjunctive therapy with daptomycin to treat difficult E. faecium infections.

Indexed as

Anti-Bacterial AgentsAntimicrobial Cationic PeptidesDaptomycinEnterococcus faeciumMicrobial Sensitivity TestsPenicillin-Binding ProteinsAnti-Bacterial AgentsAntimicrobial Cationic PeptidesDaptomycinPenicillin-Binding Proteins

Identifiers

PMID26195528
PMCPMC4576044
OpenAlexW1916720294

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.