Evidence map›Paper›PMID 30870966›Full record

ArticleSensors (Basel, Switzerland)2019

Effect of Lactamase Inhibitors on the Biosensor Penp during the Measurement of Lactam Antibiotics Concentration.

Dagoberto Soto, Camila Silva, Cristian Ugalde, Kwok-Yin Wong, Yun-Chung Leung, Lok-Yan So, Max Andresen

Open access · goldAbstract read
In one paragraph

Article in Sensors (Basel, Switzerland), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 99% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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 2 countries.

Dagoberto SotoDepartamento de Medicina Intensiva, Facultad de Medicina y Hospital Clínico, Pontificia Universidad Católica de Chile, Santiago 8330024, Chile. dasotom@uc.cl.
Camila SilvaDepartamento de Medicina Intensiva, Facultad de Medicina y Hospital Clínico, Pontificia Universidad Católica de Chile, Santiago 8330024, Chile. cfsilvag2@gmail.com.
Cristian UgaldeDepartamento de Medicina Intensiva, Facultad de Medicina y Hospital Clínico, Pontificia Universidad Católica de Chile, Santiago 8330024, Chile. cristian.ugalde@gmail.com.
Kwok-Yin WongState Key Laboratory of Chemical Biology and Drug Discovery, Department of Applied Biology and Chemical Technology, The Hong Kong Polytechnic University, Hung Hom, Kowloon, Hong Kong. kwok-yin.wong@polyu.edu.hk.
Yun-Chung LeungState Key Laboratory of Chemical Biology and Drug Discovery, Department of Applied Biology and Chemical Technology, The Hong Kong Polytechnic University, Hung Hom, Kowloon, Hong Kong. thomas.yun-chung.leung@polyu.edu.hk.
Lok-Yan SoState Key Laboratory of Chemical Biology and Drug Discovery, Department of Applied Biology and Chemical Technology, The Hong Kong Polytechnic University, Hung Hom, Kowloon, Hong Kong. annsoly@gmail.com.ORCID 0000-0002-7370-0986
Max AndresenDepartamento de Medicina Intensiva, Facultad de Medicina y Hospital Clínico, Pontificia Universidad Católica de Chile, Santiago 8330024, Chile. andresen@med.puc.cl.
Pontificia Universidad Católica de Chile · CLHong Kong Polytechnic University · HK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PenP is a fluorescent biosensor of lactam antibiotics (LA). It is structurally derived from the mutant lactamase TEM-1 comprising the substitution E166C, where fluorescein is covalently linked to cysteine. The presence of LA in the medium produces a change in the intrinsic fluorescence level of the biosensor, and the integral of the fluorescence level over time correlates directly with the LA concentration. Previously, we have successfully used PenP to determine the concentration of lactam antibiotics in clinical samples. The use of lactamase inhibitors (LI) is a common strategy to enhance the effect of LA due to the inhibition of an important resistance mechanism of pathogenic microorganisms. Structurally, LI and LA share the common element of recognition of lactamases (the lactam ring), but they differ in the reversibility of the mechanism of interaction with said enzyme. Because the biological recognition domain of PenP is derived from a lactamase, LI is expected to interfere with the PenP detection capabilities. Surprisingly, this work provides evidence that the effect of LI is marginal in the determination of LA concentration mediated by PenP.

Indexed as

Anti-Bacterial Agentsbeta-LactamasesBiosensing TechniquesLactamsAnti-Bacterial Agentsbeta-LactamasesLactamsbiosensorlactam antibioticslactamase inhibitorsPenPuse

Identifiers

PMID30870966
PMCPMC6427286
OpenAlexW2922370776

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.