Evidence map›Paper›PMID 41009919›Full record

ArticleAntibiotics (Basel, Switzerland)2025

α-Amylase-Mediated Antibiotic Degradation and Sequestration in

Robert K Murray, Allison E Martin, Sarah Zipkowitz, Nusrat Jahan, Tony D Davis, Whitni K Redman

Abstract read
In one paragraph

Article in Antibiotics (Basel, Switzerland), 2025. 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
–field-weighted citation impact
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.

  1. 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

6 authors.

Robert K MurrayDepartment of Biological Sciences, Binghamton University, Binghamton, NY 13902, USA.
Allison E MartinDepartment of Pharmaceutical Sciences, School of Pharmacy and Pharmaceutical Sciences, Binghamton University, Binghamton, NY 13902, USA.
Sarah ZipkowitzDepartment of Biological Sciences, Binghamton University, Binghamton, NY 13902, USA.ORCID 0000-0003-1005-331X
Nusrat JahanDepartment of Biological Sciences, Binghamton University, Binghamton, NY 13902, USA.
Tony D DavisDepartment of Pharmaceutical Sciences, School of Pharmacy and Pharmaceutical Sciences, Binghamton University, Binghamton, NY 13902, USA.ORCID 0000-0001-5629-7075
Whitni K RedmanDepartment of Biological Sciences, Binghamton University, Binghamton, NY 13902, USA.

Funding

Interrogation of Microbial Natural Product MethyltransferasesR00GM129454 · NIGMS · STATE UNIVERSITY OF NY,BINGHAMTON · PI DAVIS, TONY D. · 2021 to 2023
$747k
NIGMS NIH HHS R00 GM129454
6 · The paper itself

Abstract

backgroundAs of 2022, 80% of all documented microbial infections are biofilm-associated: communities of microorganisms adhered to a surface and enclosed in a complex extracellular polymeric substance (EPS). The EPS acts as a physical barrier protecting the bacteria from antimicrobial agents and host immune responses. To combat this hurdle, the application of glycoside hydrolases (GH) has been investigated due to their ability to cleave particular structural polysaccharides within the EPS, thus breaking down the protective barrier and improving antibiotic clearance. While various studies demonstrate the capacity of GHs to improve antibiotic efficacy against biofilms in combination, there is clear differential success between these treatments depending on the GH and antibiotic chosen. Due to the overlap of GH targets and antibiotic structures, it is imperative to ensure that the antibiotics in combinatorial treatments are not degraded by the GH.

methodsThis study aimed to screen the GH α-amylase produced from

resultsIncreased MICs in the presence of GHs as well as decreased antibiotic clearance against 2-day biofilms were suggestive of antibiotic degradation. LC-MS/MS stability assays of tetracycline and ciprofloxacin in the presence and absence of α-amylase further demonstrated the α-amylase-mediated antibiotic sequestration. Differential scanning fluorimetry (DSF) assays confirmed α-amylase-antibiotic interactions.

conclusionsThis study suggests that α-amylase is capable of degrading and sequestering a variety of antibiotics, and the degree to which these phenomena occur varies depending upon the source of the GH. As a potential treatment for biofilm-associated infections, it is imperative that the GH + antibiotic combinations are determined compatible prior to clinical use.

Indexed as

antibioticbiofilmglycoside hydrolasePseudomonas aeruginosatreatment

Identifiers

PMID41009919
PMCPMC12466716

What OpenQuestion holds

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Registered trials

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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.