Evidence map›Paper›PMID 40503650›Full record

ArticleACS infectious diseases2025

An Engineered Prodrug Selectively Suppresses β-Lactam-Resistant Bacteria in a Mixed Microbial Setting.

Addison M Duda, Helena R Ma, César A Villalobos, Sophia A Kuhn, Sarah S Angle, Katherine He, Abigail C Jackson, Christine M Suh, Elena A Puccio, Deverick J Anderson and 3 more

Abstract read
In one paragraph

Article in ACS infectious diseases, 2025. 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
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.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors.

Addison M DudaDepartment of Chemistry, Duke University, Durham, North Carolina 27708, United States.ORCID 0000-0002-8116-4714
Helena R MaDepartment of Biomedical Engineering, Duke University, Durham, North Carolina 27708, United States.
César A VillalobosDepartment of Biomedical Engineering, Duke University, Durham, North Carolina 27708, United States.
Sophia A KuhnDepartment of Chemistry, Duke University, Durham, North Carolina 27708, United States.
Sarah S AngleDepartment of Chemistry, Duke University, Durham, North Carolina 27708, United States.ORCID 0009-0002-4700-1513
Katherine HeDepartment of Biomedical Engineering, Duke University, Durham, North Carolina 27708, United States.
Abigail C JacksonDepartment of Chemistry, Duke University, Durham, North Carolina 27708, United States.
Christine M SuhDepartment of Chemistry, Duke University, Durham, North Carolina 27708, United States.
Elena A PuccioDepartment of Chemistry, Duke University, Durham, North Carolina 27708, United States.
Deverick J AndersonDivision of Infectious Diseases, Department of Medicine, Duke University, Durham, North Carolina 27710, United States.
Vance G FowlerDivision of Infectious Diseases, Department of Medicine, Duke University, Durham, North Carolina 27710, United States.
Lingchong YouDepartment of Biomedical Engineering, Duke University, Durham, North Carolina 27708, United States.
Katherine J FranzDepartment of Chemistry, Duke University, Durham, North Carolina 27708, United States.ORCID 0000-0002-9015-0998

Funding

Pharmacological Sciences Training ProgramT32GM133352 · NIGMS · DUKE UNIVERSITY · PI Cynthia M Kuhn, David M MacAlpine · 2020 to 2026
$3.8M
Post-antibiotic effect and design of optimal antibiotic dosing protocolsR01GM098642 · NIGMS · DUKE UNIVERSITY · PI YOU, LINGCHONG · 2011 to 2025
$3.6M
NIGMS NIH HHS R01 GM098642NIGMS NIH HHS T32 GM133352
6 · The paper itself

Abstract

The rise of β-lactam resistance necessitates new strategies to combat bacterial infections. We purposefully engineered the β-lactam prodrug AcephPT to exploit β-lactamase activity to selectively suppress resistant bacteria producing extended-spectrum-β-lactamases (ESBLs). Selective targeting of resistant bacteria requires avoiding interaction with penicillin-binding proteins, the conventional targets of β-lactam antibiotics, while maintaining recognition by ESBLs to activate AcephPT only in resistant cells. We show that AcephPT selectively suppresses Gram-negative ESBL-producing bacteria in clonal populations and in mixed microbial cultures, with effective selectivity for both lab strains and clinical isolates expressing ESBLs. Time-course NMR experiments confirm the hydrolytic activation of AcephPT exclusively by ESBL-producing bacteria. In mixed microbial cultures, AcephPT suppresses proliferation of an ESBL-producing strain while sustaining growth of β-lactamase-nonproducing bacteria, highlighting its potential to combat β-lactam resistance while promoting antimicrobial stewardship.

Indexed as

Anti-Bacterial Agentsbeta-Lactam Resistancebeta-LactamsGram-Negative BacteriaProdrugsbeta-LactamasesHumansMicrobial Sensitivity TestsAnti-Bacterial Agentsbeta-Lactamasesbeta-LactamsProdrugsantibiotic resistanceantimicrobial stewardshipextended-spectrum-β-lactamasepolymicrobialprodrugβ-lactam

Identifiers

PMID40503650
PMCPMC13012811

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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.