Evidence map›Paper›PMID 40264290›Full record

ArticleFuture microbiology

Antimicrobial action and mechanism of piscidin against

Yunhai Wei, Wenjing Hu, Huancen Guo, Jinyu Zhang, Haiyan Dong, Chu Shen, Jingrui Cao, Zhongxin Wu, Lei Yin, Yuhai Gao

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In one paragraph

Article in Future microbiology. 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
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0citing papers in PubMed
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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

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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

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

10 authors.

Yunhai WeiDepartment of Gastrointestinal Surgery, Huzhou Central Hospital, Affiliated Central Hospital of Huzhou University, Huzhou, China.
Wenjing HuDepartment of Gastrointestinal Surgery, Huzhou Central Hospital, Affiliated Central Hospital of Huzhou University, Huzhou, China.
Huancen GuoDepartment of Gastrointestinal Surgery, Huzhou Central Hospital, Affiliated Central Hospital of Huzhou University, Huzhou, China.
Jinyu ZhangDepartment of Gastrointestinal Surgery, Huzhou Central Hospital, Affiliated Central Hospital of Huzhou University, Huzhou, China.
Haiyan DongDepartment of Basic Medical Science, Huzhou University, Huzhou, China.
Chu ShenDepartment of Gastrointestinal Surgery, Huzhou Central Hospital, Affiliated Central Hospital of Huzhou University, Huzhou, China.
Jingrui CaoDepartment of Gastrointestinal Surgery, Huzhou Central Hospital, Affiliated Central Hospital of Huzhou University, Huzhou, China.
Zhongxin WuDepartment of Gastrointestinal Surgery, Huzhou Central Hospital, Affiliated Central Hospital of Huzhou University, Huzhou, China.
Lei YinDepartment of Gastrointestinal Surgery, Huzhou Central Hospital, Affiliated Central Hospital of Huzhou University, Huzhou, China.
Yuhai GaoDepartment of Gastrointestinal Surgery, Huzhou Central Hospital, Affiliated Central Hospital of Huzhou University, Huzhou, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe rise of antibiotic-resistant Helicobacter pylori (Hp) strains is complicating the management of common gastrointestinal conditions such as gastritis and ulcers. In search of effective treatment options, antimicrobial peptides are being explored as a promising strategy.

methodsLeveraging bioinformatics, we dissected structural and sequence profiles of piscidin, an antimicrobial peptide. We investigated whether long-term piscidin exposure induces resistance in Hp strains by measuring their minimum inhibitory concentration. The Oxford cup test was applied to measure inhibition zones of piscidin against Hp strains. Following piscidin treatment, we monitored morphological alterations in Hp strains using scanning electron microscopy, and changes in urease activity, expressions of virulence factors CagA and UreB, and adenosine triphosphate levels. Cytotoxicity of piscidin was evaluated in AGS and 293T cells.

resultsPiscidin inhibited proliferation of Hp strains, with a low propensity of inducing resistance. Delving into underlying mechanisms, we observed piscidin could alter morphology of Hp strains, suppress urease activity, and downregulate expressions of virulence factors CagA and UreB, while also reducing intracellular ATP levels. Piscidin had good security.

conclusionPiscidin is a potent antibacterial agent against Hp with low resistance risk, making it a safe and effective treatment candidate.

Indexed as

Anti-Bacterial AgentsAntimicrobial Cationic PeptidesFish ProteinsHelicobacter pyloriAdenosine TriphosphateAntigens, BacterialBacterial ProteinsCell LineDrug Resistance, BacterialHEK293 CellsHelicobacter InfectionsHumansMicrobial Sensitivity TestsUreaseVirulence FactorsAdenosine TriphosphateAnti-Bacterial AgentsAntigens, BacterialAntimicrobial Cationic PeptidesBacterial ProteinscagA protein, Helicobacter pyloriFish Proteinsmoronecidin protein, Morone saxatilisUreaseVirulence FactorsAntimicrobial activityantimicrobial peptideshelicobacter pylorimechanism investigationPiscidin

Identifiers

PMID40264290
PMCPMC12551399

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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.