Evidence map›Paper›PMID 40859125›Full record

ArticleBMC microbiology2025

Identification and expression of a novel antimicrobial peptide Gloverin and its antibacterial effect against Staphylococcus aureus.

Kaiqi Lian, Yuhang Wang, Yayun Jiao, Xiangfeng Meng, Zengjun Ma, Yuanchen Zhang, Lingling Zhou

Abstract read
In one paragraph

Article in BMC microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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.

Kaiqi Lian *School of Biotechnology and Food Science, Anyang Institute of Technology, Anyang, 455000, China.ORCID 0000-0003-0681-207X
Yuhang Wang *School of Biotechnology and Food Science, Anyang Institute of Technology, Anyang, 455000, China.
Yayun JiaoSchool of Biotechnology and Food Science, Anyang Institute of Technology, Anyang, 455000, China.
Xiangfeng MengSchool of Biotechnology and Food Science, Anyang Institute of Technology, Anyang, 455000, China.
Zengjun MaCollege of Animal Science and Technology, Hebei Normal University of Science and Technology, Qinhuangdao, 066004, China.
Yuanchen ZhangSchool of Biotechnology and Food Science, Anyang Institute of Technology, Anyang, 455000, China. zhangyuanchen0110@163.com.
Lingling ZhouSchool of Biotechnology and Food Science, Anyang Institute of Technology, Anyang, 455000, China. 13700719135@163.com.ORCID 0000-0002-9512-8781

Funding

Hebei Provincial Modern Agro-industry Technology System of China HBCT2024220208Henan Provincial Science and Technology Research Project 242102110073
6 · The paper itself

Abstract

backgroundAntimicrobial peptides (AMPs) have attracted extensive attention in various fields. Gloverin is a group of AMPs derived from Lepidoptera insects. In this study, a novel gloverin CpGlv was identified through sequence alignment. The open reading frame (ORF) of mature CpGlv, devoid of its signal peptide region, was recombinantly expressed in Escherichia coli. The antibacterial activity of the fusion protein CpGlv against Staphylococcus aureus (S. aureus) was then assessed by determining the minimum inhibitory concentration (MIC) and using scanning electron microscopy (SEM) to observe the ultrastructure of S. aureus cells. Furthermore, the effects of CpGlv on the cell wall and membrane permeability of S. aureus were evaluated by detecting the leakage of intracellular nucleic acids, proteins, alkaline phosphatase (ALP), and β-galactosidase, as well as through the propidium iodide (PI) staining experiment. Finally, the influence of CpGlv on the S. aureus biofilm formation was investigated using the crystal violet staining assay.

resultsThe results showed that the ORF of CpGlv contained a nucleotide sequence of 591 bp. The expressed fusion protein CpGlv had a molecular weight of approximately 24 kDa. The purified CpGlv exhibited significant antibacterial activity against S. aureus, with a MIC of 40 µg/mL. 2×MIC of CpGlv caused S. aureus cells to exhibit adhesion, swelling, deformation, and even rupture. Further, CpGlv resulted in the leakage of intracellular nucleic acids, proteins, ALP, and β-galactosidase in S. aureus. After PI staining, there was intracellular fluorescence intensity in S. aureus treated by CpGlv. Additionally, 1/4×MIC of CpGlv significantly reduced the biofilm formation of S. aureus.

conclusionA novel gloverin CpGlv was identified, expressed, and purified, and the recombinant CpGlv exhibited antimicrobial activity against S. aureus by increasing the cell membrane and wall permeability, and inhibiting the biofilm formation, laying a foundation for in-depth research on the antibacterial mechanism and application of CpGlv.

Indexed as

Anti-Bacterial AgentsAntimicrobial Cationic PeptidesAntimicrobial PeptidesInsect ProteinsStaphylococcus aureusAmino Acid SequenceAnimalsBiofilmsCell Membrane PermeabilityCell WallEscherichia coliMicrobial Sensitivity TestsOpen Reading FramesRecombinant Fusion ProteinsAnti-Bacterial AgentsAntimicrobial Cationic PeptidesAntimicrobial PeptidesInsect ProteinsRecombinant Fusion ProteinsAntibacterial effectAntimicrobial peptidesGloverinProkaryotic expressionStaphylococcus aureus

Identifiers

PMID40859125
PMCPMC12382276

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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.