Evidence map›Paper›PMID 42565929›Full record

ArticleWorld journal of microbiology & biotechnology2026

Heterologous expression and functional optimization of Cecropin A in Escherichia coli Nissle 1917.

Yu Hua, Youxi Li, Zixuan Zou, Huimin Ma, Yang Zhang, Yanhui Liu

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In one paragraph

Article in World journal of microbiology & biotechnology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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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

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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

6 authors.

Yu HuaBeijing Key Laboratory of Bioprocess, National Energy R&D Center for Biorefinery, College of Life Science and Technology, Beijing University of Chemical Technology, No. 15 of North Three-Ring East Road, Chaoyang District, Beijing, 100029, P.R. China.
Youxi LiBeijing Key Laboratory of Bioprocess, National Energy R&D Center for Biorefinery, College of Life Science and Technology, Beijing University of Chemical Technology, No. 15 of North Three-Ring East Road, Chaoyang District, Beijing, 100029, P.R. China.
Zixuan ZouBeijing Key Laboratory of Bioprocess, National Energy R&D Center for Biorefinery, College of Life Science and Technology, Beijing University of Chemical Technology, No. 15 of North Three-Ring East Road, Chaoyang District, Beijing, 100029, P.R. China.
Huimin MaBeijing Key Laboratory of Bioprocess, National Energy R&D Center for Biorefinery, College of Life Science and Technology, Beijing University of Chemical Technology, No. 15 of North Three-Ring East Road, Chaoyang District, Beijing, 100029, P.R. China.
Yang ZhangInstitute of Biological and Medical Engineering, Guangdong Academy of Sciences, Guangdong Biomaterials Engineering Technology Research Cente, Guangzhou, 510316, China. yzhang_0410@163.com.
Yanhui LiuBeijing Key Laboratory of Bioprocess, National Energy R&D Center for Biorefinery, College of Life Science and Technology, Beijing University of Chemical Technology, No. 15 of North Three-Ring East Road, Chaoyang District, Beijing, 100029, P.R. China. liuyh@mail.buct.edu.cn.

Funding

Advanced Materials-National Science and Technology Major Project 2025ZD0615002he Fundamental Research Funds for the Central Universities JD2636National Natural Science Foundation of China-Guangdong Joint Fund 22508013
6 · The paper itself

Abstract

Cecropin A (CeA) is a cationic antimicrobial peptide with potential antibacterial applications, but its recombinant production remains limited by host toxicity, peptide instability, and low recovery. In this study, an Escherichia coli Nissle 1917-based expression platform was developed for the heterologous production and functional optimization of CeA. A GST-fusion strategy combined with thrombin cleavage and ultrafiltration enabled the recovery of recombinant CeA, and the purified peptide showed antibacterial activity against E. coli JM109, with an MIC of 128 µg/mL. To further improve activity, site-directed and saturation mutagenesis were performed at selected residues. Among the G12 saturation mutants, G12M and G12Y showed the strongest activity, reducing the MIC against E. coli JM109 to 8 µg/mL, corresponding to a 16-fold improvement compared with wild-type CeA. These results indicate that residue 12 is a key position affecting CeA activity and that modulation of local physicochemical properties, especially hydrophobicity, can markedly enhance antibacterial potency. Overall, this study establishes a recombinant production and optimization strategy for CeA and provides useful insights for the engineering of antimicrobial peptides with improved activity.

Indexed as

Anti-Bacterial AgentsAntimicrobial Cationic PeptidesEscherichia coliAmino Acid SequenceGene ExpressionHydrophobic and Hydrophilic InteractionsMicrobial Sensitivity TestsMutagenesis, Site-DirectedRecombinant ProteinsAnti-Bacterial AgentsAntimicrobial Cationic Peptidescecropin ARecombinant ProteinsAntimicrobial peptideCecropin AProbiotic chassisRecombinant expressionSite-directed mutagenesis

Identifiers

PMID42565929

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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.