Evidence map›Paper›PMID 37973936›Full record

ArticleCommunications biology2023

A cleavable chimeric peptide with targeting and killing domains enhances LPS neutralization and antibacterial properties against multi-drug resistant E. coli.

Zhenlong Wang, Da Teng, Ruoyu Mao, Ya Hao, Na Yang, Xiumin Wang, Jianhua Wang

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.7field-weighted citation impact, top 16% of its field
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

8 citing papers in PubMed, 9 citations in OpenAlex.

  1. Multicopy Expression of the Marine Antimicrobial Peptide SpgillcinProbiotics and antimicrobial proteins · 2026
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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

7 authors at 2 institutions in 1 country.

Zhenlong WangTeam of AMP & Alternatives to Antibiotics, Gene Engineering Laboratory, Institute of Feed Research, Chinese Academy of Agricultural Sciences, Beijing, 100081, People's Republic of China.
Da TengTeam of AMP & Alternatives to Antibiotics, Gene Engineering Laboratory, Institute of Feed Research, Chinese Academy of Agricultural Sciences, Beijing, 100081, People's Republic of China.
Ruoyu MaoTeam of AMP & Alternatives to Antibiotics, Gene Engineering Laboratory, Institute of Feed Research, Chinese Academy of Agricultural Sciences, Beijing, 100081, People's Republic of China.
Ya HaoTeam of AMP & Alternatives to Antibiotics, Gene Engineering Laboratory, Institute of Feed Research, Chinese Academy of Agricultural Sciences, Beijing, 100081, People's Republic of China.
Na YangTeam of AMP & Alternatives to Antibiotics, Gene Engineering Laboratory, Institute of Feed Research, Chinese Academy of Agricultural Sciences, Beijing, 100081, People's Republic of China.
Xiumin WangTeam of AMP & Alternatives to Antibiotics, Gene Engineering Laboratory, Institute of Feed Research, Chinese Academy of Agricultural Sciences, Beijing, 100081, People's Republic of China. wangxiumin@caas.cn.ORCID 0000-0002-8179-074X
Jianhua WangTeam of AMP & Alternatives to Antibiotics, Gene Engineering Laboratory, Institute of Feed Research, Chinese Academy of Agricultural Sciences, Beijing, 100081, People's Republic of China. wangjianhua@caas.cn.ORCID 0000-0002-4048-6055
Chinese Academy of Agricultural Sciences · CNFeed Research Institute · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pathogenic Escherichia coli is one of the most common causes of diarrhea diseases and its characteristic component of the outer membrane-lipopolysaccharide (LPS) is a major inducer of sepsis. Few drugs have been proven to kill bacteria and simultaneously neutralize LPS toxicity. Here, the chimeric peptides-R7, A7 and G7 were generated by connecting LBP14 (LPS-targeting domain) with L7 (killing domain) via different linkers to improve antibacterial and anti-inflammatory activities. Compared to parent LBP14-RKRR and L7, the antibacterial activity of R7 with a cleavable "RKRR" linker and the "LBP14-RKRR + L7" cocktail against Escherichia coli, Salmonella typhimurium and Staphylococcus aureus was increased by 2 ~ 4-fold. Both A7 and G7 with non-cleavable linkers almost lost antibacterial activity. The ability of R7 to neutralize LPS was markedly higher than that of LBP14-RKRR and L7. In vivo, R7 could be cleaved by furin in a time-dependent manner, and release L7 and LBP14-RKRR in serum. In vivo, R7 can enhance mouse survival more effectively than L7 and alleviate lung injuries by selective inhibition of the NF-κB signaling pathways and promoting higher IAP activity. It suggests that R7 may be promising dual-function candidates as antibacterial and anti-endotoxin agents.

Indexed as

Escherichia coliLipopolysaccharidesAnimalsAnti-Bacterial AgentsBacteriaMicePeptidesAnti-Bacterial AgentsLipopolysaccharidesPeptides

Identifiers

PMID37973936
PMCPMC10654507
OpenAlexW4388734725

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.