Evidence map›Paper›PMID 37635252›Full record

ArticleMicrobial cell factories2023

Antibacterial peptide PMAP-37(F34-R), expressed in Pichia pastoris, is effective against pathogenic bacteria and preserves plums.

Chunming Dong, Lijun Xu, Weitao Lu, Mengru Li, Rui Zhang, Yanyan Sun, Jian Liu, Xinlei Chu

Open access · goldAbstract read
In one paragraph

Article in Microbial cell factories, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

3 citing papers in PubMed, 10 citations in OpenAlex.

  1. Review
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  3. The Fusion GenePlants (Basel, Switzerland) · 2025
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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

8 authors at 3 institutions in 1 country.

Chunming DongCollege of Marine and Environmental Sciences, Tianjin University of Science and Technology, Tianjin, 300457, China. mingchundongjy@tust.edu.cn.
Lijun XuCollege of Marine and Environmental Sciences, Tianjin University of Science and Technology, Tianjin, 300457, China.
Weitao LuCollege of Marine and Environmental Sciences, Tianjin University of Science and Technology, Tianjin, 300457, China.
Mengru LiCollege of Marine and Environmental Sciences, Tianjin University of Science and Technology, Tianjin, 300457, China.
Rui ZhangCollege of Marine and Environmental Sciences, Tianjin University of Science and Technology, Tianjin, 300457, China.
Yanyan SunJinan Deheng Medical Technology Co., Ltd, Jinan, 250031, Shandong Province, China.
Jian LiuCollege of Agriculture and Bioengineering, Heze University, Heze, 274000, China. liujianscholar@163.com.
Xinlei ChuDepartment of Epidemiology and Biostatistics, Tianjin Medical University Cancer Institute and Hospital, Tianjin, 300060, China. chuxinlei2014@163.com.
Tianjin University of Science and Technology · CNHeze University · CNTianjin Medical University Cancer Institute and Hospital · CN

Funding

National Natural Science Foundation of China 31900861
6 · The paper itself

Abstract

backgroundRecently, researchers have focused on the search for alternatives to conventional antibiotics. Antimicrobial peptides are small bioactive peptides that regulate immune activation and have antibacterial activity with a reduced risk of bacterial resistance. Porcine myeloid antibacterial peptide 37 (PMAP-37) is a small-molecule peptide with broad-spectrum antibacterial activity isolated from pig bone marrow, and PMAP-37(F34-R) is its analogue. In this study, PMAP-37(F34-R) was recombinantly expressed in Pichia pastoris, and the recombinant peptide was further investigated for its antibacterial properties, mechanism and preservative in plums.

resultsTo obtain a Pichia pastoris strain expressing PMAP-37(F34-R), we constructed a plasmid expressing recombinant PMAP-37(F34-R) (pPICZα-PMAP-37(F34-R)-A) and introduced it into Pichia pastoris. Finally, we obtained a highly active recombinant peptide, PMAP-37(F34-R), which inhibited the activity of both Gram-positive and Gram-negative bacteria. The minimum inhibitory concentration is 0.12-0.24 µg/mL, and it can destroy the integrity of the cell membrane, leading to cell lysis. It has good stability and is not easily affected by the external environment. Hemolysis experiments showed that 0.06 µg/mL-0.36 µg/mL PMAP-37(F34-R) had lower hemolysis ability to mammalian cells, and the hemolysis rate was below 1.5%. Additionally, 0.36 µg/mL PMAP-37(F34-R) showed a good preservative effect in plums. The decay and weight loss rates of the treated samples were significantly lower than those of the control group, and the respiratory intensity of the fruit was delayed in the experimental group.

conclusionsIn this study, we constructed a recombinant Pichia pastoris strain, which is a promising candidate for extending the shelf life of fruits and has potential applications in the development of new preservatives.

Indexed as

Prunus domesticaAnimalsAnti-Bacterial AgentsAntimicrobial Cationic PeptidesBacteriaGram-Negative BacteriaGram-Positive BacteriaHemolysisMammalsSaccharomycetalesSwineAnti-Bacterial AgentsAntimicrobial Cationic PeptidesPMAP-37Antibacterial mechanismAntimicrobial peptidesPreservation

Identifiers

PMID37635252
PMCPMC10464103
OpenAlexW4386203535

What OpenQuestion holds

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LicenceCC BY
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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.