Evidence map›Paper›PMID 26948237›Full record

ArticleApplied microbiology and biotechnology2016

Antimicrobial peptide melittin against Xanthomonas oryzae pv. oryzae, the bacterial leaf blight pathogen in rice.

Wei Shi, Caiyun Li, Man Li, Xicui Zong, Dongju Han, Yuqing Chen

Open access · hybridAbstract read
In one paragraph

Article in Applied microbiology and biotechnology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
6.1field-weighted citation impact, top 4% 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

44 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
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  3. Advances of Peptides for Plant Immunity.Plants (Basel, Switzerland) · 2025
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  18. Article
  19. Pharmacological properties and therapeutic potential of honey bee venom.Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2023
    Review
  20. Antibacterial Peptide NP-6 AffectsInternational journal of molecular sciences · 2022
    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

6 authors at 1 institution in 1 country.

Wei ShiJiangsu Province Key Laboratory for Molecular and Medical Biotechnology, Life Sciences College, Nanjing Normal University, Nanjing, 210023, China.
Caiyun LiJiangsu Province Key Laboratory for Molecular and Medical Biotechnology, Life Sciences College, Nanjing Normal University, Nanjing, 210023, China.
Man LiJiangsu Province Key Laboratory for Molecular and Medical Biotechnology, Life Sciences College, Nanjing Normal University, Nanjing, 210023, China.
Xicui ZongJiangsu Province Key Laboratory for Molecular and Medical Biotechnology, Life Sciences College, Nanjing Normal University, Nanjing, 210023, China.
Dongju HanJiangsu Province Key Laboratory for Molecular and Medical Biotechnology, Life Sciences College, Nanjing Normal University, Nanjing, 210023, China.
Yuqing ChenJiangsu Province Key Laboratory for Molecular and Medical Biotechnology, Life Sciences College, Nanjing Normal University, Nanjing, 210023, China. yuqingchen515@yahoo.com.
Nanjing Normal University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Xanthomonas oryzae pv. oryzae is a destructive bacterial disease of rice, and the development of an environmentally safe bactericide is urgently needed. Antimicrobial peptides, as antibacterial sources, may play important roles in bactericide development. In the present study, we found that the antimicrobial peptide melittin had the desired antibacterial activity against X. oryzae pv. oryzae. The antibacterial mechanism was investigated by examining its effects on cell membranes, energy metabolism, and nucleic acid, and protein synthesis. The antibacterial effects arose from its ability to interact with the bacterial cell wall and disrupt the cytoplasmic membrane by making holes and channels, resulting in the leakage of the cytoplasmic content. Additionally, melittin is able to permeabilize bacterial membranes and reach the cytoplasm, indicating that there are multiple mechanisms of antimicrobial action. DNA/RNA binding assay suggests that melittin may inhibit macromolecular biosynthesis by binding intracellular targets, such as DNA or RNA, and that those two modes eventually lead to bacterial cell death. Melittin can inhibit X. oryzae pv. oryzae from spreading, alleviating the disease symptoms, which indicated that melittin may have potential applications in plant protection.

Indexed as

Cell WallDNA, BacterialElectrophoresis, Polyacrylamide GelMelittenMicroscopy, ConfocalMicroscopy, Electron, ScanningMicroscopy, Electron, TransmissionOryzaPlant DiseasesPlant LeavesRNA, BacterialXanthomonasDNA, BacterialMelittenRNA, BacterialMelittinRiceXanthomonas oryzae pv. oryzae

Identifiers

PMID26948237
PMCPMC4866983
OpenAlexW2295930298

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.