Evidence map›Paper›PMID 40866506›Full record

ArticleScientific reports2025

In silico characterization, physiochemical analysis, and antifungal evaluation of the Zea mays PR-1 protein.

Muhammad Zafar Saleem, Zaher Uddin Babar, Sumaia Saif, Ammara Saleem, Nauman Ahmad, Asma Zulfiqar, Anis Ali Shah, Muhammad Iftikhar, Shifa Shaffique, Mohammad K Okla and 1 more

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PubMed Full text at PMC Publisher
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Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Genome-Wide Analysis of thePlants (Basel, Switzerland) · 2026
    Article
  2. Evolutionary Characteristics and Expression Patterns of theCurrent issues in molecular biology · 2026
    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

11 authors.

Muhammad Zafar SaleemCentre for Applied Molecular Biology, University of the Punjab, Lahore, 54590, Pakistan.
Zaher Uddin BabarUniversity of Education Lahore, Jauharabad Campus, Jauharabad, Pakistan.
Sumaia SaifCentre for Applied Molecular Biology, University of the Punjab, Lahore, 54590, Pakistan.
Ammara SaleemInstitute of Botany, University of the Punjab, Lahore, Pakistan.
Nauman AhmadCentre for Applied Molecular Biology, University of the Punjab, Lahore, 54590, Pakistan.
Asma ZulfiqarInstitute of Botany, University of the Punjab, Lahore, Pakistan.
Anis Ali ShahDepartment of Botany, Division of Science and Technology, University of Education , Lahore, 54770, Pakistan. anisalibot@gmail.com.
Muhammad IftikharDepartment of Botany, Division of Science and Technology, University of Education , Lahore, 54770, Pakistan. Iftikharf12m38@gmail.com.
Shifa ShaffiqueCollege of Agriculture & Life Science, School of Applied Biosciences, Kyungpook National University, 80 Daehak-ro, Buk-Gu, Daegu, 41566, Korea.
Mohammad K OklaBotany and Microbiology Department, College of Science, King Saud University, P.O. Box 2455, 11451, Riyadh, Saudi Arabia.
Ibrahim A AlaraidhBotany and Microbiology Department, College of Science, King Saud University, P.O. Box 2455, 11451, Riyadh, Saudi Arabia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pathogenesis-related protein 1 (PR-1) is a critical component of plant defense mechanisms, exhibiting significant antifungal activity. This study focused on the PR-1 protein from Zea mays and five other plant species (Triticum aestivum, Hordeum vulgare, Oryza sativa, Avena sativa, and Secale cereale) to explore their physicochemical, structural, and functional characteristics. The PR-1 gene from Z. mays was isolated and expressed in Escherichia coli BL21-DE3 cells, enabling structural characterization. Recombinant expression in E. coli enabled structural characterization and functional studies of the PR-1 protein, laying a foundation for future experiments. Sequence analysis revealed high similarity (65-90%) among PR-1 proteins across species, although physicochemical properties varied based on plant origin. Structural analysis showed a conserved beta-barrel structure surrounded by alpha-helices in all PR-1 proteins. In addition to in silico and structural characterization, antifungal bioassays were performed using the purified recombinant PR-1 protein against Fusarium oxysporum, a major fungal phytopathogen. These assays demonstrated notable antifungal activity, supporting the predicted defense role of PR-1 and laying experimental groundwork for its potential use in developing fungi-resistant transgenic crops.

Indexed as

Antifungal AgentsPlant ProteinsZea maysAmino Acid SequenceComputer SimulationFusariumPlant DiseasesRecombinant ProteinsAntifungal AgentsPlant ProteinsRecombinant ProteinsPathogenesis-related proteinPathogen resistanceStructural analysisZea mays

Identifiers

PMID40866506
PMCPMC12391533

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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.