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In silico characterization, physiochemical analysis, and antifungal evaluation of the Zea mays PR-1 protein
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In silico characterization, physiochemical analysis, and antifungal evaluation of the Zea mays PR-1 protein
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Journal Article
In silico characterization, physiochemical analysis, and antifungal evaluation of the Zea mays PR-1 protein
2025
Overview
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.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 631/449
/ Antifungal Agents - chemistry
/ Antifungal Agents - pharmacology
/ Cloning
/ Corn
/ E coli
/ Enzymes
/ Fungi
/ Humanities and Social Sciences
/ Pathogenesis-related protein
/ Plant Diseases - microbiology
/ Plant Proteins - pharmacology
/ Proteins
/ Recombinant Proteins - chemistry
/ Recombinant Proteins - genetics
/ Recombinant Proteins - pharmacology
/ Science
/ Structure-function relationships
/ Wheat
/ Zea mays
