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<p>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 <i>Zea mays</i> and five other plant species (<i>Triticum aestivum</i>, <i>Hordeum vulgare</i>, <i>Oryza sativa</i>, <i>Avena sativa</i>, and <i>Secale cereale</i>) to explore their physicochemical, structural, and functional characteristics. The PR-1 gene from <i>Z. mays</i> was isolated and expressed in <i>Escherichia coli</i> BL21-DE3 cells, enabling structural characterization. Recombinant expression in <i>E. coli</i> 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 <i>Fusarium oxysporum</i>, 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.</p>

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

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年8月27日

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  • Muhammad Zafar Saleem,
  • Zaher Uddin Babar,
  • Sumaia Saif,
  • Ammara Saleem,
  • Nauman Ahmad,
  • Asma Zulfiqar,
  • Anis Ali Shah,
  • Muhammad Iftikhar,
  • Shifa Shaffique,
  • Mohammad K. Okla,
  • Ibrahim A. Alaraidh

摘要

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.