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<p>Polygalacturonase-inhibiting proteins are leucine-rich repeat, pathogenesis-related cell wall proteins that play a vital role in plant defense by inhibiting polygalacturonases, which are pectin-degrading enzymes secreted by pathogens. The PGIP–PG interaction limits pathogen invasion and triggers host immune responses. <i>Fusarium oxysporum</i>, a soil-borne fungal pathogen responsible for wilt disease in radish and various other crops, relies on PG activity for infection, making the PG–PGIP interaction a key element of the plant–pathogen interface. To elucidate the molecular mechanism of the PG–PGIP interaction, we employed molecular modeling, protein–protein docking, and molecular dynamics simulations to analyze the binding of radish PGIP with <i>Fusarium oxysporum</i> polygalacturonase. In addition, in silico site-directed mutagenesis was used to generate a mutant PGIP, and its interaction with foPG was similarly assessed. Docking and simulation results revealed that key residues in both rsPGIP and mrsPGIP form stable interactions with foPG, inducing conformational changes that likely inhibit its enzymatic activity. These findings offer valuable insights into PG–PGIP interactions and may support the development of <i>Fusarium</i> wilt resistant radish cultivars.</p>

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Computational investigation of structural and functional impacts of L163G and W235K mutations in LRR-PGIP of Raphanus sativus: insights into host–pathogen interaction dynamics

  • 期刊论文

  • 发表日期：

    2026年2月24日

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  • Soumya Sharma,
  • Mayank Rashmi,
  • Mahender Kumar Singh,
  • Sarika Sahu,
  • Raja Shankar,
  • Anurag Chaurasia,
  • Girish Kumar Jha,
  • Sunil Kumar

摘要

Polygalacturonase-inhibiting proteins are leucine-rich repeat, pathogenesis-related cell wall proteins that play a vital role in plant defense by inhibiting polygalacturonases, which are pectin-degrading enzymes secreted by pathogens. The PGIP–PG interaction limits pathogen invasion and triggers host immune responses. Fusarium oxysporum, a soil-borne fungal pathogen responsible for wilt disease in radish and various other crops, relies on PG activity for infection, making the PG–PGIP interaction a key element of the plant–pathogen interface. To elucidate the molecular mechanism of the PG–PGIP interaction, we employed molecular modeling, protein–protein docking, and molecular dynamics simulations to analyze the binding of radish PGIP with Fusarium oxysporum polygalacturonase. In addition, in silico site-directed mutagenesis was used to generate a mutant PGIP, and its interaction with foPG was similarly assessed. Docking and simulation results revealed that key residues in both rsPGIP and mrsPGIP form stable interactions with foPG, inducing conformational changes that likely inhibit its enzymatic activity. These findings offer valuable insights into PG–PGIP interactions and may support the development of Fusarium wilt resistant radish cultivars.