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Poster

Session: Session 2 Presenting Authors at Posters (Odds)

P-141 - Nucleoporin 50a is a novel interactor of geminivirus-encoded C4 proteins and effectively facilitates the virus accumulation

Wednesday, July 16, 2025
13:30 - 15:15  
Location: Confex Hall 3
Effector Interference Mechanisms

    Presenting Author(s)

  • AC

    Aparna Chodon

    Department of Plant Biochemistry, Centre for Plant Molecular Biology (ZMBP), Eberhard Karls University, Tübingen, Germany and Department of Plant Biotechnology, School of Biotechnology, Madurai Kamaraj University, India
    Tubingen, Baden-Wurttemberg, Germany

    • Author(s)

  • RL

    Rosa Lozano-Durán

    University of Tü​bingen
    Tübingen, GERMANY

  • GP

    Gopal Pandi

    Department of Plant Biotechnology, School of Biotechnology, Madurai Kamaraj University, India
    Madurai, Tamil Nadu, India

Nucleoporin 50a (Nup50a) is an essential component of the nuclear pore complex that plays a critical role in regulating the nucleo-cytoplasmic transport of macromolecules. Beyond its involvement in nuclear trafficking through the interaction with nuclear transport receptors, Nup50a also interacts with euchromatin, promoting the transcription of development- and cell cycle-related genes. In this study, we report the interaction of NbNup50a with the C4 protein from bhendi yellow vein mosaic virus (BYVMV), identified through affinity purification-mass spectrometry analysis. BYVMV is a monopartite begomovirus that infects okra leading to up to 96% yield loss in infected plants. BYVMV C4 is a small, multifunctional protein that localizes in the nucleus and at the plasma membrane. It acts as a symptom determinant, suppresses transcriptional gene silencing and post-transcriptional gene silencing, and facilitates viral movement. Various protein-protein interaction techniques confirmed the direct interaction between NbNup50a and the nucleus-localized C4. Silencing NbNup50a significantly reduced symptoms and virus accumulation, underscoring its important role in successful infection. Furthermore, C4 proteins from three other geminiviruses also interact with Nup50a, indicating a potentially conserved strategy employed by the viruses. Further studies are required to elucidate the molecular mechanisms underlying C4-Nup50a-mediated stimulation of viral infection.