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Tomato Chlorotic Virus Minor Coat Protein Interferes With the Host Proteasome Function by Competitive Disruption of SlPAD1–SlPA4 Interaction to Enhance Viral Infection
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Tomato Chlorotic Virus Minor Coat Protein Interferes With the Host Proteasome Function by Competitive Disruption of SlPAD1–SlPA4 Interaction to Enhance Viral Infection
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Tomato Chlorotic Virus Minor Coat Protein Interferes With the Host Proteasome Function by Competitive Disruption of SlPAD1–SlPA4 Interaction to Enhance Viral Infection
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Journal Article
Tomato Chlorotic Virus Minor Coat Protein Interferes With the Host Proteasome Function by Competitive Disruption of SlPAD1–SlPA4 Interaction to Enhance Viral Infection
2025
Overview
The tomato chlorosis virus (ToCV) is one of the most destructive plant viruses affecting tomato crops, leading to significant agricultural losses. As an obligate parasite, ToCV depends on the macromolecular machinery of host cells for replication. The ubiquitin 26S proteasome system maintains the intracellular protein homeostasis, which is essential for plant growth and development. Our study found that the CPm protein of ToCV interacted with SlPAD1, a component of the 26S proteasome, to enhance viral infection. This interaction disrupts the binding between SlPAD1 and SlPA4, thereby impairing the 26S proteasome function. In addition, SlPAD1 and SlPA4 positively regulate plant resistance to ToCV. Our findings reveal a mechanism by which ToCV proteins facilitate infection by interfering with 26S proteasome function. CPm interacts with tomato SlPAD1 to block 26S proteasome function. Under physiological conditions, tomato SlPAD1 binds SlPA4 to form the 26S proteasome, maintaining protein homeostasis. During ToCV infection, viral CPm competitively interacts with SlPAD1, impairing proteasome function and inhibiting degradation of ubiquitinated proteins, thereby promoting viral pathogenesis.
