Picornavirus VP3 protein induces autophagy through the TP53-BAD-BAX axis to promote viral replication
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Updated: Jun 26, 2025

siRNA Electroporation to Modulate Autophagy in Herpes Simplex Virus Type 1-Infected Monocyte-Derived Dendritic Cells
Published on: October 28, 2019
Ruoqing Mao1, Zixiang Zhu1, Fan Yang1
1State Key Laboratory for Animal Disease Control and Prevention, College of Veterinary Medicine, Lanzhou University, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, China.
Abstract:
Macroautophagy/autophagy and apoptosis are pivotal interconnected host cell responses to viral infection, including picornaviruses. Here, the VP3 proteins of picornaviruses were determined to trigger autophagy, with the autophagic flux being triggered by the TP53-BAD-BAX axis. Using foot-and-mouth disease virus (FMDV) as a model system, we unraveled a novel mechanism of how picornavirus hijacks autophagy to bolster viral replication and enhance pathogenesis. FMDV infection induced both autophagy and apoptosis in vivo and in vitro. FMDV VP3 protein facilitated the phosphorylation and translocation of TP53 from the nucleus into the mitochondria, resulting in BAD-mediated apoptosis and BECN1-mediated autophagy. The amino acid Gly129 in VP3 is essential for its interaction with TP53, and crucial for induction of autophagy and apoptosis. VP3-induced autophagy and apoptosis are both essential for FMDV replication, while, autophagy plays a more important role in VP3-mediated pathogenesis. Mutation of Gly129 to Ala129 in VP3 abrogated the autophagic regulatory function of VP3, which significantly decreased the viral replication and pathogenesis of FMDV. This suggested that VP3-induced autophagy benefits viral replication and pathogenesis. Importantly, this Gly is conserved and showed a common function in various picornaviruses. This study provides insight for developing broad-spectrum antivirals and genetic engineering attenuated vaccines against picornaviruses.Abbreviations: 3-MA, 3-methyladenine; ATG, autophagy related; BAD, BCL2 associated agonist of cell death; BAK1, BCL2 antagonist/killer 1; BAX, BCL2 associated X, apoptosis regulator; BBC3/PUMA, BCL2 binding component 3; BCL2, BCL2 apoptosis regulator; BID, BH3 interacting domain death agonist; BIP-V5, BAX inhibitor peptide V5; CFLAR/FLIP, CASP8 and FADD like apoptosis regulator; CPE, cytopathic effects; CQ, chloroquine; CV, coxsackievirus; DAPK, death associated protein kinase; DRAM, DNA damage regulated autophagy modulator; EV71, enterovirus 71; FMDV, foot-and-mouth disease virus; HAV, hepatitis A virus; KD, knockdown; MAP1LC3/LC3, microtubule associated protein 1 light chain 3; MOI, multiplicity of infection; MTOR, mechanistic target of rapamycin kinase; PML, promyelocytic leukemia; PV, poliovirus; SVA, Seneca Valley virus; TCID50, 50% tissue culture infectious doses; TOR, target of rapamycin. TP53/p53, tumor protein p53; WCL, whole-cell lysate.
Insights
Picornaviruses hijack host cell autophagy via the VP3 protein, utilizing the TP53-BAD-BAX pathway to enhance viral replication and pathogenesis. Targeting this interaction offers a strategy for broad-spectrum antiviral development.
Area of Science:
- Virology
- Cellular Biology
- Immunology
Background:
- Macroautophagy/autophagy and apoptosis are critical host responses to viral infections, including those caused by picornaviruses.
- Picornaviruses are known to manipulate host cell processes, but the specific mechanisms involving autophagy and apoptosis require further elucidation.
Purpose of the Study:
- To investigate the role of picornavirus VP3 proteins in triggering autophagy and apoptosis.
- To elucidate the mechanism by which picornaviruses, using foot-and-mouth disease virus (FMDV) as a model, hijack autophagy for replication and pathogenesis.
- To identify key viral components and host factors involved in this process for potential therapeutic targeting.
Main Methods:
- Utilized FMDV as a model system to study viral-induced autophagy and apoptosis.
- Investigated the interaction between FMDV VP3 protein and host factors, including TP53, BAD, and BAX.
- Employed genetic mutations (Gly129 to Ala129 in VP3) to assess the functional importance of specific viral amino acids.
- Assessed viral replication and pathogenesis in vitro and in vivo.
Main Results:
- FMDV VP3 protein induces both autophagy and apoptosis by facilitating TP53 translocation to mitochondria, activating the BAD-mediated apoptosis and BECN1-mediated autophagy pathways.
- Amino acid Gly129 in VP3 is essential for TP53 interaction, autophagy, and apoptosis induction, crucial for FMDV replication and pathogenesis.
- Mutation of Gly129 abrogated VP3's autophagic function, significantly reducing viral replication and pathogenesis, indicating VP3-induced autophagy benefits the virus.
Conclusions:
- Picornavirus VP3 protein hijacks host autophagy through the TP53-BAD-BAX axis, essential for viral replication and pathogenesis.
- The conserved Gly129 residue in VP3 plays a critical role in mediating these viral-host interactions.
- This mechanism provides a potential target for developing broad-spectrum antivirals and attenuated vaccines against picornaviruses.
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