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Isolation of Viral Replication Compartment-enriched Sub-nuclear Fractions from Adenovirus-infected Normal Human Cells
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ASFV pE146L-induced ER remodeling is essential for viral replication
Yilin Guo1,2, Sai Niu1,2, Xueying Wang1,2
1State Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan, China.
Journal of Virology
|August 6, 2025
Summary
African swine fever virus (ASFV) inner envelope protein pE146L is essential for viral replication. Disrupting its structure or lipid-binding function impedes ASFV assembly and offers a new target for antiviral drug development.
Area of Science:
- Virology
- Structural Biology
- Molecular Biology
Background:
- African swine fever virus (ASFV) causes a severe hemorrhagic disease in pigs, impacting the global swine industry.
- The functions of many of the ASFV's nearly 200 encoded proteins remain uncharacterized, limiting our understanding of viral replication.
- Limited knowledge of ASFV replication and assembly mechanisms hinders the development of effective vaccines and antiviral drugs.
Purpose of the Study:
- To identify and characterize the function of the uncharacterized ASFV inner envelope protein pE146L.
- To elucidate the structural and functional properties of pE146L, including its role in viral replication and interaction with host cell components.
- To explore pE146L as a potential target for developing novel antiviral therapies against ASFV.
Main Methods:
- Identification and functional analysis of ASFV pE146L protein.
- Localization studies within infected cells, including endoplasmic reticulum (ER) colocalization and induction of ER aggregation.
- High-resolution crystal structure determination of the pE146L extracellular soluble region (pE146L-ΔTM).
- Biochemical analyses, including disruption of disulfide bonds (C103A mutant) and lipid-binding assays.
Main Results:
- The inner envelope protein pE146L is essential for ASFV replication.
- pE146L localizes to the endoplasmic reticulum lumen and induces perinuclear ER aggregation, which is crucial for viral factory formation.
- The crystal structure of pE146L-ΔTM revealed its dimeric nature, and disruption of intermolecular disulfide bonds abrogated ER aggregation and viral replication.
- pE146L possesses lipid-binding capabilities via a positively charged surface patch, indicating a role in lipid regulation critical for ASFV replication.
Conclusions:
- ASFV pE146L is a multifunctional protein critical for viral morphogenesis and replication.
- The structural integrity of pE146L dimers and its lipid-binding activity are essential for its function.
- pE146L represents a promising novel target for the development of anti-ASFV drugs.
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