ArticleProceedings of the National Academy of Sciences of the United States of America2020
The structural basis of African swine fever virus pA104R binding to DNA and its inhibition by stilbene derivatives.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 44 citations in OpenAlex.
- Mechanistic insights and therapeutic advances in antiviral strategies against African swine fever virus.Acta pharmaceutica Sinica. B · 2026Review
- Cinnamic-Hydroxamic-Acid Derivatives Exhibit Antibiotic, Anti-Biofilm, and Supercoiling Relaxation Properties by Targeting Bacterial Nucleoid-Associated Protein HU.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Chloroquine phosphate targets the MAPK-ERK pathway to inhibit ASFV SY-1 replication in vitro.Virology journal · 2026Article
- Article
- Thonningianin A disrupts pA104R-DNA binding and inhibits African swine fever virus replication.Emerging microbes & infections · 2025Article
- Giant endogenous viral elements in the genome of the model protistJournal of virology · 2025Article
- Development and Application of Mouse-Derived CD2v Monoclonal Antibodies Against African Swine Fever Virus from Single B Cells.Viruses · 2025Article
- Exploring antiviral strategies to combat African swine fever.FEMS microbiology reviews · 2025Review
- Structural basis for difunctional mechanism of m-AMSA against African swine fever virus pP1192R.Nucleic acids research · 2024Article
- Advancement in the Antigenic Epitopes and Vaccine Adjuvants of African Swine Fever Virus.Pathogens (Basel, Switzerland) · 2024Review
- Article
- Characterization of the monoclonal antibody and the immunodominant B-cell epitope of African swine fever virus pA104R by using mouse model.Microbiology spectrum · 2024Article
- Advancement in the development of gene/protein-based vaccines against African swine fever virus.Current research in microbial sciences · 2024Review
- Article
- The 2022 Outbreaks of African Swine Fever Virus Demonstrate the First Report of Genotype II in Ghana.Viruses · 2023Article
- African swine fever virus pA104R protein acts as a suppressor of type I interferon signaling.Frontiers in microbiology · 2023Article
- Structure and function of African swine fever virus proteins: Current understanding.Frontiers in microbiology · 2023Review
- Complete Structural Predictions of the Proteome of African Swine Fever Virus Strain Georgia 2007.Microbiology resource announcements · 2022Article
- Arginine 58 is indispensable for proper function of theVirulence · 2022Article
- African Swine Fever Virus: A Review.Life (Basel, Switzerland) · 2022Review
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Authors and funding
15 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
African swine fever virus (ASFV) is a highly contagious nucleocytoplasmic large DNA virus (NCLDV) that causes nearly 100% mortality in swine. The development of effective vaccines and drugs against this virus is urgently needed. pA104R, an ASFV-derived histone-like protein, shares sequence and functional similarity with bacterial HU/IHF family members and is essential for viral replication. Herein, we solved the crystal structures of pA104R in its apo state as well as in complex with DNA. Apo-pA104R forms a homodimer and folds into an architecture conserved in bacterial heat-unstable nucleoid proteins/integration host factors (HUs/IHFs). The pA104R-DNA complex structure, however, uncovers that pA104R has a DNA binding pattern distinct from its bacterial homologs, that is, the β-ribbon arms of pA104R stabilize DNA binding by contacting the major groove instead of the minor groove. Mutations of the basic residues at the base region of the β-strand DNA binding region (BDR), rather than those in the β-ribbon arms, completely abolished DNA binding, highlighting the major role of the BDR base in DNA binding. An overall DNA bending angle of 93.8° is observed in crystal packing of the pA104R-DNA complex structure, which is close to the DNA bending angle in the HU-DNA complex. Stilbene derivatives SD1 and SD4 were shown to disrupt the binding between pA104R and DNA and inhibit the replication of ASFV in primary porcine alveolar macrophages. Collectively, these results reveal the structural basis of pA104R binding to DNA highlighting the importance of the pA104R-DNA interaction in the ASFV replication cycle and provide inhibitor leads for ASFV chemotherapy.
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