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In Silico Characterization of African Swine Fever Virus Nucleoprotein p10 Interaction with DNA
Claudia Istrate1,2, Jéssica Marques3, Pedro Bule1,2
1CIISA-Centre for Interdisciplinary Research in Animal Health, Faculty of Veterinary Medicine, University of Lisbon, 1300-477 Lisboa, Portugal.
Viruses
|November 11, 2022
Summary
African swine fever virus (ASFV) p10 protein binds double-stranded DNA (dsDNA) via a helix-turn-helix motif. This research elucidates the molecular mechanism, aiding in understanding ASFV replication and potential therapeutic targets.
Area of Science:
- Virology
- Structural Biology
- Molecular Biology
Background:
- African swine fever virus (ASFV) causes a severe swine disease with significant economic impact.
- No vaccines or treatments are currently available globally.
- The ASFV p10 protein is a structural nucleoprotein known to bind double-stranded DNA (dsDNA).
Purpose of the Study:
- To elucidate the molecular mechanism of ASFV p10 protein's interaction with dsDNA.
- To generate a structural model for the p10 protein and identify key DNA-binding regions.
Main Methods:
- Ab initio modeling of the ASFV p10 protein.
- Molecular dynamics simulations for structural characterization and DNA recognition analysis.
- Experimental binding assays to validate findings.
Main Results:
- An ab initio model of the p10 protein was successfully generated.
- A helix-turn-helix motif in the C-terminal region was identified as crucial for dsDNA binding.
- Serine and lysine-rich regions within the protein's helices were confirmed as key for DNA interaction.
Conclusions:
- The study provides a structural basis for understanding ASFV p10 protein's dsDNA binding mechanism.
- Identified motifs and residues are critical for p10-dsDNA interaction, potentially influencing ASFV replication.
- These findings offer insights for developing future ASFV interventions.

