Abstract
Dengue virus (DENV) is a mosquito-borne pathogen that causes dengue fever, a potentially severe illness. During infection, DENV interacts with various host factors to facilitate viral production. However, certain host restriction factors, such as the voltage-gated potassium channel Kv1.3, can impede viral replication by limiting DENV entry into host cells. While the interplay of DENV proteins and the specific mechanism facilitating this event remain unclear, our previous yeast two-hybrid interactomes study identified an interaction between DENV non-structural protein 2A (NS2A) and Kv1.3. This study aimed to identify potential binding sites between DENV NS2A and Kv1.3 using in silico approach. Crystal structures of DENV NS2A and Kv1.3 was obtained from RCSB PDB. Protein-protein interaction analysis was conducted using molecular docking with HADDOCK v2.4, and the interaction was assessed based on HADDOCK scores. Our results revealed that the HADDOCK score was -64.7±3.2, indicating an excellent binding affinity between DENV NS2A and Kv1.3. The robust interaction between NS2A and Kv1.3 underscores the need for further investigation into the role of potassium channels in DENV replication.
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