Dengue virus (DENV) is a mosquito-borne flavivirus responsible for approximately 390 million infections annually, representing one of the most significant global public health challenges among arboviruses. The dengue envelope (E) glycoprotein is the principal mediator of viral attachment, receptor recognition, and membrane fusion during host cell entry. This study characterizes the structural interaction landscape between sixteen dengue envelope genotype variants and a curated panel of host proteins involved in viral attachment, endocytic trafficking, immune signaling, and vascular regulation. Three-dimensional structural models were obtained through a hierarchical pipeline integrating experimentally determined structures, AlphaFold predictions, I-TASSER template-based modeling, and MODELLER refinement, followed by molecular dynamics relaxation. Protein--protein docking simulations were performed using HDOCK across all envelope--host protein combinations. Interaction interfaces were quantitatively characterized through a vector-based formalism encoding hydrogen bond directionality, occupancy, and angular entropy. To approximate cellular interaction environments, triple docking simulations incorporating first-neighbor host proteins were implemented under both pre-assembly and post-assembly scenarios, and binding cooperativity was evaluated through DeltaDelta G thermodynamic analysis. This framework provides a multiscale representation of viral--host interaction architecture and identifies structural determinants potentially associated with viral entry, host immune modulation, and vascular pathogenesis.
Neto, D. F. d. L., Teixeira, J. P., Corat, M. A. F., Bajay, M. M., Trossini, G. H. G., Mansur, D. S., Leal, E. d. S., Janini, L. M. R., Freire, C. C. d. M.
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