Structure-based in silico evaluation of ribavirin targeting the RSV G protein central conserved domain (CCD)

Abstract

Respiratory syncytial virus (RSV) remains a leading cause of acute lower respiratory tract infections worldwide, with limited therapeutic options available beyond monoclonal antibody-based interventions. The central conserved domain (CCD) of the RSV attachment glycoprotein (G), containing the CX3C chemokine-like motif, represents an underexplored but an important target for small molecule drug discovery. Molecular docking revealed a binding affinity of −6.70 kcal/mol with six hydrogen bond interactions. One hundred nanosecond molecular dynamics simulations showed stable binding, favorable energetics and conserved binding-site integrity. This work advances knowledge by identifying ribavirin as a thermodynamically competent binder of the RSV G protein CCD and establishing a structure-guided framework for optimizing CCD-targeted antiviral agents.