Title
Structure-based in silico evaluation of ribavirin targeting the RSV G protein central conserved domain (CCD)
Authors
Ufaq Razi1, Anwar Ahmed2 & Shama Parveen1,*
Affiliation
1Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, India; 2Centre of Excellence in Biotechnology Research, College of Applied Medical Sciences, King Saud University, Riyadh, Saudi Arabia; *Corresponding author
Ufaq Razi - E-mail: ufaq2400706@st.jmi.ac.in
Anwar Ahmed - E-mail: anahmed@ksu.edu.sa
Shama Parveen - E-mail: sparveen2@jmi.ac.in
Article Type
Research Article
Date
Received September 1, 2026; Revised
September 30, 2026; Accepted September 30, 2026, Published September
30, 2026
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.
Keywords
Respiratory syncytial virus (RSV), G protein, ribavirin, CX3C motif
Citation
Razi et al. Bioinformation 22(9): 6086-6091 (2026)
Edited by
P Kangueane
ISSN
0973-2063
Publisher
License
This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.
