8YDL

Crystal structure of single-chain dimer for RSV F protein

Summary for 8YDL

• Entry DOI: 10.2210/pdb8ydl/pdb
• Descriptor: Fusion glycoprotein F2, F1 (2 entities in total)
• Functional Keywords: respiratory syncytial virus, fusion protein, pre-fusion state, single-chain dimer, viral protein
• Biological source: Respiratory syncytial virus
• Total number of polymer chains: 2
• Total formula weight: 108841.06

Authors

Qi, J.X.,Li, J.,Zhao, J.R.,Guo, W.J. (deposition date: 2024-02-20, release date: 2025-08-20, Last modification date: 2025-09-10)

Primary citation

Li, J.,Ma, X.,Xu, Z.,Guo, W.,Peng, R.,Zhang, Y.,Meng, Y.,Zhao, J.,Wang, Q.,Li, S.,Chen, J.,Guo, Y.,Lu, X.,Wang, Q.,Guo, Y.,Jia, M.A.,Li, Y.,Zhang, Y.,Li, S.,Du, P.,Wang, Q.,Gao, G.F.,Qi, J.
Rational design of respiratory syncytial virus dimeric F-subunit vaccines in protein and mRNA forms.
Ebiomedicine, 119:105902-105902, 2025

PubMed Abstract: Respiratory syncytial virus (RSV) poses a significant public health threat, particularly to children and the elderly. Two protein-based vaccines and one mRNA vaccine have been approved, all targeting the prefusion conformation of the fusion (F) trimer. However, it has been reported that the epitope activity of the F protein gradually declines during storage, resulting in a reduction of the vaccines' immunogenicity.

PubMed: 40886405
DOI: 10.1016/j.ebiom.2025.105902

Experimental method

X-RAY DIFFRACTION (2.6 Å)