9B6Y

Envelope protein ASU of YFV-ES504 T380R

Summary for 9B6Y

• Entry DOI: 10.2210/pdb9b6y/pdb
• EMDB information: 44292
• Descriptor: Envelope protein (1 entity in total)
• Functional Keywords: flavivirus, envelope protein, yellow fever virus, virus
• Biological source: Yellow fever virus
• Total number of polymer chains: 3
• Total formula weight: 127974.88

Authors

Bibby, S.,Jung, J.,Modhiran, N.,Watterson, D. (deposition date: 2024-03-26, release date: 2025-09-03, Last modification date: 2025-10-15)

Primary citation

Bibby, S.,Jung, J.,Low, Y.S.,Amarilla, A.A.,Newton, N.D.,Scott, C.A.P.,Balk, J.,Ting, Y.T.,Freney, M.E.,Liang, B.,Grant, T.,Coulibaly, F.,Young, P.,Hall, R.A.,Hobson-Peters, J.,Modhiran, N.,Watterson, D.
A single residue in the yellow fever virus envelope protein modulates virion architecture and antigenicity.
Nat Commun, 16:8449-8449, 2025

PubMed Abstract: Yellow fever virus (YFV) is a re-emerging flavivirus that causes severe hepatic disease and mortality in humans. Despite being researched for over a century, the structure of YFV has remained elusive. Here we use a chimeric virus platform to resolve the first high resolution cryo-EM structures of YFV. Stark differences in particle morphology and homogeneity are observed between vaccine and virulent strains of YFV, and these are found to have significant implications on antibody recognition and neutralisation. We identify a single residue (R380) in the YFV envelope protein that stabilises the virion surface, and leads to reduced exposure of the cross-reactive fusion loop epitope. The differences in virion morphology between YFV strains also contribute to the reduced sensitivity of the virulent YFV virions to vaccine-induced antibodies. These findings have significant implications for YFV biology, vaccinology and structure-based flavivirus antigen design.

PubMed: 41006244
DOI: 10.1038/s41467-025-63038-5

Experimental method

ELECTRON MICROSCOPY (3.3 Å)