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6CXC

3.9A Cryo-EM structure of murine antibody bound at a novel epitope of respiratory syncytial virus fusion protein

Summary for 6CXC
Entry DOI10.2210/pdb6cxc/pdb
EMDB information7774
DescriptorR4.C6 Fab Heavy Chain, R4.C6 Fab Light Chain, Fusion glycoprotein F0, Envelope glycoprotein chimera, ... (4 entities in total)
Functional Keywordsrespiratory syncytial virus fusion protein, murine antibody, novel epitope, complex, viral protein-immune system complex, viral protein/immune system
Biological sourceMus musculus (Mouse)
More
Total number of polymer chains12
Total formula weight444561.11
Authors
Xie, Q.,Wang, Z.,Chen, X.,Ni, F.,Ma, J.,Wang, Q. (deposition date: 2018-04-02, release date: 2019-07-31, Last modification date: 2024-11-06)
Primary citationXie, Q.,Wang, Z.,Ni, F.,Chen, X.,Ma, J.,Patel, N.,Lu, H.,Liu, Y.,Tian, J.H.,Flyer, D.,Massare, M.J.,Ellingsworth, L.,Glenn, G.,Smith, G.,Wang, Q.
Structure basis of neutralization by a novel site II/IV antibody against respiratory syncytial virus fusion protein.
Plos One, 14:e0210749-e0210749, 2019
Cited by
PubMed Abstract: Globally, human respiratory syncytial virus (RSV) is a leading cause of lower respiratory tract infections in newborns, young children, and the elderly for which there is no vaccine. The RSV fusion (F) glycoprotein is a major target for vaccine development. Here, we describe a novel monoclonal antibody (designated as R4.C6) that recognizes both pre-fusion and post-fusion RSV F, and binds with nanomole affinity to a unique neutralizing site comprised of antigenic sites II and IV on the globular head. A 3.9 Å-resolution structure of RSV F-R4.C6 Fab complex was obtained by single particle cryo-electron microscopy and 3D reconstruction. The structure unraveled detailed interactions of R4.C6 with antigenic site II on one protomer and site IV on a neighboring protomer of post-fusion RSV F protein. These findings significantly further our understanding of the antigenic complexity of the F protein and provide new insights into RSV vaccine design.
PubMed: 30730999
DOI: 10.1371/journal.pone.0210749
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.9 Å)
Structure validation

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