6CXC
3.9A Cryo-EM structure of murine antibody bound at a novel epitope of respiratory syncytial virus fusion protein
Summary for 6CXC
Entry DOI | 10.2210/pdb6cxc/pdb |
EMDB information | 7774 |
Descriptor | R4.C6 Fab Heavy Chain, R4.C6 Fab Light Chain, Fusion glycoprotein F0, Envelope glycoprotein chimera, ... (4 entities in total) |
Functional Keywords | respiratory syncytial virus fusion protein, murine antibody, novel epitope, complex, viral protein-immune system complex, viral protein/immune system |
Biological source | Mus musculus (Mouse) More |
Total number of polymer chains | 12 |
Total formula weight | 444561.11 |
Authors | |
Primary citation | Xie, 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: 30730999DOI: 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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