6AJ9
The structure of Enterovirus D68 mature virion in complex with Fab 15C5 and 11G1
Summary for 6AJ9
| Entry DOI | 10.2210/pdb6aj9/pdb |
| EMDB information | 9634 |
| Descriptor | VL of Fab 11G1, VH of Fab 11G1, VL of Fab 15C5, ... (7 entities in total) |
| Functional Keywords | enterovirus d68, neutralizing antibody, immune-complex, virus |
| Biological source | Mus musculus More |
| Total number of polymer chains | 7 |
| Total formula weight | 138209.44 |
| Authors | |
| Primary citation | Zheng, Q.,Zhu, R.,Xu, L.,He, M.,Yan, X.,Liu, D.,Yin, Z.,Wu, Y.,Li, Y.,Yang, L.,Hou, W.,Li, S.,Li, Z.,Chen, Z.,Li, Z.,Yu, H.,Gu, Y.,Zhang, J.,Baker, T.S.,Zhou, Z.H.,Graham, B.S.,Cheng, T.,Li, S.,Xia, N. Atomic structures of enterovirus D68 in complex with two monoclonal antibodies define distinct mechanisms of viral neutralization Nat Microbiol, 4:124-133, 2019 Cited by PubMed Abstract: Enterovirus D68 (EV-D68) undergoes structural transformation between mature, cell-entry intermediate (A-particle) and empty forms throughout its life cycle. Structural information for the various forms and antibody-bound capsids will facilitate the development of effective vaccines and therapeutics against EV-D68 infection, which causes childhood respiratory and paralytic diseases worldwide. Here, we report the structures of three EV-D68 capsid states representing the virus at major phases. We further describe two original monoclonal antibodies (15C5 and 11G1) with distinct structurally defined mechanisms for virus neutralization. 15C5 and 11G1 engage the capsid loci at icosahedral three-fold and five-fold axes, respectively. To block viral attachment, 15C5 binds three forms of capsids, and triggers mature virions to transform into A-particles, mimicking engagement by the functional receptor ICAM-5, whereas 11G1 exclusively recognizes the A-particle. Our data provide a structural and molecular explanation for the transition of picornavirus capsid conformations and demonstrate distinct mechanisms for antibody-mediated neutralization. PubMed: 30397341DOI: 10.1038/s41564-018-0275-7 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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