6AD1
The structure of CVA10 procapsid from its complex with Fab 2G8
Summary for 6AD1
Entry DOI | 10.2210/pdb6ad1/pdb |
EMDB information | 9605 |
Descriptor | VP1, VP0, VP3 (3 entities in total) |
Functional Keywords | cva10, immune complex, neutralizing antibody, virus |
Biological source | Coxsackievirus A10 More |
Total number of polymer chains | 3 |
Total formula weight | 94542.98 |
Authors | Zhu, R.,Zheng, Q.B.,Xu, L.F.,Cui, Y.X.,Li, S.W.,Yan, X.D.,Zhou, Z.H.,Cheng, T. (deposition date: 2018-07-28, release date: 2018-11-21, Last modification date: 2024-05-29) |
Primary citation | Zhu, R.,Xu, L.,Zheng, Q.,Cui, Y.,Li, S.,He, M.,Yin, Z.,Liu, D.,Li, S.,Li, Z.,Chen, Z.,Yu, H.,Que, Y.,Liu, C.,Kong, Z.,Zhang, J.,Baker, T.S.,Yan, X.,Hong Zhou, Z.,Cheng, T.,Xia, N. Discovery and structural characterization of a therapeutic antibody against coxsackievirus A10. Sci Adv, 4:eaat7459-eaat7459, 2018 Cited by PubMed Abstract: Coxsackievirus A10 (CVA10) recently emerged as a major pathogen of hand, foot, and mouth disease and herpangina in children worldwide, and lack of a vaccine or a cure against CVA10 infections has made therapeutic antibody identification a public health priority. By targeting a local isolate, CVA10-FJ-01, we obtained a potent antibody, 2G8, against all three capsid forms of CVA10. We show that 2G8 exhibited both 100% preventive and 100% therapeutic efficacy against CVA10 infection in mice. Comparisons of the near-atomic cryo-electron microscopy structures of the three forms of CVA10 capsid and their complexes with 2G8 Fab reveal that a single Fab binds a border region across the three capsid proteins (VP1 to VP3) and explain 2G8's remarkable cross-reactivities against all three capsid forms. The atomic structures of this first neutralizing antibody of CVA10 should inform strategies for designing vaccines and therapeutics against CVA10 infections. PubMed: 30255146DOI: 10.1126/sciadv.aat7459 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (4.2 Å) |
Structure validation
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