7D3R
FOOT AND MOUTH DISEASE VIRUS A/WH/CHA/09-BOUND THE SINGLE CHAIN FRAGME ANTIBODY R50
Summary for 7D3R
Entry DOI | 10.2210/pdb7d3r/pdb |
EMDB information | 30565 3631 |
Descriptor | A/WH/CHA/09 VP1, A/WH/CHA/09 VP2, A/WH/CHA/09 VP3, ... (6 entities in total) |
Functional Keywords | foot and mouth disease virus, fmdv, virus |
Biological source | Bos taurus More |
Total number of polymer chains | 6 |
Total formula weight | 111666.06 |
Authors | |
Primary citation | He, Y.,Li, K.,Cao, Y.,Sun, Z.,Li, P.,Bao, H.,Wang, S.,Zhu, G.,Bai, X.,Sun, P.,Liu, X.,Yang, C.,Liu, Z.,Lu, Z.,Rao, Z.,Lou, Z. Structures of Foot-and-mouth Disease Virus with neutralizing antibodies derived from recovered natural host reveal a mechanism for cross-serotype neutralization. Plos Pathog., 17:e1009507-e1009507, 2021 Cited by PubMed Abstract: The development of a universal vaccine against foot-and-mouth disease virus (FMDV) is hindered by cross-serotype antigenic diversity and by a lack of knowledge regarding neutralization of the virus in natural hosts. In this study, we isolated serotype O-specific neutralizing antibodies (NAbs) (F145 and B77) from recovered natural bovine hosts by using the single B cell antibody isolation technique. We also identified a serotype O/A cross-reacting NAb (R50) and determined virus-NAb complex structures by cryo-electron microscopy at near-atomic resolution. F145 and B77 were shown to engage the capsid of FMDV-O near the icosahedral threefold axis, binding to the BC/HI-loop of VP2. In contrast, R50 engages the capsids of both FMDV-O and FMDV-A between the 2- and 5-fold axes and binds to the BC/EF/GH-loop of VP1 and to the GH-loop of VP3 from two adjacent protomers, revealing a previously unknown antigenic site. The cross-serotype neutralizing epitope recognized by R50 is highly conserved among serotype O/A. These findings help to elucidate FMDV neutralization by natural hosts and provide epitope information for the development of a universal vaccine for cross-serotype protection against FMDV. PubMed: 33909694DOI: 10.1371/journal.ppat.1009507 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.49 Å) |
Structure validation
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