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7C81

E30 F-particle in complex with 6C5

Summary for 7C81
Entry DOI10.2210/pdb7c81/pdb
EMDB information30304
DescriptorVP1, VP2, VP3, ... (7 entities in total)
Functional Keywordsmab, 6c5, e30, virus-immune system complex, virus/immune system
Biological sourceEchovirus E30
More
Total number of polymer chains6
Total formula weight142896.97
Authors
Wang, K.,Zheng, B.,Zhang, L.,Cui, L.,Su, X.,Zhang, Q.,Guo, Y.,Zhu, L.,Zhu, F.,Rao, Z.,Wang, X. (deposition date: 2020-05-28, release date: 2020-07-29, Last modification date: 2020-09-16)
Primary citationWang, K.,Zheng, B.,Zhang, L.,Cui, L.,Su, X.,Zhang, Q.,Guo, Z.,Guo, Y.,Zhang, W.,Zhu, L.,Zhu, F.,Rao, Z.,Wang, X.
Serotype specific epitopes identified by neutralizing antibodies underpin immunogenic differences in Enterovirus B.
Nat Commun, 11:4419-4419, 2020
Cited by
PubMed Abstract: Echovirus 30 (E30), a serotype of Enterovirus B (EV-B), recently emerged as a major causative agent of aseptic meningitis worldwide. E30 is particularly devastating in the neonatal population and currently no vaccine or antiviral therapy is available. Here we characterize two highly potent E30-specific monoclonal antibodies, 6C5 and 4B10, which efficiently block binding of the virus to its attachment receptor CD55 and uncoating receptor FcRn. Combinations of 6C5 and 4B10 augment the sum of their individual anti-viral activities. High-resolution structures of E30-6C5-Fab and E30-4B10-Fab define the location and nature of epitopes targeted by the antibodies. 6C5 and 4B10 engage the capsid loci at the north rim of the canyon and in-canyon, respectively. Notably, these regions exhibit antigenic variability across EV-Bs, highlighting challenges in development of broad-spectrum antibodies. Our structures of these neutralizing antibodies of E30 are instructive for development of vaccines and therapeutics against EV-B infections.
PubMed: 32887892
DOI: 10.1038/s41467-020-18250-w
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.1 Å)
Structure validation

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