8DPL

Structure of EBOV GP lacking the mucin-like domain with 2.1.1D5 scFv and 6D6 scFv bound

Summary for 8DPL

• Entry DOI: 10.2210/pdb8dpl/pdb
• EMDB information: 27637
• Descriptor: 2.1.1D5 heavy chain variable domain, 2.1.1D5 light chain variable domain, 6D6 single-chain variable fragment, ... (7 entities in total)
• Functional Keywords: viral protein, glycoprotein, immune system, antibody, ebola virus, viral protein-immune system complex, viral protein/immune system
• Biological source: Homo sapiens; More
• Total number of polymer chains: 15
• Total formula weight: 295729.80

Authors

Yu, X.,Saphire, E.O. (deposition date: 2022-07-15, release date: 2023-07-19, Last modification date: 2025-05-14)

Primary citation

Yu, X.,Hastie, K.M.,Davis, C.W.,Avalos, R.D.,Williams, D.,Parekh, D.,Hui, S.,Mann, C.,Hariharan, C.,Takada, A.,Ahmed, R.,Saphire, E.O.
The evolution and determinants of neutralization of potent head-binding antibodies against Ebola virus.
Cell Rep, 42:113366-113366, 2023

PubMed Abstract: Monoclonal antibodies against the Ebola virus (EBOV) surface glycoprotein are effective treatments for EBOV disease. Antibodies targeting the EBOV glycoprotein (GP) head epitope have potent neutralization and Fc effector function activity and thus are of high interest as therapeutics and for vaccine design. Here we focus on the head-binding antibodies 1A2 and 1D5, which have been identified previously in a longitudinal study of survivors of EBOV infection. 1A2 and 1D5 have the same heavy- and light-chain germlines despite being isolated from different individuals and at different time points after recovery from infection. Cryoelectron microscopy analysis of each antibody in complex with the EBOV surface GP reveals key amino acid substitutions in 1A2 that contribute to greater affinity, improved neutralization potency, and enhanced breadth as well as two strategies for antibody evolution from a common site.

PubMed: 37938974
DOI: 10.1016/j.celrep.2023.113366

Experimental method

ELECTRON MICROSCOPY (2.53 Å)