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-Structure paper
Title | The evolution and determinants of neutralization of potent head-binding antibodies against Ebola virus. |
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Journal, issue, pages | Cell Rep, Vol. 42, Issue 11, Page 113366, Year 2023 |
Publish date | Nov 7, 2023 |
Authors | Xiaoying Yu / Kathryn M Hastie / Carl W Davis / Ruben Diaz Avalos / Dewight Williams / Diptiben Parekh / Sean Hui / Colin Mann / Chitra Hariharan / Ayato Takada / Rafi Ahmed / Erica Ollmann Saphire / |
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 ...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. |
External links | Cell Rep / PubMed:37938974 / PubMed Central |
Methods | EM (single particle) |
Resolution | 2.53 - 3.0 Å |
Structure data | EMDB-27637, PDB-8dpl: EMDB-27638, PDB-8dpm: |
Chemicals | ChemComp-NAG: |
Source |
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Keywords | VIRAL PROTEIN/Immune System / VIRAL PROTEIN / glycoprotein / immune system / antibody / Ebola virus / VIRAL PROTEIN-Immune System complex |