8E1G

SARS-CoV-2 RBD in complex with Omicron-neutralizing antibody 2A10

Summary for 8E1G

• Entry DOI: 10.2210/pdb8e1g/pdb
• Descriptor: 2A10 Fab, heavy chain, 2A10 Fab, light chain, Spike protein S1, ... (4 entities in total)
• Functional Keywords: sars-cov-2, omicron, antibody, neutralizing, viral protein
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 6
• Total formula weight: 158344.71

Authors

Wasserman, H.,Hastie, K.M.,Buck, T.K.,Saphire, E.O. (deposition date: 2022-08-10, release date: 2023-06-28, Last modification date: 2024-11-13)

Primary citation

Hastie, K.M.,Yu, X.,Ana-Sosa-Batiz, F.,Zyla, D.S.,Harkins, S.S.,Hariharan, C.,Wasserman, H.,Zandonatti, M.A.,Miller, R.,Maule, E.,Kim, K.,Valentine, K.M.,Shresta, S.,Saphire, E.O.
Potent Omicron-neutralizing antibodies isolated from a patient vaccinated 6 months before Omicron emergence.
Cell Rep, 42:112421-112421, 2023

PubMed Abstract: Therapeutic antibodies are an important tool in the arsenal against coronavirus infection. However, most antibodies developed early in the pandemic have lost most or all efficacy against newly emergent strains of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), particularly those of the Omicron lineage. Here, we report the identification of a panel of vaccinee-derived antibodies that have broad-spectrum neutralization activity. Structural and biochemical characterization of the three broadest-spectrum antibodies reveal complementary footprints and differing requirements for avidity to overcome variant-associated mutations in their binding footprints. In the K18 mouse model of infection, these three antibodies exhibit protective efficacy against BA.1 and BA.2 infection. This study highlights the resilience and vulnerabilities of SARS-CoV-2 antibodies and provides road maps for further development of broad-spectrum therapeutics.

PubMed: 37083327
DOI: 10.1016/j.celrep.2023.112421

Experimental method

X-RAY DIFFRACTION (2.57 Å)