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Title | Structural basis for potent antibody neutralization of SARS-CoV-2 variants including B.1.1.529. |
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Journal, issue, pages | Science, Vol. 376, Issue 6591, Page eabn8897, Year 2022 |
Publish date | Apr 22, 2022 |
Authors | Tongqing Zhou / Lingshu Wang / John Misasi / Amarendra Pegu / Yi Zhang / Darcy R Harris / Adam S Olia / Chloe Adrienna Talana / Eun Sung Yang / Man Chen / Misook Choe / Wei Shi / I-Ting Teng / Adrian Creanga / Claudia Jenkins / Kwanyee Leung / Tracy Liu / Erik-Stephane D Stancofski / Tyler Stephens / Baoshan Zhang / Yaroslav Tsybovsky / Barney S Graham / John R Mascola / Nancy J Sullivan / Peter D Kwong / |
PubMed Abstract | The rapid spread of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) B.1.1.529 (Omicron) variant and its resistance to neutralization by vaccinee and convalescent sera are driving a ...The rapid spread of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) B.1.1.529 (Omicron) variant and its resistance to neutralization by vaccinee and convalescent sera are driving a search for monoclonal antibodies with potent neutralization. To provide insight into effective neutralization, we determined cryo-electron microscopy structures and evaluated receptor binding domain (RBD) antibodies for their ability to bind and neutralize B.1.1.529. Mutations altered 16% of the B.1.1.529 RBD surface, clustered on an RBD ridge overlapping the angiotensin-converting enzyme 2 (ACE2)-binding surface and reduced binding of most antibodies. Substantial inhibitory activity was retained by select monoclonal antibodies-including A23-58.1, B1-182.1, COV2-2196, S2E12, A19-46.1, S309, and LY-CoV1404-that accommodated these changes and neutralized B.1.1.529. We identified combinations of antibodies with synergistic neutralization. The analysis revealed structural mechanisms for maintenance of potent neutralization against emerging variants. |
External links | Science / PubMed:35324257 / PubMed Central |
Methods | EM (single particle) |
Resolution | 2.83 - 5.08 Å |
Structure data | EMDB-25794, PDB-7tb8: EMDB-25797, PDB-7tbf: EMDB-25806, PDB-7tc9: EMDB-25807, PDB-7tca: EMDB-25808, PDB-7tcc: EMDB-26256, PDB-7u0d: |
Chemicals | ChemComp-NAG: |
Source |
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Keywords | VIRAL PROTEIN/Immune System / SARS-CoV-2 / spike / antibody / VIRAL PROTEIN / VIRAL PROTEIN-Immune System complex / Omicron / Vral Protein/IMMUNE SYSTEM / B.1.1.529 / Receptor binding domain / IMMUNE SYSTEM / Vral Protein-IMMUNE SYSTEM complex |