| Literature DB >> 35324257 |
Tongqing Zhou1, Lingshu Wang1, John Misasi1, John R Mascola1, Nancy J Sullivan1, Peter D Kwong1, Amarendra Pegu1, Yi Zhang1, Darcy R Harris1, Adam S Olia1, Chloe Adrienna Talana1, Eun Sung Yang1, Man Chen1, Misook Choe1, Wei Shi1, I-Ting Teng1, Adrian Creanga1, Claudia Jenkins2, Kwanyee Leung1, Tracy Liu1, Erik-Stephane D Stancofski1, Tyler Stephens2, Baoshan Zhang1, Yaroslav Tsybovsky2, Barney S Graham1.
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 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.Entities:
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Year: 2022 PMID： 35324257 PMCID： PMC9580340 DOI： 10.1126/science.abn8897
Source DB: PubMed Journal: Science ISSN： 0036-8075 Impact factor: 63.714