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TitleStructural basis for potent antibody neutralization of SARS-CoV-2 variants including B.1.1.529.
Journal, issue, pagesScience, Vol. 376, Issue 6591, Page eabn8897, Year 2022
Publish dateApr 22, 2022
AuthorsTongqing 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 AbstractThe 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 linksScience / PubMed:35324257 / PubMed Central
MethodsEM (single particle)
Resolution2.83 - 5.08 Å
Structure data

25794

7tb8

EMDB-25794, PDB-7tb8:
Cryo-EM structure of SARS-CoV-2 spike in complex with antibodies B1-182.1 and A19-61.1
Method: EM (single particle) / Resolution: 2.83 Å

25797

7tbf

EMDB-25797, PDB-7tbf:
Locally refined region of SARS-CoV-2 spike in complex with antibodies B1-182.1 and A19-61.1
Method: EM (single particle) / Resolution: 3.1 Å

25806

7tc9

EMDB-25806, PDB-7tc9:
Locally refined region of SARS-CoV-2 spike in complex with antibody A19-46.1
Method: EM (single particle) / Resolution: 5.08 Å

25807

7tca

EMDB-25807, PDB-7tca:
Cryo-EM structure of SARS-CoV-2 Omicron spike in complex with antibody A19-46.1
Method: EM (single particle) / Resolution: 3.85 Å

25808

7tcc

EMDB-25808, PDB-7tcc:
Cryo-EM structure of SARS-CoV-2 Omicron spike in complex with antibodies A19-46.1 and B1-182.1
Method: EM (single particle) / Resolution: 3.86 Å

26256

7u0d

EMDB-26256, PDB-7u0d:
Local refinement of cryo-EM structure of the interface of the Omicron RBD in complex with antibodies B-182.1 and A19-46.1
Method: EM (single particle) / Resolution: 4.8 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

Source
  • severe acute respiratory syndrome coronavirus 2
  • homo sapiens (human)
KeywordsVIRAL 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

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