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TitleStructural insights for neutralization of Omicron variants BA.1, BA.2, BA.4, and BA.5 by a broadly neutralizing SARS-CoV-2 antibody.
Journal, issue, pagesSci Adv, Vol. 8, Issue 40, Page eadd2032, Year 2022
Publish dateOct 7, 2022
AuthorsSanjeev Kumar / Anamika Patel / Lilin Lai / Chennareddy Chakravarthy / Rajesh Valanparambil / Elluri Seetharami Reddy / Kamalvishnu Gottimukkala / Meredith E Davis-Gardner / Venkata Viswanadh Edara / Susanne Linderman / Kaustuv Nayak / Kritika Dixit / Pragati Sharma / Prashant Bajpai / Vanshika Singh / Filipp Frank / Narayanaiah Cheedarla / Hans P Verkerke / Andrew S Neish / John D Roback / Grace Mantus / Pawan Kumar Goel / Manju Rahi / Carl W Davis / Jens Wrammert / Sucheta Godbole / Amy R Henry / Daniel C Douek / Mehul S Suthar / Rafi Ahmed / Eric Ortlund / Amit Sharma / Kaja Murali-Krishna / Anmol Chandele /
PubMed AbstractIn this study, by characterizing several human monoclonal antibodies (mAbs) isolated from single B cells of the COVID-19-recovered individuals in India who experienced ancestral Wuhan strain (WA.1) ...In this study, by characterizing several human monoclonal antibodies (mAbs) isolated from single B cells of the COVID-19-recovered individuals in India who experienced ancestral Wuhan strain (WA.1) of SARS-CoV-2 during early stages of the pandemic, we found a receptor binding domain (RBD)-specific mAb 002-S21F2 that has rare gene usage and potently neutralized live viral isolates of SARS-CoV-2 variants including Alpha, Beta, Gamma, Delta, and Omicron sublineages (BA.1, BA.2, BA.2.12.1, BA.4, and BA.5) with IC ranging from 0.02 to 0.13 μg/ml. Structural studies of 002-S21F2 in complex with spike trimers of Omicron and WA.1 showed that it targets a conformationally conserved epitope on the outer face of RBD (class 3 surface) outside the ACE2-binding motif, thereby providing a mechanistic insights for its broad neutralization activity. The discovery of 002-S21F2 and the broadly neutralizing epitope it targets have timely implications for developing a broad range of therapeutic and vaccine interventions against SARS-CoV-2 variants including Omicron sublineages.
External linksSci Adv / PubMed:36197988 / PubMed Central
MethodsEM (single particle)
Resolution3.76 - 4.1 Å
Structure data

26262

7u0p

EMDB-26262, PDB-7u0p:
SARS-Cov2 S protein structure in complex with neutralizing monoclonal antibody 002-S21F2
Method: EM (single particle) / Resolution: 3.76 Å

26669

7upl

EMDB-26669, PDB-7upl:
SARS-Cov2 Omicron varient S protein structure in complex with neutralizing monoclonal antibody 002-S21F2
Method: EM (single particle) / Resolution: 4.1 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • severe acute respiratory syndrome coronavirus 2
  • homo sapiens (human)
KeywordsVIRAL PROTEIN / SARS-Cov2 6P spike protein / immune complex / SARS-Cov2 / 6P / spike protein

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