7upl | pdb_00007upl
SARS-Cov2 Omicron varient S protein structure in complex with neutralizing monoclonal antibody 002-S21F2
Structural highlights
Publication Abstract from PubMedIn 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(50) ranging from 0.02 to 0.13 mug/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. Structural insights for neutralization of Omicron variants BA.1, BA.2, BA.4, and BA.5 by a broadly neutralizing SARS-CoV-2 antibody.,Kumar S, Patel A, Lai L, Chakravarthy C, Valanparambil R, Reddy ES, Gottimukkala K, Davis-Gardner ME, Edara VV, Linderman S, Nayak K, Dixit K, Sharma P, Bajpai P, Singh V, Frank F, Cheedarla N, Verkerke HP, Neish AS, Roback JD, Mantus G, Goel PK, Rahi M, Davis CW, Wrammert J, Godbole S, Henry AR, Douek DC, Suthar MS, Ahmed R, Ortlund E, Sharma A, Murali-Krishna K, Chandele A Sci Adv. 2022 Oct 7;8(40):eadd2032. doi: 10.1126/sciadv.add2032. Epub 2022 Oct 5. PMID:36197988[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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